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}.
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; 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
//