ID A6LLV4_THEM4 Unreviewed; 364 AA.
AC A6LLV4;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ABR30905.1};
GN OrderedLocusNames=Tmel_1044 {ECO:0000313|EMBL:ABR30905.1};
OS Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Thermosipho.
OX NCBI_TaxID=391009 {ECO:0000313|EMBL:ABR30905.1, ECO:0000313|Proteomes:UP000001110};
RN [1] {ECO:0000313|EMBL:ABR30905.1, ECO:0000313|Proteomes:UP000001110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12029 / CIP 104789 / BI429
RC {ECO:0000313|Proteomes:UP000001110};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermosipho melanesiensis BI429.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABR30905.1, ECO:0000313|Proteomes:UP000001110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12029 / CIP 104789 / BI429
RC {ECO:0000313|Proteomes:UP000001110};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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DR EMBL; CP000716; ABR30905.1; -; Genomic_DNA.
DR RefSeq; WP_012057265.1; NC_009616.1.
DR AlphaFoldDB; A6LLV4; -.
DR STRING; 391009.Tmel_1044; -.
DR KEGG; tme:Tmel_1044; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_0; -.
DR OrthoDB; 9776731at2; -.
DR Proteomes; UP000001110; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd03886; M20_Acy1; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABR30905.1}.
FT DOMAIN 173..264
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 364 AA; 41367 MW; AE8E657705D2062F CRC64;
MEAIELRHIL HQNPEISFRE FETQKILLNA LKSLNNNNLK IYKIAGTGVI AIYEPKKGKP
FIIYRADIDG LPIEEKTDWK YASKNSNMHA CGHDIHMSIA YDLIKKITEN NIDQNFAFVF
QPGEETGAGA RYVLDEIEEL PVKYAIALHV TDEYDFKTIS TTKGTLFAAA TEIDVTFYGK
ASHVAFYENG IDSIKMASNF LNEFYSLKFE DSLVAFGKIA GGNARNIVSQ ETTIMGSIRT
NSSEKTKSII SILENLAEKT AKENKGSFSI SKGSEYPPVI VNDELFFKFK DFLKSTDANF
VECNMKFTGE DFGYFSQEYP SLMFWIGTRI DEKYGLHNPK FLPKDDVIPY YSNIIFNFLK
ELTK
//
