ID A0A093BNT3_9AVES Unreviewed; 1748 AA.
AC A0A093BNT3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 9 {ECO:0000313|EMBL:KFV05430.1};
DE Flags: Fragment;
GN ORFNames=N339_03660 {ECO:0000313|EMBL:KFV05430.1};
OS Pterocles gutturalis (yellow-throated sandgrouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; Pterocles.
OX NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV05430.1, ECO:0000313|Proteomes:UP000053149};
RN [1] {ECO:0000313|EMBL:KFV05430.1, ECO:0000313|Proteomes:UP000053149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV05430.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
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; KL230575; KFV05430.1; -; Genomic_DNA.
DR MEROPS; M12.021; -.
DR Proteomes; UP000053149; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 12.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR012314; Pept_M12B_GON-ADAMTSs.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF33; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 9; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF08685; GON; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 12.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 14.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 13.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS51046; GON; 1.
DR PROSITE; PS50092; TSP1; 13.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Integrin {ECO:0000313|EMBL:KFV05430.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR613273-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053149};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT DOMAIN 101..309
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1549..1748
FT /note="GON"
FT /evidence="ECO:0000259|PROSITE:PS51046"
FT REGION 23..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1338..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 245
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 176..228
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 204..210
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 222..304
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 260..288
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 331..353
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 342..363
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 348..382
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 376..387
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 410..447
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 414..452
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 425..437
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV05430.1"
FT NON_TER 1748
FT /evidence="ECO:0000313|EMBL:KFV05430.1"
SQ SEQUENCE 1748 AA; 195613 MW; 94F226F5C3FA33D8 CRC64;
LGTFKSDDGD YFVEPLLSLE EQEYEEEHNK PHLVYRHRTP PNNSSGDRQT CDTPENSMLS
DVEMLKHSLE VNSFSADGNK TGNVSEKKSH RRTKRFLSYP RFVEVMVVAD SRMVAYHGAN
LQHYVLTLMS IVASIYKDPS IGNLINIVIV KLVVIHNEQD GPAISYNAQT TLKNFCQWQQ
SQNHPEGSHL RHDTAVLVTR QDICRAHDKC DTLGLAELGT VCDPYRSCSI SEDNGLSTAF
TIAHELGHVF NMPHDDNHKC KEDGGKNQQH VMAPTLNFYT NPWMWSKCSR KYITEFLDTG
YGECLLDEPT SRTYTLPQQL PGLIYDVNKQ CELIFGPGSQ VCPYMMQCRR LWCINIDGAH
KGCRTQHTPW ADGTECEPGK HCRFGMCVPK EREAPVTDGA WGTWSPFGTC SRTCGGGIKT
AIRECNRPEP KNGGKYCVGR RMKFKSCNTE PCSKLKKDFR DEQCADFDGK HFNINGLPTN
VRWVPKYSGI LMKDRCKLFC RVAGNTAYYQ LRDRVIDGTP CGPDTNDICV QGLCRQAGCD
HVLNSKARRD KCGVCGGDNS SCKTVAGTFN TVHYGYNVVV RIPAGATNID VRQHSYSGKP
EDDNYLALSN SQGDFILNGD FVVSMFKREI KVGNAVIEYS GSDNTIERIN STDRIEQEIT
LQVLSVGNLY NPDVRYTFNI PIEDKPQQFY WNAYGPWQPC SKLCQGERKR KPVCTRESDQ
LTVSDQRCDR LPQPDPITEP CGTECELRWH IARKSECTAQ CGLGYRTLEI YCSKYSRLEG
KIEKVDDRFC SSQPKPSTRE KCTGDCNVGG WRYSAWTECS KSCGGGTRRR RAMCVNTYND
ILDDSKCSQQ EKLTVQRCSD FSCPQWKTGD WSECLVTCGK GHKHRQTWCQ FGEDRLNDRF
CDPETKPESV QTCQQQECAS WQVGPWGQCT MTCGQGYQMR AVKCVVGTYM SVVDDNECNA
ATRPTDTQDC EIAACPPHPN SPEAKRSISG IHRTQWRFGS WTPCSATCGK GTRMRYVSCR
DDQGSVADES ACFHLPKPSA TEMCTVTPCG QWKALEWSSC SVTCGQGKAT RQVICINYSD
QLVDRSECDP EDLPATEQDC SMSPCHPNSH DYGRPIHPFL YPDHRLKLHP GGSPNRNRAH
IPGGNQWRIG PWGACSSTCA GGFQRRVVVC QDENGYTANN CDEKSKPMEQ RSCESGPCPQ
WAYGNWGECT KPCGAGTRTR LVVCQRPNGE RFTDLSCEIL DKPPDREQCN VQDCPRDAAW
SAGPWSSCSV SCGRGQKHRD VYCLSKEGRH IEEDYCKHLA KPNVQKKCRG GRCPKWKAGD
WGQSGCNICP RGLQQGQGFT PGTQQSESTT LHRATRPPPQ RDCHLPECPT HHWAAGEWQA
CMKTCGEASR YRKVVCVDEN KRVQNSGYCD ASKRPPEIES CGLPPCEYIW ITGEWSECSV
TCGKGYKQRL VSCSEIYTGK DHYEYGYQNT VNCPGTQPPN IQPCYLGECP VSASWRVGNW
GSCSVTCGVG VMHRSVQCLT NEDQLSSLCH ADLKPEERRT CHNVHDCELP RSCKDVKNLK
GVTEDGEYFL QVKGKMLKVY CSGMQTDSPK EYVTLVNGDE ENFSEVYGYR LHNPTECPYN
GSRREDCQCR KDYTAAGFST FSKVRLDLNT MQIITTDLQF ARTHDGRPVP YATAGDCYSA
AKCPQGRFSI DLYGTGLSLT GTAKWLSQGN YAVSEIQKSP DGTKVVGKCG GYCGKCTPSS
GTGLDVQV
//
