ID   A0A0C5VNZ6_9GAMM        Unreviewed;       430 AA.
AC   A0A0C5VNZ6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=YC6258_04360 {ECO:0000313|EMBL:AJQ96392.1};
OS   Gynuella sunshinyii YC6258.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Saccharospirillaceae; Gynuella.
OX   NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ96392.1, ECO:0000313|Proteomes:UP000032266};
RN   [1] {ECO:0000313|EMBL:AJQ96392.1, ECO:0000313|Proteomes:UP000032266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC6258 {ECO:0000313|EMBL:AJQ96392.1,
RC   ECO:0000313|Proteomes:UP000032266};
RA   Khan H., Chung E.J., Chung Y.R.;
RT   "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT   YC6258T gen. nov., sp. nov.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP007142; AJQ96392.1; -; Genomic_DNA.
DR   RefSeq; WP_044618403.1; NZ_CP007142.1.
DR   AlphaFoldDB; A0A0C5VNZ6; -.
DR   STRING; 1445510.YC6258_04360; -.
DR   KEGG; gsn:YC6258_04360; -.
DR   PATRIC; fig|1445510.3.peg.4325; -.
DR   HOGENOM; CLU_019532_2_0_6; -.
DR   OrthoDB; 5288740at2; -.
DR   Proteomes; UP000032266; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05658; M18_DAP; 1.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032266};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   430 AA;  47159 MW;  5D4DDBAF2E356DE1 CRC64;
     MSDLLVIQEL LDFLGKSPTP FHAVQQVTEQ LLKAGYVRLD EKQSWQLAPE GKYFTTRNDS
     SLIAFHTGRH DPTEAGIRMM GAHTDSPALK VKPSPVTINK GYLQLAVEVY GGVLLNPWFD
     RDLSLAGRVS YKTNDGILKN ALIDFRTPIA IIPSLAIHLD RTQNESKKIN PQTDLPPILA
     QVSNSENFSF ESLLKDQIND DALAEVLDWE LFFYDTQLPA EVGLNKEFIA SARLDNLLSC
     FIGLQSFINS DASQPALIVF NDHEEVGSAS ASGADGPFLK QVLERWIGDS AETFVQTISR
     SLMISVDNAH GVHPNFASWH EPDHQPILNS GPVIKINANQ RYASNSTSQA LFRHICQQVN
     VPVQVFVVRS DLACGSTIGP ITATNLGVNT VDVGVATFAM HSIRETAGAK DPLLLLKALQ
     HFFNSSSISA
//