Third LRR domain of human Slit2
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Chains | Domain Info | Class | Fold | Superfamily | Family | Domain | Species | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | d2v70a_ | Alpha and beta proteins (a/b) | Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) | L domain-like | automated matches | automated matches | HUMAN (Homo sapiens ) [TaxId: 9606 ], | SCOPe (2.08) |
B | d2v70b_ | Alpha and beta proteins (a/b) | Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) | L domain-like | automated matches | automated matches | HUMAN (Homo sapiens ) [TaxId: 9606 ], | SCOPe (2.08) |
C | d2v70c_ | Alpha and beta proteins (a/b) | Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) | L domain-like | automated matches | automated matches | HUMAN (Homo sapiens ) [TaxId: 9606 ], | SCOPe (2.08) |
D | d2v70d_ | Alpha and beta proteins (a/b) | Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) | L domain-like | automated matches | automated matches | HUMAN (Homo sapiens ) [TaxId: 9606 ], | SCOPe (2.08) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | LRR_8_1 | e2v70A1 | A: beta duplicates or obligate multimers | X: Single-stranded right-handed beta-helix | H: Leucine-rich repeats (From Topology) | T: Leucine-rich repeats | F: LRR_8_1 | ECOD (1.6) |
B | LRR_8_1 | e2v70B1 | A: beta duplicates or obligate multimers | X: Single-stranded right-handed beta-helix | H: Leucine-rich repeats (From Topology) | T: Leucine-rich repeats | F: LRR_8_1 | ECOD (1.6) |
C | LRR_8_1 | e2v70C1 | A: beta duplicates or obligate multimers | X: Single-stranded right-handed beta-helix | H: Leucine-rich repeats (From Topology) | T: Leucine-rich repeats | F: LRR_8_1 | ECOD (1.6) |
D | LRR_8_1 | e2v70D1 | A: beta duplicates or obligate multimers | X: Single-stranded right-handed beta-helix | H: Leucine-rich repeats (From Topology) | T: Leucine-rich repeats | F: LRR_8_1 | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
A | 3.80.10.10 | Alpha Beta | Alpha-Beta Horseshoe | Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) | Ribonuclease Inhibitor | CATH (4.3.0) |
B | 3.80.10.10 | Alpha Beta | Alpha-Beta Horseshoe | Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) | Ribonuclease Inhibitor | CATH (4.3.0) |
C | 3.80.10.10 | Alpha Beta | Alpha-Beta Horseshoe | Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) | Ribonuclease Inhibitor | CATH (4.3.0) |
D | 3.80.10.10 | Alpha Beta | Alpha-Beta Horseshoe | Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) | Ribonuclease Inhibitor | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR018097 | EGF-like calcium-binding, conserved site | Conserved Site | |
IPR013320 | Concanavalin A-like lectin/glucanase domain superfamily | Homologous Superfamily | |
IPR013032 | EGF-like, conserved site | Conserved Site | |
IPR001611 | Leucine-rich repeat | Repeat | |
IPR003645 | Follistatin-like, N-terminal | Domain | |
IPR001881 | EGF-like calcium-binding domain | Domain | |
IPR000483 | Cysteine-rich flanking region, C-terminal | Domain | |
IPR000372 | Leucine-rich repeat N-terminal domain | Domain | |
IPR003591 | Leucine-rich repeat, typical subtype | Repeat | |
IPR000742 | EGF-like domain | Domain | |
IPR051355 | Notch and Slit guidance protein | Family | |
IPR001791 | Laminin G domain | Domain | |
IPR032675 | Leucine-rich repeat domain superfamily | Homologous Superfamily | |
IPR006207 | Cystine knot, C-terminal | Domain | |
IPR000152 | EGF-type aspartate/asparagine hydroxylation site | PTM |