ID A6LNR1_THEM4 Unreviewed; 465 AA.
AC A6LNR1;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Dipeptidase, putative {ECO:0000313|EMBL:ABR31562.1};
GN OrderedLocusNames=Tmel_1723 {ECO:0000313|EMBL:ABR31562.1};
OS Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Thermosipho.
OX NCBI_TaxID=391009 {ECO:0000313|EMBL:ABR31562.1, ECO:0000313|Proteomes:UP000001110};
RN [1] {ECO:0000313|EMBL:ABR31562.1, 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:ABR31562.1, 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).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000716; ABR31562.1; -; Genomic_DNA.
DR RefSeq; WP_012057921.1; NC_009616.1.
DR AlphaFoldDB; A6LNR1; -.
DR STRING; 391009.Tmel_1723; -.
DR KEGG; tme:Tmel_1723; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_031786_2_0_0; -.
DR OrthoDB; 9761532at2; -.
DR Proteomes; UP000001110; Chromosome.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd03888; M20_PepV; 1.
DR Gene3D; 3.30.70.360; -; 2.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR010964; M20A_pepV-rel.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01887; dipeptidaselike; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF33; DIPEPTIDASE SAOUHSC_01868-RELATED; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Dipeptidase {ECO:0000256|ARBA:ARBA00022997};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022997};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022997}.
FT DOMAIN 261..368
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 465 AA; 52573 MW; B78F7007B5E6EF32 CRC64;
MSFDIEKQID LKVEKYFDEI LDSLSKIIKI RSVMEKPTEE YPFGKGPAKA LIETLNLSKS
LGFKDVKNVD NYAGHVEYGN KGRLYGILGH LDVVPEGDLD RWESDPYELT IREGKMYGRG
VSDDKGPSIG ALYALKIVSE LVKNPKNRVR IIFGTNEENG SKCLKYYFKK EPYPKEAVTP
DGMFPLVFAE KGNATYKIST LLNSNYHTRL LYLKAGTAVN VVPEKCEAVI KTEKVSEIVY
FLENYKTECK LKYVIDENII RLQTIGKSVH ASTPHLGINA ISCMVDILSK IDFGVYNWIF
DTLYKKLGRD YNGIGLDIYS EDNASGKLTC NLGTIELIDG NLELKINIRY PIFMSNEMIS
MQIKKALKGF EVERISHKGP LYVSKDSELV KTLLSVYRSV TNDESEPIAI GGGTYARTVP
YGVAFGATFP GEDTGMHQPN ESWSLESFKK FIKIYARLIY KWLTR
//
