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Database: UniProt
Entry: W9DR50_METTI
LinkDB: W9DR50_METTI
Original site: W9DR50_METTI 
ID   W9DR50_METTI            Unreviewed;       462 AA.
AC   W9DR50;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:ETA68103.1};
GN   ORFNames=MettiDRAFT_1555 {ECO:0000313|EMBL:ETA68103.1};
OS   Methanolobus tindarius DSM 2278.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX   NCBI_TaxID=1090322 {ECO:0000313|EMBL:ETA68103.1, ECO:0000313|Proteomes:UP000019483};
RN   [1] {ECO:0000313|EMBL:ETA68103.1, ECO:0000313|Proteomes:UP000019483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2278 {ECO:0000313|EMBL:ETA68103.1,
RC   ECO:0000313|Proteomes:UP000019483};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
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   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290}.
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:ETA68103.1}.
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DR   EMBL; AZAJ01000001; ETA68103.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9DR50; -.
DR   STRING; 1090322.MettiDRAFT_1555; -.
DR   Proteomes; UP000019483; 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: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:0000313|EMBL:ETA68103.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   462 AA;  51490 MW;  28B543F1C57BEF6E CRC64;
     MFRAHALIEN LLFTIVPVLK KRDSVTSDNM DTSKDYTSGF FNFMKKATTP VQTVDTIIER
     LDAEGFSKLD LNEQWNFSAS GKYWLSPYPS MIIAFTIGKS DSLTKSMRII AAHTDNPAFR
     IKPNPEVSSE GMLTLNVERY GGPILNTWFD RPLSIAGRIA VKSDEVLKPK VIHLDFQRPI
     LTLPNLAIHM NPGPNQSTEI KVQKEMQPLL TRLMEDEVKD NYLLDLVAKE IGVNAEEILD
     MDLNVYCCEE GMLVGLKEEF VSCPRIDDLS MVYAAMEALV ASDNNSGINI AAFMDNEEVG
     SMTKQGADSV LLSSILEKIH AGIEGIDQRS ECQVKDYFVI SADGAHGLHP NYAEKNDITN
     KPVMNKGITI KISGSRSYAS EVETIAAFQQ LCNKAGVKYQ KFVNHSDQRG GTTLGPLLSK
     YLPVHVVDVG VPMLAMHSTR ELMGKQDFLD SIEVFRTFFQ LE
//
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