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Database: UniProt
Entry: A0A091NUM0_APAVI
LinkDB: A0A091NUM0_APAVI
Original site: A0A091NUM0_APAVI 
ID   A0A091NUM0_APAVI        Unreviewed;       538 AA.
AC   A0A091NUM0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Tolloid-like 1 {ECO:0000313|EMBL:KFP92634.1};
DE   Flags: Fragment;
GN   ORFNames=N311_01970 {ECO:0000313|EMBL:KFP92634.1};
OS   Apaloderma vittatum (Bar-tailed trogon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX   NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP92634.1, ECO:0000313|Proteomes:UP000054244};
RN   [1] {ECO:0000313|EMBL:KFP92634.1, ECO:0000313|Proteomes:UP000054244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP92634.1};
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; KL394010; KFP92634.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091NUM0; -.
DR   Proteomes; UP000054244; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   CDD; cd00041; CUB; 4.
DR   CDD; cd00054; EGF_CA; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 4.
DR   InterPro; IPR015446; BMP_1/tolloid-like.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR24251:SF42; BONE MORPHOGENETIC PROTEIN 1; 1.
DR   PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR   Pfam; PF00431; CUB; 4.
DR   Pfam; PF14670; FXa_inhibition; 2.
DR   PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
DR   SMART; SM00042; CUB; 4.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 4.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01180; CUB; 4.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00023049};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054244};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          2..114
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          115..227
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          227..268
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          271..383
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          383..423
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          427..538
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP92634.1"
FT   NON_TER         538
FT                   /evidence="ECO:0000313|EMBL:KFP92634.1"
SQ   SEQUENCE   538 AA;  60798 MW;  F1D60A91A056DF57 CRC64;
     ACGETLQDST GNFSSPGFPN GYPSYTHCIW RVSVTPGEKI VLNFTTMDLY KSSLCWYDYI
     EVRDGYWRKS PLLGRFCGDK LPEVLASSDS RMWIEFRSSS NWVGKGFAAI YEAICGGEIH
     KNEGQIQSPN YPDDYRPMKE CVWKITVSEN YNVGLTFQAF EIERHDNCAY DYLEIRDGAN
     ENSPLIGHFC GYDKPEDIRS TSNTLWMKFV SDGTVNKAGF AANFFKEEDE CAKPDNGGCE
     QRCVNTLGSY QCACDPGYEL GPDKKSCEAA CGGLLTKLNG TITTPGWPKE YPPNKNCVWQ
     VVAPTQYRIS MKFEFFELEG NEVCKYDYVE IRSGLSSDSK LHGKFCGTEV PEVITSQYNN
     MRIEFRSDNT VSKKGFKAHF FSDKDECSKD NGGCQHECIN TVGSYVCQCR NGFVLHENKH
     DCKEAECEQK IHSPNGIITS PNWPDKYPSR KECTWEISAT PGQRVKLTFN EFEIEQHQEC
     AYDHLEVFDG ESEKSPILGR LCGNKIPDPL IATGNKMFLR FISDASVQRK GFQATHST
//
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