ID A0A091NEV6_9PASS Unreviewed; 440 AA.
AC A0A091NEV6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 8 {ECO:0000313|EMBL:KFP87444.1};
DE Flags: Fragment;
GN ORFNames=N310_01816 {ECO:0000313|EMBL:KFP87444.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP87444.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP87444.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP87444.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; KK845823; KFP87444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091NEV6; -.
DR MEROPS; M12.208; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF20; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 8; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00068}; Integrin {ECO:0000313|EMBL:KFP87444.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000053537};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 127..315
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 315..401
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT ACT_SITE 262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 373..393
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP87444.1"
FT NON_TER 440
FT /evidence="ECO:0000313|EMBL:KFP87444.1"
SQ SEQUENCE 440 AA; 48286 MW; F035F3040572B4A0 CRC64;
RALLGQHYTE THYLADGTEV TEKPDTQDHC FYQGHVRGHS DSAVSISTCG GLRAYLMCDP
SSRLGVSSMQ PETTNFTVEP GDLLALEDTP GSNTGHERVT AWLGKPQAEP HFPLPFQKSA
PLHKGPRYVE LVLVADNEEF RKHKDLRTVQ NRMKEIVNHV DKLYQPLRLR VALIGLEVWS
HKDKIVVSPN PEVTLDNFLH WRESELLRKK PHDNAQLITG IDFHGNTVGL AKKLVMCTRD
SGGVNQDHSM NPIGAASTMA HEMGHNLGMS HDEDVAGCRC PIPKVDGGCV MAGSVGPVYP
KLFSRCSEQD MWQFLGVCGN QFVERGEQCD CGTPEECSDR CCNATTCQLR EGAECARGEC
CQDCKVKAAG VLCRASKNDC DLPEHCSGLS AECPEDVFQE NGISCHNGNG YCYNGACPSH
GEQCRALWGA EAQVAPDVCF
//
