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
//