ID A0A2G3E1U5_9FIRM Unreviewed; 479 AA.
AC A0A2G3E1U5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=CSX02_09290 {ECO:0000313|EMBL:PHU37191.1};
OS Agathobacter ruminis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Agathobacter.
OX NCBI_TaxID=1712665 {ECO:0000313|EMBL:PHU37191.1, ECO:0000313|Proteomes:UP000224563};
RN [1] {ECO:0000313|EMBL:PHU37191.1, ECO:0000313|Proteomes:UP000224563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JK623 {ECO:0000313|EMBL:PHU37191.1,
RC ECO:0000313|Proteomes:UP000224563};
RA Sheridan P.O., Walker A.W., Duncan S.H., Scott K.P., Toole P.W.O., Luis P.,
RA Flint H.J.;
RT "Resolving the taxonomy of Roseburia spp., Eubacterium rectale and
RT Agathobacter spp. through phylogenomic analysis.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PHU37191.1, ECO:0000313|Proteomes:UP000224563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JK623 {ECO:0000313|EMBL:PHU37191.1,
RC ECO:0000313|Proteomes:UP000224563};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) 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:PHU37191.1}.
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DR EMBL; PDYG01000074; PHU37191.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G3E1U5; -.
DR Proteomes; UP000224563; 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 Reference proteome {ECO:0000313|Proteomes:UP000224563};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 479 AA; 52675 MW; 76CB80C48D02E532 CRC64;
MAGKTAKKQK ETKIVYAWEK YPQGKERDKV MKFAESYRKF ISENKTEREC TSTIYEDAIK
NGFVDLEEVI ASGKKLEAGS RVIANNMGKG LALFIVGEEP IQNGMNILGA HIDSPRIDLK
QVPLYEDALY KTHFAMLDTH YYGGIKKYQW VTLPLALHGV FAKKDGSVVN VSIGDKPGDP
VFGISDLLIH LAGSQMSKKA TEVITGEKLD ILVGSIAKSK EEEEEAKDLV KKNVLAILAE
TYGIEEDDFL SAEIEVVPAG EARDYGLDRS MIMGYGHDDR VCAYPSYKAM LKIDQPKYTS
VCLLVDKEEI GSVGASGMQS RFFENCVAEM IALTGEYSDL YVRRALKNSK ALSSDVSAAL
DPNFPAVMED KNSAFFGKGL VFNKYTGSRG KSGSNDANAE YVAKVRAIMD NNNVKFQTAE
LGKVDEGGGG TIAYILGNYN MNVIDSGVAV LNMHAPWEII SKVDLYEAYL GYVAFLKEA
//
