ID D4JT92_9FIRM Unreviewed; 487 AA.
AC D4JT92;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=EUS_11230 {ECO:0000313|EMBL:CBK96311.1};
OS [Eubacterium] siraeum 70/3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=657319 {ECO:0000313|EMBL:CBK96311.1, ECO:0000313|Proteomes:UP000008803};
RN [1] {ECO:0000313|EMBL:CBK96311.1, ECO:0000313|Proteomes:UP000008803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70/3 {ECO:0000313|EMBL:CBK96311.1,
RC ECO:0000313|Proteomes:UP000008803};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Eubacterium siraeum 70/3.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK96311.1, ECO:0000313|Proteomes:UP000008803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70/3 {ECO:0000313|EMBL:CBK96311.1,
RC ECO:0000313|Proteomes:UP000008803};
RA Pajon A.;
RL Submitted (MAR-2010) 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}.
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DR EMBL; FP929044; CBK96311.1; -; Genomic_DNA.
DR AlphaFoldDB; D4JT92; -.
DR KEGG; esu:EUS_11230; -.
DR PATRIC; fig|657319.3.peg.1407; -.
DR HOGENOM; CLU_590123_0_0_9; -.
DR BioCyc; ESIR657319:G136K-952-MONOMER; -.
DR Proteomes; UP000008803; Chromosome.
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 487 AA; 53871 MW; D96AB41A84E8A191 CRC64;
MPTILIAGFI KNKGRQRKMA EKKSQAEQLK EKLFYVKKHA TLVMSEQEEK KADKYCEGYK
KFLDAGKTER EAAATAVAMA EKAGFKPFDK KAQYKAGDKI YVLNREKAVI LAVIGKSNIS
NGVNLTAAHI DSPRLDLKQN PLYESDELGY FKTHYYGGIK KYQWPTVPMS LHGVIVRADG
SKVTVRIGED EGDPVFVVTD LLPHLAEEQY KRPATKLIKG EELNILIGSR PFRDDKISEK
VKLNLMNILF EKYGIVEKDF LSAELECVPA FKAKDVGFDR SLVGAYGQDD RVCAYTAFTA
IIDMKAVPEK TAVCVLTDKE ETGSDGNTGL RSAYLKFFLY DLAENMGSDG RTVISATRCL
SADVNAAYDP TFPDGYERNN CSFVNKGIVV TKYTGARGKS GTSDASAEYV GLIHNMLDKN
DVVWQTGELG KVDFGGGGTV AAYIANLNID TIDVGVPVLS MHAPYELTAK NDVYMAYKAF
TAFYKMK
//
