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Database: UniProt
Entry: A0A091SB28_NESNO
LinkDB: A0A091SB28_NESNO
Original site: A0A091SB28_NESNO 
ID   A0A091SB28_NESNO        Unreviewed;       826 AA.
AC   A0A091SB28;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Disintegrin and metalloproteinase domain-containing protein 9 {ECO:0000313|EMBL:KFQ55768.1};
DE   Flags: Fragment;
GN   ORFNames=N333_11013 {ECO:0000313|EMBL:KFQ55768.1};
OS   Nestor notabilis (Kea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX   NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ55768.1, ECO:0000313|Proteomes:UP000053840};
RN   [1] {ECO:0000313|EMBL:KFQ55768.1, ECO:0000313|Proteomes:UP000053840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ55768.1};
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:PRU00076}.
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DR   EMBL; KK947738; KFQ55768.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091SB28; -.
DR   MEROPS; M12.209; -.
DR   Proteomes; UP000053840; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
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:SF136; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 9; 1.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
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.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Integrin {ECO:0000313|EMBL:KFQ55768.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053840};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   TRANSMEM        662..681
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          178..372
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          380..467
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   DOMAIN          606..640
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          713..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          778..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..807
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        314
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         317
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   DISULFID        331..336
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   DISULFID        439..459
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT   DISULFID        630..639
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ55768.1"
FT   NON_TER         826
FT                   /evidence="ECO:0000313|EMBL:KFQ55768.1"
SQ   SEQUENCE   826 AA;  91891 MW;  12018DAF06CCD231 CRC64;
     QQVSLLSSYE VVIPQRLGRE RREAFNVSSV QDKVSYAIEI EGKEYTIHLE KNKELLPKDF
     TVYTYNKEGK LQSEYPDVQD HCHYQGYVEG SLDSVVALST CSGLRGLVTI GNITYGIEPM
     DSSSGSKHIL YRLDNVRKEP TMCGVTAEDH GREHTEENHH PTMTQLLRMK RAVLHQTRYV
     ELFIVVDKEK FEDFGKSETE VREHMVQLAN FLDSMYIMLN IRIVLVGLEI WKYENIISTD
     GGAGDVLANF VQWREKNLVL RRRHDSAQFV LKKGFGGTAG MAYVGTVCSK SHAGGINVFG
     RISIQMFASI MAHELGHNLG MNHDDERVCH CGASSCIMSS GASGSRNFSS CSAEDFEKLT
     LNKGGSCLLN VPKPDETYSV PYCGNKLVDA GEECDCGSPK ECESDPCCEP GTCRLRSSAA
     CAYGDCCKNC QLLPGGTECR ASSNECDLPE YCNGTSQFCQ PDFTVQNGHP CHNEEAYCYN
     GVCQYYDAQC QDIFGSKAKA APNICFAEVN SKGDRFGNCG FHGHDYKKCS SWNAMCGKLQ
     CENVKTMPVF GIKPAIIQTP IRGTMCWGVD FQLGSDVPDP GMVNEGTKCD TGKICRHFQC
     VSASVLNYDC DVEKQCHGHG VCNNNRNCHC EPGWAPPYCD VKGYGGSVDS GPPYNGKSRN
     GLLVFFFLVL PLLVAAALAF VKRDRLKRCY RRAMSRCHSV TCSLHWLGFR SRPSAPPRTE
     AEPRDHHHHH HQGFSHGMPY APRGAPMDME PNTFPVPSYP VNQHPQQAYH QSYYPPLQYQ
     APQPQKLPTR PPPPQQQRAP QGPPPSQHKC LPQGQYFPSR PAPLPP
//
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