ID   A0A1Y5Y380_KIBAR        Unreviewed;       850 AA.
AC   A0A1Y5Y380;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Zinc carboxypeptidase {ECO:0000313|EMBL:SMD23252.1};
GN   ORFNames=SAMN05661093_07826 {ECO:0000313|EMBL:SMD23252.1};
OS   Kibdelosporangium aridum.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kibdelosporangium.
OX   NCBI_TaxID=2030 {ECO:0000313|EMBL:SMD23252.1, ECO:0000313|Proteomes:UP000192674};
RN   [1] {ECO:0000313|EMBL:SMD23252.1, ECO:0000313|Proteomes:UP000192674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43828 {ECO:0000313|EMBL:SMD23252.1,
RC   ECO:0000313|Proteomes:UP000192674};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   EMBL; FWXV01000009; SMD23252.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5Y380; -.
DR   Proteomes; UP000192674; Unassembled WGS sequence.
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   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:SMD23252.1};
KW   Hydrolase {ECO:0000313|EMBL:SMD23252.1};
KW   Protease {ECO:0000313|EMBL:SMD23252.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192674};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..850
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013209737"
FT   DOMAIN          98..381
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
FT   REGION          27..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   850 AA;  91355 MW;  689684CCB2078871 CRC64;
     MHLRPVGRVL AASALSLLTV ITLAPAAAGA PSRSPKGEEP GNGPERNEVA AVDPPSIGIA
     ARSASGENKL GSREGYPRTT QLRVYPEDPA DKAIKLGLAP YHAIAPKLNE LQGRSNRISV
     EVVGQSGLGR DLYLVTLTAP ERPSETRQQE RWRDKIENDP AAAARDRQLA REYKTPIWIN
     NNIHGDEWEG TDAALRQIEY LATTRDRKAL DLLSRNRVYF NVTANPDGRN LGTRANANGF
     DLNRDFVTSS QPEGIVMRDI VKTVQPVMML DEHGYVPGTL IEPTGPPHGQ NYDFDLYIKH
     GYANGLNIEK AVKALGYPEA QDTQIPFRDY PSGEWDGWAP IYTAQYSMFH GAISYTIEIP
     MRVNRGDYNL PETELRRRSA INTDVSEASM KASLDYVHDN RSALIANQIE MFRRGAAGEA
     QRFIPDGFVP GFGPEDRFTT KFPRAYVIPA GATQRSGAAA ARLVDLLVAH DVRVRQADRP
     FSLAGRTYPA GSYIVDMHQP KRALANVMLE QGRDVSASAE VMYDISGWSH RLLWGASVDI
     VQGGDLRVSS KPVVAASPTG GVDAGPGQDL AITVRDGKDA AAVNDLLGRG IELKRRANGS
     VIVPASARVA ALQVADRYGV RFSLAPAGDT GVVMRRPTIA AAVGPDELFA LRDMGFEVRP
     VSTDALNAGF DLSRVDVLMV SSGLRYDLLN ASAKAAVDAF AARGGVVTRG ATGSKFNADA
     KLLDVTAVAG RGDANGIVNV INGTGPIGAD ALAQSFVYSP QWFTDLGTGV TVEQRYATGN
     PLAAGHWRPN EDGTGGPQAA SGQAVVVSGT DERGAKVVMF GTEPLFRAHP KGMYAQVANA
     VYWSATRNPV
//