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Database: UniProt
Entry: A0A3L8SXZ1_CHLGU
LinkDB: A0A3L8SXZ1_CHLGU
Original site: A0A3L8SXZ1_CHLGU 
ID   A0A3L8SXZ1_CHLGU        Unreviewed;       513 AA.
AC   A0A3L8SXZ1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   22-FEB-2023, entry version 14.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN   ORFNames=DV515_00002314 {ECO:0000313|EMBL:RLW10382.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW10382.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLW10382.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLW10382.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLW10382.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC         ECO:0000256|RuleBase:RU361183};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLW10382.1}.
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DR   EMBL; QUSF01000004; RLW10382.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8SXZ1; -.
DR   STRING; 44316.ENSEGOP00005001502; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd04283; ZnMc_hatching_enzyme; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR017370; Hatching_enzyme_Uvs2-like.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR034039; ZnMP_hatching_enz.
DR   PANTHER; PTHR10127:SF872; ASTACIN-LIKE METALLOENDOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00431; CUB; 2.
DR   PIRSF; PIRSF038057; Hatching_enzyme_Uvs2; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS01180; CUB; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU01211};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT   DOMAIN          87..284
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   DOMAIN          286..398
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          400..512
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   ACT_SITE        184
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         193
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   DISULFID        91..94
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   513 AA;  57316 MW;  6FCA6D25DBEFCA03 CRC64;
     MLVNNSSSFP IKLAPSKLTT ILRTELQSKE VHLGNLKMKY FLLPTHLAFL CSFAFSKPVQ
     IATRKNDLGS EITVYEGDIL LRRGRRSAIN CESCLWPKSQ DGLVKVPVNI SSDFSITERS
     WIADALQEIS TLTCVQFVNR TTETDYVYVE RGQSCWSYFG KIGGRQAVGL VKNGCMDKGA
     IQHEMNHALG FIHEQARSDR DRFVKIMWEH IVAGEQGNFG KINSKNLGLP YDYSSVMHYG
     AYDFSSTPGK PTIVPVPDPS IPIGQREGLS NLDVAKINKL YKCNCCSSVL PKPKGSFSSV
     NYPSPYPNNS NCLWLIRIRR SKIFLQFEAF DLQYSSDCSS DYIKIYNGNS KSSPVLLDKY
     CGKGPLPSLV ASGSTVLVEF ASDESITATG FRASYNRVNC GATFRDSKGV ITSPNYPNKY
     PKNRACFWVI TSPVGYKISL KMLSFELEYS DRCIFDYLLI HDGSRPMSPA VGPYCGTEKV
     ADFTSTGNFV LVEFHSDLVW ELPGFVMSYT FAR
//
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