ID U2R0Y4_9FUSO Unreviewed; 450 AA.
AC U2R0Y4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=HMPREF1984_00202 {ECO:0000313|EMBL:ERK68915.1};
OS Leptotrichia sp. oral taxon 215 str. W9775.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=1321779 {ECO:0000313|EMBL:ERK68915.1, ECO:0000313|Proteomes:UP000016640};
RN [1] {ECO:0000313|EMBL:ERK68915.1, ECO:0000313|Proteomes:UP000016640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W9775 {ECO:0000313|EMBL:ERK68915.1,
RC ECO:0000313|Proteomes:UP000016640};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ERK68915.1}.
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DR EMBL; AWVR01000007; ERK68915.1; -; Genomic_DNA.
DR AlphaFoldDB; U2R0Y4; -.
DR STRING; 1321779.HMPREF1984_00202; -.
DR PATRIC; fig|1321779.3.peg.199; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_019532_2_0_0; -.
DR OrthoDB; 9764268at2; -.
DR Proteomes; UP000016640; 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:UP000016640};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 450 AA; 50256 MW; CFC29716C6EC5014 CRC64;
MIEIQDEMKL MQEKFEDMEV KSFAREVIEF IDECPSTYHV AKNCSEILEE NGFERLIPQE
KWNLKKGGKY YVKKSNSTVV AFTLGTDINL KKGFKIFGSH TDSPGFRIKP NPEMVTENIL
RLNTEVYGGP ILSTWFDRPL SIAGRVVVKS DNIFLPKTIR VKSEEPLMVI PNLAIHQNRE
VNNGVKIDRQ ADTLPVLGLI NDKLEKDDYL LKLIAEKMKL KKEDILDFDL YVYSIEKGCL
AGANEEFISA PKIDNLASVY AGLLGLVEAE DVHDQINVFV GFDNEEIGSA TKQGADSNYL
LNTLERIVCG LGYGRGEFLQ MLNCSFLLSA DGAHAAHPAH MNKTDPTSRG RINEGISIKI
SANQSYTSDG FSIAVVKQII EGTDIKIQPF VNQSNERGGS TIGPISSTHL DIDAVDLGVP
MLAMHSVREL CGIYDVFYLK ELAKEFFNKN
//
