ID D4M2Q5_9FIRM Unreviewed; 466 AA.
AC D4M2Q5;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=RTO_08080 {ECO:0000313|EMBL:CBL25517.1};
OS [Ruminococcus] torques L2-14.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=657313 {ECO:0000313|EMBL:CBL25517.1, ECO:0000313|Proteomes:UP000008956};
RN [1] {ECO:0000313|EMBL:CBL25517.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL25517.1,
RC ECO:0000313|Proteomes:UP000008956};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Ruminococcus torques L2-14.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL25517.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL25517.1,
RC ECO:0000313|Proteomes:UP000008956};
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; FP929055; CBL25517.1; -; Genomic_DNA.
DR AlphaFoldDB; D4M2Q5; -.
DR STRING; 33039.ERS852502_02132; -.
DR KEGG; rto:RTO_08080; -.
DR PATRIC; fig|657313.3.peg.487; -.
DR HOGENOM; CLU_590123_0_0_9; -.
DR Proteomes; UP000008956; 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 466 AA; 51797 MW; 650AA4FDB498A64B CRC64;
MDRKNAWTTY SKEELDRLEQ VNTEYKNCLD AGKTERECVT LAVEKAKAEG YKDIRDIIKN
GEKVKAGDKL YAVCMNKTIA LFHMGTKPLT EGMNILGAHI DSPRIDVKQN PLYENEEFAY
LDTHYYGGIK KYQWVTLPLA LHGVIAKKDG TTVQVSIGEK EDDPVFVITD LLIHLASKQM
EKKAATVVEG EKLDLLIGSR PIEQDETLEE KEKEAVKANV INLLKQYYDM EEEDFLSAEL
EIVPAGKARD CGLDRSMVLA YGQDDRVCAF TSLFAMLDVE EVEHTACCIL VDKEEIGSVG
ATGMHSRFFE NTVAELVALT EGESDLKVRR ALMNSRMLSS DVSAAYDPMY AEVFEKRSSA
FFGKGLVFNK FTGARGKSGS NDANAEYLAK IRNAMDAQSV AYQFAELGKV DAGGGGTIAY
IMANYGMEVI DSGVAVLSMH APWEVTSKAD VYEAYKGYKA FIEEMR
//
