ID   E9SCW6_RUMAL            Unreviewed;       469 AA.
AC   E9SCW6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-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=CUS_6720 {ECO:0000313|EMBL:EGC02919.1};
OS   Ruminococcus albus 8.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=246199 {ECO:0000313|EMBL:EGC02919.1, ECO:0000313|Proteomes:UP000004259};
RN   [1] {ECO:0000313|EMBL:EGC02919.1, ECO:0000313|Proteomes:UP000004259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8 {ECO:0000313|EMBL:EGC02919.1,
RC   ECO:0000313|Proteomes:UP000004259};
RA   Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D., Montgomery R.,
RA   Ziemer C., Klaassens E., Ocuiv P., Morrison M.;
RL   Submitted (FEB-2011) 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:EGC02919.1}.
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DR   EMBL; ADKM02000085; EGC02919.1; -; Genomic_DNA.
DR   RefSeq; WP_002849985.1; NZ_JAJFOM010000003.1.
DR   AlphaFoldDB; E9SCW6; -.
DR   STRING; 246199.CUS_6720; -.
DR   eggNOG; COG1362; Bacteria.
DR   OrthoDB; 89722at2; -.
DR   Proteomes; UP000004259; 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:UP000004259};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   469 AA;  51880 MW;  170B484F5F2DF839 CRC64;
     MADKKKTAAE ELSEKLLSKP KNGILRVDDK ELKACDDFNE GYKAFLNTAK TEREAVEEIT
     AQAEAAGFKV FERGKKYKAG DKFYFVNRKK AVILTVMGKK SIAEGIRLAA AHIDSPRLDM
     KQNPLYEDKE IAYFKTHYYG GIKKYQWPTV PLSLHGVIIK ADGESVKVRI GEDEGDPVFC
     ISDILPHLAE SQYKRPAPKL ITGEELNIIV GSRPFKDDKI SQKVKLNIMA ILNEKYGIVE
     DDFISAELEA VPAFKASDVG FDRSLVGAYG QDDRVCAYTA LQAILQLKKP EYTCMTVLTD
     KEETGSDGNT GLNSSYLPYF INDLAEVYGV NGYNVMSRSE CLSADVNAAV DPTFIEPFEI
     RNCSQLNYGV VATKFTGARG KSGTSDASAE FVGRVRRLFD KNGIIWQTGE LGKVDAGGGG
     TVAQFIANLD FDVIDVGVSV LSMHAPFEIT SKLDNYMAYK SFKVFFEDK
//