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Database: UniProt
Entry: C6LJQ7_9FIRM
LinkDB: C6LJQ7_9FIRM
Original site: C6LJQ7_9FIRM 
ID   C6LJQ7_9FIRM            Unreviewed;       440 AA.
AC   C6LJQ7;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=BRYFOR_08894 {ECO:0000313|EMBL:EET59180.1};
OS   Marvinbryantia formatexigens DSM 14469.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Marvinbryantia.
OX   NCBI_TaxID=478749 {ECO:0000313|EMBL:EET59180.1, ECO:0000313|Proteomes:UP000005561};
RN   [1] {ECO:0000313|EMBL:EET59180.1, ECO:0000313|Proteomes:UP000005561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14469 {ECO:0000313|EMBL:EET59180.1,
RC   ECO:0000313|Proteomes:UP000005561};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JUL-2009) 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:EET59180.1}.
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DR   EMBL; ACCL02000021; EET59180.1; -; Genomic_DNA.
DR   RefSeq; WP_006863657.1; NZ_CP102268.1.
DR   AlphaFoldDB; C6LJQ7; -.
DR   STRING; 168384.SAMN05660368_01983; -.
DR   eggNOG; COG1362; Bacteria.
DR   OrthoDB; 9764268at2; -.
DR   Proteomes; UP000005561; 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; cd05658; M18_DAP; 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:SF3; ASPARTYL AMINOPEPTIDASE; 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:UP000005561};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   440 AA;  48309 MW;  2071020E6984A74D CRC64;
     MSVQLTRELF DFIEGSPSCF HAVESMRRQL DGAGYTQLLE SRPWSLAPGG KYYVVRNGSS
     LIAFRIPETE ICGFQIMASH SDSPCFKIKE NPEMEAEGHY IKLNVEKYGG MLMAPWFDRP
     LSVAGRLMVR ENGQIKVKLV NVDRDLLMIP NLAIHMNREA NDGMKYNVQK DLLPLYGDET
     AKGSFQALVA EAAGVSPEAV TGSDLFLYNR MPGSIWGANR EFISIGRLDD LQCAFSSLKG
     FLEAEEGESI PVHCVFDNEE VGSGTRQGAA STFLYDTLAN ICGALGKTMM EYRRMLAASF
     MLSADNAQGV HPNYGEKACP TNRPYLNGGI VLKYSANQKY TTDGIAAAVF KEICTMAEVP
     YQNYVNRSDI LGGSTLGNIS GTQVAVATAD IGLAQLAMHS PYETGGIRDT EYLVKAAKVF
     FESSVCETGY GSFRIQRKAY
//
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