ID A0A0M9YLW8_9ACTN Unreviewed; 435 AA.
AC A0A0M9YLW8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=ADK55_17275 {ECO:0000313|EMBL:KOU52216.1};
OS Streptomyces sp. WM4235.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415551 {ECO:0000313|EMBL:KOU52216.1, ECO:0000313|Proteomes:UP000037699};
RN [1] {ECO:0000313|EMBL:KOU52216.1, ECO:0000313|Proteomes:UP000037699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM4235 {ECO:0000313|EMBL:KOU52216.1,
RC ECO:0000313|Proteomes:UP000037699};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOU52216.1}.
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DR EMBL; LGDE01000226; KOU52216.1; -; Genomic_DNA.
DR RefSeq; WP_053679659.1; NZ_LGDE01000226.1.
DR AlphaFoldDB; A0A0M9YLW8; -.
DR PATRIC; fig|1415551.3.peg.3771; -.
DR OrthoDB; 5288740at2; -.
DR Proteomes; UP000037699; 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:UP000037699};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 435 AA; 46331 MW; C211856CC21891DC CRC64;
MTLVNDPSHA EDLLAFLKDS SSPYHAVAES ARRLEKAGFT ELSETEEWTG GTGGRFITRA
GALIAWYVPE GAPAHTPFRI IGAHTDSPNL RVKPTPDTSS AGWRQIAVEV YGGVPLNTWL
DRDLGISGRI SLRDGGSALV KIDEPLFRVP QLAIHLDRSV NDGLALDRQR QTQPIWALGA
SEPGALLRRI ARAADRDPDQ ILGWDLMLHD IQPPGHLGEE SEFLVSSRLD NLVSVHAGVT
ALTAAAEAYA RNTVPAEGPR IPVLAAFDHE ECGSGSETGA RSPLLERILN RSVSGRGGGG
EDWSRAIAGS FCVSSDMAHA VHPNYSERHD PDNHPLPNGG PVVKVNVNQR YATDGTGFAA
FAAACERADV PWQRFVSNNA MACGTSIGPL TAAQLGVTTV DVGIPGLSMH SARELVGAQD
PGYLTRALAE FVTTG
//
