ID F3BBI8_9FIRM Unreviewed; 463 AA.
AC F3BBI8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=HMPREF9477_01308 {ECO:0000313|EMBL:EGG82299.1};
OS Lachnospiraceae bacterium 2_1_46FAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=742723 {ECO:0000313|EMBL:EGG82299.1, ECO:0000313|Proteomes:UP000018451};
RN [1] {ECO:0000313|EMBL:EGG82299.1, ECO:0000313|Proteomes:UP000018451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_1_46FAA {ECO:0000313|EMBL:EGG82299.1,
RC ECO:0000313|Proteomes:UP000018451};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Ambrose C., Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 2_1_46FAA.";
RL Submitted (DEC-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:EGG82299.1}.
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DR EMBL; ADLB02000009; EGG82299.1; -; Genomic_DNA.
DR AlphaFoldDB; F3BBI8; -.
DR STRING; 742723.HMPREF9477_01308; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_590123_0_0_9; -.
DR OrthoDB; 89722at2; -.
DR Proteomes; UP000018451; 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 CDD; cd05659; M18_API; 1.
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:UP000018451};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 463 AA; 51249 MW; C9B79D37D35EA35B CRC64;
MERKNMWKQY TVEQLNEVEE VSKRYKDCLD AGKTERECVS LAVSMAEEHG YRNLEECIAE
NTELKAGDKV YVNQMGKALV LFQIGQKPLE EGMNILGAHV DSPRIDIKQN PLYEDTDLAY
LDTHYYGGIK KYQWVSIPLA IHGTVAKKDG TTVDIVVGEK EEDPVLVISD LLIHLAGEQM
DKKASVVIEG EGLDVLVGSK PLSTEDKEEK ELVKATILSF LKDNYGIEEE DFLSAELEIV
PAGKARDCGF DRSMIMGYGH DDRICAFTSL FAMLEVENPE RTSCCLLVDK EEIGSVGATG
MESKFFENAV AELVALTVGE SSLKVRRALQ NSYMLSSDVS AAYDPMFANA FEKKNTAYFG
RGLCLNKYTG ARGKSGSSDA NAEYIAKIRK VFDDNEIGFQ TAELGKVDFG GGGTIAYIMA
DYGMNVIDSG MAVLSMHAPW EIASKADIYE GYKGYKAFLR EMK
//