ID A0A1J8Q0L4_9GAMM Unreviewed; 438 AA.
AC A0A1J8Q0L4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=QHL1GM_07235 {ECO:0000313|EMBL:OJA05196.1};
OS Halomonas sp. QHL1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1123773 {ECO:0000313|EMBL:OJA05196.1, ECO:0000313|Proteomes:UP000183854};
RN [1] {ECO:0000313|EMBL:OJA05196.1, ECO:0000313|Proteomes:UP000183854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QHL1 {ECO:0000313|EMBL:OJA05196.1,
RC ECO:0000313|Proteomes:UP000183854};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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:OJA05196.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MINL01000001; OJA05196.1; -; Genomic_DNA.
DR RefSeq; WP_071693873.1; NZ_MINL01000001.1.
DR AlphaFoldDB; A0A1J8Q0L4; -.
DR OrthoDB; 5288740at2; -.
DR Proteomes; UP000183854; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 438 AA; 47658 MW; BC245CCE9FF22822 CRC64;
MSETFNADRL TRLCDFLRQS PTPWHAAGNM ASRLEQAGFQ RLEEKANWQL TPGKRYYVTR
NDSAIIAFQL PESELTALRM IGAHTDSPGL HLKPNATQCS AGWLQLGVQV YGGVLLAPWF
DRDLGLAGRV HVRHADGRLE SVLLNIDRAI AMVPSLAIHL DRDVNSGRPI NPQTQMAPVL
MQSESATLGE LVAQWLEEQH GMRAVEVVDF ELGFYDVQPP SLVGVKKELV ASARLDNLLS
CFIGLEALLD CDGSQGALLV ANDHEEVGSA SACGAQGPFL ADVLKRINAQ VGKGREKRSD
ESLIQLIQSS LMISCDNAHA LHPNFRDKHD ERHGPAINGG PVIKVNSSQR YATNSVTGAL
FRDVCREADV PVQSFVTRAD MGCGSTIGPI TATELGVPTI DVGVPQWAMH SIRETAGSKD
VEYLTRALVG FLNRAKLS
//
