ID   H0R102_9ACTN            Unreviewed;       421 AA.
AC   H0R102;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=GOEFS_063_00270 {ECO:0000313|EMBL:GAB18753.1};
OS   Gordonia effusa NBRC 100432.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB18753.1, ECO:0000313|Proteomes:UP000035034};
RN   [1] {ECO:0000313|EMBL:GAB18753.1, ECO:0000313|Proteomes:UP000035034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB18753.1,
RC   ECO:0000313|Proteomes:UP000035034};
RA   Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA   Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL   Submitted (DEC-2011) 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:GAB18753.1}.
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DR   EMBL; BAEH01000063; GAB18753.1; -; Genomic_DNA.
DR   RefSeq; WP_007318089.1; NZ_BAEH01000063.1.
DR   AlphaFoldDB; H0R102; -.
DR   STRING; 1077974.GOEFS_063_00270; -.
DR   eggNOG; COG1362; Bacteria.
DR   OrthoDB; 5288740at2; -.
DR   Proteomes; UP000035034; 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:UP000035034};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   421 AA;  44862 MW;  5C249CCF1980F534 CRC64;
     MSNNTSATAA GLGAFIDASP SPFHVCATVA SELDTAGYLR LAETDQWPGG CGSFYVIRGG
     SIIAWSSESD EGPFRIIGGH TDSPNLRVKQ HPDKTSAGLS MVGLEPYGGA WLNSWLDRDL
     GLSGRIAYRE GSSVSHKLIH IGEPILRVPQ LAIHLSEDRK GVAPNPQRHV DAIFAVRDAP
     PLLDWVAGQV GVDPREVLGW ELMTHDVSPS RVVGAQSDLL SAPRLDNQGT CYAGLRALLD
     SPETSGVRML ALFDHEEVGS GSERGAASDF LSTVCERIVL SRGGSRDDYL QTMAASVCVS
     GDMAHATHPN YPERHEPAHQ IAINGGPVLK VNQNLRYASD ALGEAVFAIA CDRAGVPLQR
     YVHRADLPCG STIGPITATR TGLRTVDVGA PQLAMHSARE LMGVDDVWMY SAALQAFLLG
     S
//