7LJ1

Human Prx1-Srx Decameric Complex

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d7lj1a_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C [auth B]	d7lj1b_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D [auth C]	d7lj1c_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F [auth E]	d7lj1e_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
G [auth F]	d7lj1f_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
H [auth G]	d7lj1g_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
I [auth H]	d7lj1h_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
J [auth I]	d7lj1i_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
K [auth J]	d7lj1j_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
M [auth L]	d7lj1l_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
N [auth M]	d7lj1m_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
O [auth N]	d7lj1n_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
P [auth O]	d7lj1o_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
Q [auth P]	d7lj1p_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
R [auth Q]	d7lj1q_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
S [auth R]	d7lj1r_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
T [auth S]	d7lj1s_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
U [auth T]	d7lj1t_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E [auth D]	d7lj1d_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
L [auth K]	d7lj1k_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
AA [auth g]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
B [auth a]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
BA [auth h]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
CA [auth i]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
DA [auth j]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
EA [auth k]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
FA [auth l]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
GA [auth m]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
HA [auth n]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
IA [auth o]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
JA [auth p]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
KA [auth q]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
LA [auth r]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
MA [auth s]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
NA [auth t]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
V [auth b]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
W [auth c]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
X [auth d]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
Y [auth e]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)
Z [auth f]	SCOP2B Superfamily	ParB/Sulfiredoxin	8033419	3001301	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	AhpC-TSA_1	e7lj1A1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
C [auth B]	AhpC-TSA_1	e7lj1B1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
D [auth C]	AhpC-TSA_1	e7lj1C1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
F [auth E]	AhpC-TSA_1	e7lj1E1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
G [auth F]	AhpC-TSA_1	e7lj1F1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
H [auth G]	AhpC-TSA_1	e7lj1G1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
I [auth H]	AhpC-TSA_1	e7lj1H1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
J [auth I]	AhpC-TSA_1	e7lj1I1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
K [auth J]	AhpC-TSA_1	e7lj1J1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
M [auth L]	AhpC-TSA_1	e7lj1L1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
N [auth M]	AhpC-TSA_1	e7lj1M1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
O [auth N]	AhpC-TSA_1	e7lj1N1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
P [auth O]	AhpC-TSA_1	e7lj1O1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
Q [auth P]	AhpC-TSA_1	e7lj1P1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
R [auth Q]	AhpC-TSA_1	e7lj1Q1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
S [auth R]	AhpC-TSA_1	e7lj1R1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
T [auth S]	AhpC-TSA_1	e7lj1S1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
U [auth T]	AhpC-TSA_1	e7lj1T1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
E [auth D]	AhpC-TSA_1	e7lj1D1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
L [auth K]	AhpC-TSA_1	e7lj1K1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
AA [auth g]	ParBc	e7lj1g1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
B [auth a]	ParBc	e7lj1a1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
BA [auth h]	ParBc	e7lj1h1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
CA [auth i]	ParBc	e7lj1i1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
DA [auth j]	ParBc	e7lj1j1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
EA [auth k]	ParBc	e7lj1k1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
FA [auth l]	ParBc	e7lj1l1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
GA [auth m]	ParBc	e7lj1m1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
HA [auth n]	ParBc	e7lj1n1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
IA [auth o]	ParBc	e7lj1o1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
JA [auth p]	ParBc	e7lj1p1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
KA [auth q]	ParBc	e7lj1q1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
LA [auth r]	ParBc	e7lj1r1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
MA [auth s]	ParBc	e7lj1s1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
NA [auth t]	ParBc	e7lj1t1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
V [auth b]	ParBc	e7lj1b1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
W [auth c]	ParBc	e7lj1c1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
X [auth d]	ParBc	e7lj1d1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
Y [auth e]	ParBc	e7lj1e1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
Z [auth f]	ParBc	e7lj1f1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
C [auth B]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
D [auth C]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
F [auth E]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
