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Database: UniProt
Entry: W1NC49_9GAMM
LinkDB: W1NC49_9GAMM
Original site: W1NC49_9GAMM 
ID   W1NC49_9GAMM            Unreviewed;       442 AA.
AC   W1NC49;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=BJB45_17425 {ECO:0000313|EMBL:ERL53058.1};
OS   Halomonas huangheensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1178482 {ECO:0000313|EMBL:ERL53058.1, ECO:0000313|Proteomes:UP000019113};
RN   [1] {ECO:0000313|EMBL:ERL53058.1, ECO:0000313|Proteomes:UP000019113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BJGMM-B45 {ECO:0000313|EMBL:ERL53058.1,
RC   ECO:0000313|Proteomes:UP000019113};
RA   Miao C., Wan Y., Jin W.;
RT   "draft genome of Halomonas huanghegensis, strain BJGMM-B45T.";
RL   Submitted (AUG-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERL53058.1}.
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DR   EMBL; AVBC01000011; ERL53058.1; -; Genomic_DNA.
DR   RefSeq; WP_021817040.1; NZ_CP013106.1.
DR   AlphaFoldDB; W1NC49; -.
DR   KEGG; hhu:AR456_12485; -.
DR   PATRIC; fig|1178482.3.peg.97; -.
DR   eggNOG; COG1362; Bacteria.
DR   OrthoDB; 5288740at2; -.
DR   Proteomes; UP000019113; Unassembled WGS sequence.
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:UP000019113};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   442 AA;  48018 MW;  C08E50799D72BEAA CRC64;
     MSQECLPKDD STQGARLDRL REFLHRSPTP WHATATMARR LEAAGYRCLD ETDSWSLKPG
     DRFYVTRNDS AIIAVSLPAS PLTELRMVGA HTDSPCLRLK TNAAQTSAGW LQLGVQVYGG
     ALLAPWFDRD LGLSGRVHVR HPDGRLEGLL INVEQPVAII PSLAIHLDRE ANEGRAMNAQ
     TQMAPVFLQG GEAEDLERLL KDWVKEQHGL DDIRVMDFEL GFHDLQPPSI VGIGGELIAS
     ARLDNLLSCF IGLEAMLEAD GSQGMVLVAN DHEEVGSASA CGAQGPFLGD VLKRINAQLG
     QSGDEGYIRL IQASRMISCD NAHALHPNFR DKHDAQHGPA INGGPVIKVN TSQRYATNSA
     TAAMFRALCE EVEVPVQTFV TRADMGCGST IGPITATEIG VPTLDVGVPQ WAMHSIRETA
     GTRDVEYLTR VLTAFFNCPE LA
//
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