ID U2Q0X0_9CLOT Unreviewed; 466 AA.
AC U2Q0X0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 03-MAY-2023, entry version 30.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=CINTURNW_2852 {ECO:0000313|EMBL:ERK29679.1};
OS Clostridium intestinale URNW.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1294142 {ECO:0000313|EMBL:ERK29679.1, ECO:0000313|Proteomes:UP000016721};
RN [1] {ECO:0000313|EMBL:ERK29679.1, ECO:0000313|Proteomes:UP000016721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URNW {ECO:0000313|EMBL:ERK29679.1,
RC ECO:0000313|Proteomes:UP000016721};
RX PubMed=24136853;
RA Lal S., Ramachandran U., Zhang X., Sparling R., Levin D.B.;
RT "Draft Genome Sequence of the Hydrogen- and Ethanol-Producing Bacterium
RT Clostridium intestinale Strain URNW.";
RL Genome Announc. 1:e00871-13(2013).
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:ERK29679.1}.
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DR EMBL; APJA01000014; ERK29679.1; -; Genomic_DNA.
DR RefSeq; WP_021802834.1; NZ_KI273145.1.
DR AlphaFoldDB; U2Q0X0; -.
DR STRING; 1294142.CINTURNW_2852; -.
DR PATRIC; fig|1294142.3.peg.2962; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_590123_0_0_9; -.
DR OrthoDB; 89722at2; -.
DR Proteomes; UP000016721; 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:UP000016721};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 466 AA; 52177 MW; 818CEA95906D5D3B CRC64;
MEQNLRKEYA LAWDKYDEED LKKVFSISDR YKNFISKCKT ERESVDELIV LAEKEGYRNV
QDIINNGETL KAGDKVYANN MGKTLALFLI GSEPLEKGLR ILGAHVDSPR LDLKQNPLYE
DGGLALFDTH YYGGVKKYQW VTIPLAIHGV IVKKDGTLVK VEIGEDDNDP VVGISDLLIH
LAGKQLEKKA REVIEGEDLN VLVGSMPIKN KEVKERVKEN ILVLLNEKYG IIEEDFVSSE
LEIVPAGKAR DYGLDRSMVM GYGHDDRICA YTSFEALLEL KDTDRTCVAL FVDKEEIGSV
GATGMNSKFF ENILAEIMDR KGEYSELKLR RCLNNSHMLS SDVTAAHDPN FPGVLEKNNA
AYFGKGVVFC KYTGARGKSG SNDANPEYIA RIREIMDKNE VVWQTAELGK VDQGGGGTIA
YILAQYNMEV IDCGIALHNM HAPWEVASKA DIYEAVKCYK AFLKEI
//