G [auth F]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
H [auth G]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
I [auth H]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
J [auth I]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
K [auth J]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
M [auth L]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
N [auth M]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
O [auth N]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
P [auth O]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
Q [auth P]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
R [auth Q]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
S [auth R]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
T [auth S]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
U [auth T]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
E [auth D]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)
L [auth K]	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], I [auth H], J [auth I], K [auth J], L [auth K], M [auth L], N [auth M], O [auth N], P [auth O], Q [auth P], R [auth Q], S [auth R], T [auth S], U [auth T]	PF00578	AhpC/TSA family (AhpC-TSA)	AhpC/TSA family	This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).	Domain
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], I [auth H], J [auth I], K [auth J], L [auth K], M [auth L], N [auth M], O [auth N], P [auth O], Q [auth P], R [auth Q], S [auth R], T [auth S], U [auth T]	PF10417	C-terminal domain of 1-Cys peroxiredoxin (1-cysPrx_C)	C-terminal domain of 1-Cys peroxiredoxin	This is the C-terminal domain of 1-Cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding al ...	This is the C-terminal domain of 1-Cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding alcohols [1]. The C-terminal domain is crucial for providing the extra cysteine necessary for dimerisation of the whole molecule. Loss of the enzyme's peroxidase activity is associated with oxidation of the catalytic cysteine, upstream of this domain; and glutathionylation, presumably through its disruption of protein structure, facilitates access for GSH, resulting in spontaneous reduction of the mixed disulfide to the sulfhydryl and consequent activation of the enzyme [2]. The domain is associated with family AhpC-TSA, Pfam:PF00578, which carries the catalytic cysteine.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], I [auth H], J [auth I], K [auth J], L [auth K], M [auth L], N [auth M], O [auth N], P [auth O], Q [auth P], R [auth Q], S [auth R], T [auth S], U [auth T]	Peroxiredoxin-1	peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor catalytic activity RNA binding binding organic cyclic compound binding nucleic acid binding thioredoxin-dependent peroxiredoxin activity thioredoxin peroxidase activity peroxiredoxin activity cell adhesion molecule binding cadherin binding peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor catalytic activity RNA binding binding organic cyclic compound binding nucleic acid binding thioredoxin-dependent peroxiredoxin activity thioredoxin peroxidase activity peroxiredoxin activity cell adhesion molecule binding cadherin binding protein binding identical protein binding	catabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process cellular process hydrogen peroxide catabolic process cellular response to stimulus regulation of biological process regulation of cellular process response to stimulus signaling biological regulation canonical NF-kappaB signal transduction intracellular signal transduction catabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process cellular process hydrogen peroxide catabolic process cellular response to stimulus regulation of biological process regulation of cellular process response to stimulus signaling biological regulation canonical NF-kappaB signal transduction intracellular signal transduction cell communication intracellular signaling cassette signal transduction cellular response to oxidative stress detoxification cellular response to chemical stress response to superoxide cellular oxidant detoxification cellular response to oxygen radical cellular response to reactive oxygen species cellular response to stress response to stress cellular detoxification response to oxygen-containing compound cellular response to oxygen-containing compound response to reactive oxygen species response to toxic substance removal of superoxide radicals superoxide metabolic process response to oxidative stress cellular response to chemical stimulus response to chemical cellular response to superoxide cellular response to toxic substance response to oxygen radical multicellular organismal process immune system process cell activation leukocyte activation developmental process multicellular organism development skeletal system development anatomical structure development system development cell population proliferation multicellular organismal-level homeostasis homeostatic process homeostasis of number of cells myeloid cell homeostasis erythrocyte homeostasis regulation of cellular response to stress regulation of signal transduction stress-activated MAPK cascade regulation of intracellular signal transduction regulation of response to stress regulation of signaling regulation of stress-activated protein kinase signaling cascade regulation of MAPK cascade regulation of stress-activated MAPK cascade stress-activated protein kinase signaling cascade regulation of response to stimulus MAPK cascade regulation of cell communication non-canonical NF-kappaB signal transduction regulation of non-canonical NF-kappaB signal transduction lymphocyte mediated immunity biological process involved in interspecies interaction between organisms immune response response to other organism defense response defense response to symbiont response to external stimulus leukocyte mediated cytotoxicity response to biotic stimulus immune effector process defense response to other organism natural killer cell mediated cytotoxicity innate immune response leukocyte mediated immunity response to external biotic stimulus natural killer cell mediated immunity cell killing fibroblast proliferation natural killer cell activation lymphocyte activation cell redox homeostasis cellular homeostasis	membrane-bounded organelle intracellular anatomical structure pigment granule intracellular vesicle intracellular membrane-bounded organelle intracellular organelle melanosome cellular anatomical structure cytoplasmic vesicle organelle cytoplasm vesicle extracellular exosome extracellular vesicle membrane-bounded organelle intracellular anatomical structure pigment granule intracellular vesicle intracellular membrane-bounded organelle intracellular organelle melanosome cellular anatomical structure cytoplasmic vesicle organelle cytoplasm vesicle extracellular exosome extracellular vesicle extracellular organelle extracellular region extracellular space extracellular membrane-bounded organelle cytosol nucleus
