ID A0A094K1X0_ANTCR Unreviewed; 443 AA.
AC A0A094K1X0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
DE Flags: Fragment;
GN ORFNames=N321_05356 {ECO:0000313|EMBL:KFZ49765.1};
OS Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC Caprimulgidae; Antrostomus.
OX NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ49765.1, ECO:0000313|Proteomes:UP000053620};
RN [1] {ECO:0000313|EMBL:KFZ49765.1, ECO:0000313|Proteomes:UP000053620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ49765.1};
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|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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL335794; KFZ49765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094K1X0; -.
DR Proteomes; UP000053620; 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:SF780; 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:UP000053620};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT DOMAIN 19..216
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 218..330
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 332..443
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT ACT_SITE 116
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 23..26
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFZ49765.1"
FT NON_TER 443
FT /evidence="ECO:0000313|EMBL:KFZ49765.1"
SQ SEQUENCE 443 AA; 49266 MW; 8350513EF79EC680 CRC64;
GSEIAVYEGD ILLRRGRRSA INCESCLWPK SQDGLVKVPI NISSDFSVTE RSWIADALQE
ISTLTCVQFV NRTTETDYVY VERGQSCWSY FGKIGGRQAV GLMKNGCMDK GAIQHEMNHA
LGFIHEQARS DRDRFVKIMW EHIVAGEQGN FGKVKSKNLG LPYDYSSVMH YGAYDFSSTP
GKPTIVPVPD PSIPIGQREG LSNLDVAKIN KLYKCNCCSS VLPKSKGSFS SVNYPSPYPN
NSNCLWLIRI HRSKIFLQFE AFDLQPSSDC SSDYIKIYNG NSKNSPVLLD KYCGKGPLPS
LVTSGSTMLV EFASDGSVTA TGFRASYNRV NCGDTFTDSR GVITSPNYPN KYPKNRACFW
VISSPVGYKI SLKMLSFELE DSDRCIYDYL LIHDGSRPTS PAVGPYCGTE EVADFTSTGN
FVLVEFHSDL VWELPGFVMS YTF
//
