4DDN

Structure analysis of a wound-inducible lectin ipomoelin from sweet potato

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4ddna_	All beta proteins	beta-Prism I	Mannose-binding lectins	automated matches	automated matches	batate (Ipomoea batatas ) [TaxId: 4120 ],	SCOPe (2.08)
B	d4ddnb_	All beta proteins	beta-Prism I	Mannose-binding lectins	automated matches	automated matches	batate (Ipomoea batatas ) [TaxId: 4120 ],	SCOPe (2.08)
D	d4ddnd_	All beta proteins	beta-Prism I	Mannose-binding lectins	automated matches	automated matches	batate (Ipomoea batatas ) [TaxId: 4120 ],	SCOPe (2.08)
C	d4ddnc_	All beta proteins	beta-Prism I	Mannose-binding lectins	automated matches	automated matches	batate (Ipomoea batatas ) [TaxId: 4120 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Mannose-binding lectins	8083692	3001715	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Mannose-binding lectins	8083692	3001715	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Mannose-binding lectins	8083692	3001715	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Mannose-binding lectins	8083692	3001715	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	Jacalin	e4ddnA1	A: beta duplicates or obligate multimers	X: beta-Prism I (From Topology)	H: beta-Prism I (From Topology)	T: beta-Prism I	F: Jacalin	ECOD (1.6)
B	Jacalin	e4ddnB1	A: beta duplicates or obligate multimers	X: beta-Prism I (From Topology)	H: beta-Prism I (From Topology)	T: beta-Prism I	F: Jacalin	ECOD (1.6)
D	Jacalin	e4ddnD1	A: beta duplicates or obligate multimers	X: beta-Prism I (From Topology)	H: beta-Prism I (From Topology)	T: beta-Prism I	F: Jacalin	ECOD (1.6)
C	Jacalin	e4ddnC1	A: beta duplicates or obligate multimers	X: beta-Prism I (From Topology)	H: beta-Prism I (From Topology)	T: beta-Prism I	F: Jacalin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.100.10.30	Mainly Beta	Aligned Prism	Vitelline Membrane Outer Layer Protein I, subunit A	Jacalin-like lectin domain	CATH (4.3.0)
B	2.100.10.30	Mainly Beta	Aligned Prism	Vitelline Membrane Outer Layer Protein I, subunit A	Jacalin-like lectin domain	CATH (4.3.0)
D	2.100.10.30	Mainly Beta	Aligned Prism	Vitelline Membrane Outer Layer Protein I, subunit A	Jacalin-like lectin domain	CATH (4.3.0)
C	2.100.10.30	Mainly Beta	Aligned Prism	Vitelline Membrane Outer Layer Protein I, subunit A	Jacalin-like lectin domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF01419	Jacalin-like lectin domain (Jacalin)	Jacalin-like lectin domain	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Ipomoelin	binding carbohydrate binding	protein-containing complex organization protein homotetramerization cellular component organization cellular component biogenesis cellular component assembly protein complex oligomerization protein tetramerization protein-containing complex assembly protein homooligomerization cellular process cellular component organization or biogenesis cellular response to stimulus positive regulation of cell communication regulation of cellular process protein-containing complex organization protein homotetramerization cellular component organization cellular component biogenesis cellular component assembly protein complex oligomerization protein tetramerization protein-containing complex assembly protein homooligomerization cellular process cellular component organization or biogenesis cellular response to stimulus positive regulation of cell communication regulation of cellular process positive regulation of signal transduction response to stimulus signaling regulation of cellular response to stress positive regulation of biological process regulation of signal transduction intracellular signal transduction cell communication positive regulation of response to stimulus stress-activated MAPK cascade cellular response to stress regulation of intracellular signal transduction response to stress regulation of response to stress intracellular signaling cassette signal transduction positive regulation of stress-activated protein kinase signaling cascade positive regulation of cellular process regulation of biological process regulation of signaling positive regulation of stress-activated MAPK cascade positive regulation of MAPK cascade biological regulation regulation of stress-activated protein kinase signaling cascade positive regulation of intracellular signal transduction 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 positive regulation of signaling defense response to insect biological process involved in interspecies interaction between organisms response to other organism defense response defense response to other organism response to external stimulus response to external biotic stimulus response to biotic stimulus response to wounding	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR036404	Jacalin-like lectin domain superfamily	Homologous Superfamily
A, B, C, D	IPR033734	Jacalin-like lectin domain, plant	Domain
A, B, C, D	IPR001229	Jacalin-like lectin domain	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.