ID A7HLW2_FERNB Unreviewed; 464 AA.
AC A7HLW2;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Dipeptidase, putative {ECO:0000313|EMBL:ABS60895.1};
GN OrderedLocusNames=Fnod_1046 {ECO:0000313|EMBL:ABS60895.1};
OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=381764 {ECO:0000313|EMBL:ABS60895.1, ECO:0000313|Proteomes:UP000002415};
RN [1] {ECO:0000313|EMBL:ABS60895.1, ECO:0000313|Proteomes:UP000002415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC {ECO:0000313|Proteomes:UP000002415};
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., Saunders E., 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 Fervidobacterium nodosum Rt17-B1.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABS60895.1, ECO:0000313|Proteomes:UP000002415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC {ECO:0000313|Proteomes:UP000002415};
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; CP000771; ABS60895.1; -; Genomic_DNA.
DR RefSeq; WP_011994209.1; NC_009718.1.
DR AlphaFoldDB; A7HLW2; -.
DR STRING; 381764.Fnod_1046; -.
DR KEGG; fno:Fnod_1046; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_031786_2_0_0; -.
DR OrthoDB; 9761532at2; -.
DR Proteomes; UP000002415; Chromosome.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 NCBIfam; TIGR01887; dipeptidaselike; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF33; DIPEPTIDASE SAOUHSC_01868-RELATED; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002415}.
SQ SEQUENCE 464 AA; 51767 MW; 150C27DA0A42591C CRC64;
MENIDGKIKE LVDKHFDSIL KALDRVIAIR SVMGEPKEGM PFGEGPAKAL EETLEIAKEL
GFEPVNVDNY AGHVEYGSKD GKYYAVLGHL DVVPEGDLER WETDPYKLSI RDGKMYARGV
SDDKGPSIGA LFALKIASEL VDKPKNRVRI IFGTNEENGS KCLKYYFTKE PYPDAAVTPD
GDFPLVFAEK GIVTYKISKN MSQNYSTKIV ELKAGTAANV VPEECIAVIE SDKVKEIAYV
VENYKSACRY EYSIDGNKIT IKSLGKSAHG AHPEAGLNAA GGMLELLSRL DLGPETETIR
MLYEKLGKDY YGIGLGISGQ DDVSRKLTCN LGVLKLENGK IEAIINIRHP IFFNVDMITL
QIKEAMKGFE VEQMSYSKPL YVSKDSDLVK TLMEIYYSET KDETQPLAIG GGTYARSVPY
GVAYGAVFPG EETHMHEPNE NWSLESFKKF IRIYTKLIYR WLTE
//
