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Database: UniProt
Entry: J4XJX9_9ACTN
LinkDB: J4XJX9_9ACTN
Original site: J4XJX9_9ACTN 
ID   J4XJX9_9ACTN            Unreviewed;       484 AA.
AC   J4XJX9;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   03-MAY-2023, entry version 37.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF1155_0286 {ECO:0000313|EMBL:EJU34876.1};
OS   Slackia sp. CM382.
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Slackia.
OX   NCBI_TaxID=1111137 {ECO:0000313|EMBL:EJU34876.1, ECO:0000313|Proteomes:UP000004399};
RN   [1] {ECO:0000313|EMBL:EJU34876.1, ECO:0000313|Proteomes:UP000004399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM382 {ECO:0000313|EMBL:EJU34876.1,
RC   ECO:0000313|Proteomes:UP000004399};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2012) 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:EJU34876.1}.
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DR   EMBL; ALNO01000005; EJU34876.1; -; Genomic_DNA.
DR   RefSeq; WP_009076997.1; NZ_ALNO01000005.1.
DR   AlphaFoldDB; J4XJX9; -.
DR   PATRIC; fig|1111137.3.peg.450; -.
DR   Proteomes; UP000004399; 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   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:SF2; M18 FAMILY AMINOPEPTIDASE 1-RELATED; 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   484 AA;  52281 MW;  526C54F5E558E301 CRC64;
     MKRTNAWLAY DEAARGEAFD FAERYRMFIS ENKTERECAA TAIDMARAAG YISLDEALER
     GSLKPGDKVY AANYGKSVLL AHIGARPLSE GLNILGAHID SPRLDVKQNP LYEASELALL
     DTHYYGGIKK YQWVTIPLAI HGVIAKKDGS VERVDVGEDA GDPVFCVTDL LIHLSQEQLQ
     KNAAKVIDGE ALDVLVGGRP AKKGEIEDVP ASKADAAGED EEDETLAKLA EKEPVKAFLL
     DLLAQKYSME EEDFLSSELE VVPAGAARDL GFDRSMILGY GHDDRSCSFP SLVAQLEAED
     LERTGVCLLV DKEEIGSVGA TGMTSLFFEN TMAEILALAG EPGDLALRRC LARSSMLSSD
     VSAGFDPTYA SAFEEKNAAF LGRGVVFNKF TGSRGKAGSN DANAEYMARI RAVMEKGGAA
     FQTAELGKVD VGGGGTIAYI LAQYGMEVID CGVPVLNMHA PWEVVDKADL YEALKGYRAF
     LKWA
//
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