ID A0A0A0B291_CHAVO Unreviewed; 620 AA.
AC A0A0A0B291;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE SubName: Full=Inactive carboxypeptidase-like X2 {ECO:0000313|EMBL:KGL99440.1};
DE Flags: Fragment;
GN ORFNames=N301_09453 {ECO:0000313|EMBL:KGL99440.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL99440.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL99440.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL99440.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; KL873581; KGL99440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0B291; -.
DR STRING; 50402.A0A0A0B291; -.
DR MEROPS; M14.955; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd03869; M14_CPX_like; 1.
DR CDD; cd11308; Peptidase_M14NE-CP-C_like; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF45; INACTIVE CARBOXYPEPTIDASE-LIKE PROTEIN X2; 1.
DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KGL99440.1};
KW Hydrolase {ECO:0000313|EMBL:KGL99440.1};
KW Protease {ECO:0000313|EMBL:KGL99440.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858}.
FT DOMAIN 1..158
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL99440.1"
FT NON_TER 620
FT /evidence="ECO:0000313|EMBL:KGL99440.1"
SQ SEQUENCE 620 AA; 70924 MW; 6A7592DA380C3093 CRC64;
CPPLGLETLK ITDFQLHAST AKRYGLGAHR GRLNIQAGVN ENDFYDGAWC AGRNDPYQWI
EVDARRLTKF TGVITQGRNS LWSSNWVTSY RVLVSNDSHA WTAVRNESGD VIFEGNSEKE
IPVLNMLPVP LVARYIRINP RSWFEEGSIC MRLEILGCPL PDPNNYYHRR NEMTTTDNLD
FKHHNYKEMR QLMKTVNKMC PNITRIYNIG KSNQGLKLYA VEISDNPGEH EVGEPEFRYI
AGAHGNEVLG RELILLLMQF MCQEYLAGNP RIVHLIEDTR IHLLPSVNPD GYDKAYKAGS
ELGGWSLGRW TQDGIDINNN FPDLNSLLWE SEDQKKSKRK VPNHHIPIPD WYLSENATVA
VETRAIIAWM EKIPFVLGGN LQGGELVVAY PYDMVRSMWK TQDYTPTPDD HVFRWLAYSY
ASTHRLMTDA RRRACHTEDF QKEDGTVNGA SWHTVAGSIN DFSYLHTNCF ELSIYVGCDK
YPHESELPEE WENNRESLIV FMEQVHRGIK GIVKDVHGKG IPNAVISVEG VNHDIRTGAD
GDYWRLLNPG EYVVGVKAEG YTAATKTCEV GYDMGATRCD FTISKTNLAR IKEIMKKFGK
QPISLSMRRL RQRARQWRQQ
//