AA [auth g], B [auth a], BA [auth h], CA [auth i], DA [auth j], AA [auth g], B [auth a], BA [auth h], CA [auth i], DA [auth j], EA [auth k], FA [auth l], GA [auth m], HA [auth n], IA [auth o], JA [auth p], KA [auth q], LA [auth r], MA [auth s], NA [auth t], V [auth b], W [auth c], X [auth d], Y [auth e], Z [auth f]	Sulfiredoxin-1	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding oxidoreductase activity, acting on a sulfur group of donors oxidoreductase activity catalytic activity antioxidant activity sulfiredoxin activity	response to oxidative stress response to stimulus response to stress cellular response to stimulus cellular response to chemical stimulus cellular response to stress response to chemical cellular response to oxidative stress cellular process cellular response to chemical stress	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle organelle subcompartment membrane intracellular membrane-bounded organelle endomembrane system endoplasmic reticulum subcompartment intracellular organelle organelle nuclear outer membrane-endoplasmic reticulum membrane network endoplasmic reticulum cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle organelle subcompartment membrane intracellular membrane-bounded organelle endomembrane system endoplasmic reticulum subcompartment intracellular organelle organelle nuclear outer membrane-endoplasmic reticulum membrane network endoplasmic reticulum organelle membrane endoplasmic reticulum membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], I [auth H], J [auth I], K [auth J], L [auth K], M [auth L], N [auth M], O [auth N], P [auth O], Q [auth P], R [auth Q], S [auth R], T [auth S], U [auth T]	IPR019479	Peroxiredoxin, C-terminal	Domain
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], I [auth H], J [auth I], K [auth J], L [auth K], M [auth L], N [auth M], O [auth N], P [auth O], Q [auth P], R [auth Q], S [auth R], T [auth S], U [auth T]	IPR024706	Peroxiredoxin, AhpC-type	Family
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], I [auth H], J [auth I], K [auth J], L [auth K], M [auth L], N [auth M], O [auth N], P [auth O], Q [auth P], R [auth Q], S [auth R], T [auth S], U [auth T]	IPR050217	Thiol-specific antioxidant peroxiredoxin	Family
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], I [auth H], J [auth I], K [auth J], L [auth K], M [auth L], N [auth M], O [auth N], P [auth O], Q [auth P], R [auth Q], S [auth R], T [auth S], U [auth T]	IPR013766	Thioredoxin domain	Domain
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], I [auth H], J [auth I], K [auth J], L [auth K], M [auth L], N [auth M], O [auth N], P [auth O], Q [auth P], R [auth Q], S [auth R], T [auth S], U [auth T]	IPR036249	Thioredoxin-like superfamily	Homologous Superfamily
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], I [auth H], J [auth I], K [auth J], L [auth K], M [auth L], N [auth M], O [auth N], P [auth O], Q [auth P], R [auth Q], S [auth R], T [auth S], U [auth T]	IPR000866	Alkyl hydroperoxide reductase subunit C/ Thiol specific antioxidant	Domain
AA [auth g], B [auth a], BA [auth h], CA [auth i], DA [auth j], AA [auth g], B [auth a], BA [auth h], CA [auth i], DA [auth j], EA [auth k], FA [auth l], GA [auth m], HA [auth n], IA [auth o], JA [auth p], KA [auth q], LA [auth r], MA [auth s], NA [auth t], V [auth b], W [auth c], X [auth d], Y [auth e], Z [auth f]	IPR016692	Sulfiredoxin	Family
AA [auth g], B [auth a], BA [auth h], CA [auth i], DA [auth j], AA [auth g], B [auth a], BA [auth h], CA [auth i], DA [auth j], EA [auth k], FA [auth l], GA [auth m], HA [auth n], IA [auth o], JA [auth p], KA [auth q], LA [auth r], MA [auth s], NA [auth t], V [auth b], W [auth c], X [auth d], Y [auth e], Z [auth f]	IPR036086	ParB/Sulfiredoxin superfamily	Homologous Superfamily
AA [auth g], B [auth a], BA [auth h], CA [auth i], DA [auth j], AA [auth g], B [auth a], BA [auth h], CA [auth i], DA [auth j], EA [auth k], FA [auth l], GA [auth m], HA [auth n], IA [auth o], JA [auth p], KA [auth q], LA [auth r], MA [auth s], NA [auth t], V [auth b], W [auth c], X [auth d], Y [auth e], Z [auth f]	IPR003115	ParB/Sulfiredoxin	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], I [auth H], J [auth I], K [auth J], L [auth K], M [auth L], N [auth M], O [auth N], P [auth O], Q [auth P], R [auth Q], S [auth R], T [auth S], U [auth T]	Pharos: Q06830	schistosomiasis esophageal squamous cell carcinoma non-small cell lung carcinoma asbestosis keloid methylmalonic acidemia with homocystinuria Liver Neoplasms, Experimental pancreatic intraductal papillary-mucinous carcinoma lung benign neoplasm lymphoplasmacytic lymphoma medulloblastoma ovarian cancer plasma cell myeloma chronic obstructive pulmonary disease hepatocellular carcinoma schistosomiasis esophageal squamous cell carcinoma non-small cell lung carcinoma asbestosis keloid methylmalonic acidemia with homocystinuria Liver Neoplasms, Experimental pancreatic intraductal papillary-mucinous carcinoma lung benign neoplasm lymphoplasmacytic lymphoma medulloblastoma ovarian cancer plasma cell myeloma chronic obstructive pulmonary disease hepatocellular carcinoma intestinal schistosomiasis lung cancer pancreatic ductal adenocarcinoma invasive ductal breast carcinoma malignant pancreatic neoplasm
AA [auth g], B [auth a], BA [auth h], CA [auth i], DA [auth j], AA [auth g], B [auth a], BA [auth h], CA [auth i], DA [auth j], EA [auth k], FA [auth l], GA [auth m], HA [auth n], IA [auth o], JA [auth p], KA [auth q], LA [auth r], MA [auth s], NA [auth t], V [auth b], W [auth c], X [auth d], Y [auth e], Z [auth f]	Pharos: Q9BYN0	psoriasis