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
//