DING_MYCTO
ID DING_MYCTO Reviewed; 664 AA.
AC P9WMR4; L0T6J2; P64314; Q10640;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Probable ATP-dependent helicase DinG homolog;
DE EC=3.6.4.12;
GN Name=dinG; OrderedLocusNames=MT1371;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Probable helicase involved in DNA repair and perhaps also
CC replication. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK45635.1; -; Genomic_DNA.
DR PIR; E70770; E70770.
DR RefSeq; WP_003898827.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WMR4; -.
DR SMR; P9WMR4; -.
DR EnsemblBacteria; AAK45635; AAK45635; MT1371.
DR GeneID; 45425307; -.
DR KEGG; mtc:MT1371; -.
DR PATRIC; fig|83331.31.peg.1478; -.
DR HOGENOM; CLU_012117_2_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11472; PTHR11472; 2.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding.
FT CHAIN 1..664
FT /note="Probable ATP-dependent helicase DinG homolog"
FT /id="PRO_0000427256"
FT DOMAIN 14..290
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 246..249
FT /note="DEAH box"
FT BINDING 49..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 664 AA; 70168 MW; 875A13606091CDB1 CRC64;
MSESVSMSVP ELLAIAVAAL GGTRRRGQQE MAAAVAHAFE TGEHLVVQAG TGTGKSLAYL
VPAIIRALCD DAPVVVSTAT IALQRQLVDR DLPQLVDSLT NALPRRPKFA LLKGRRNYLC
LNKIHNSVTA SDHDDERPQE ELFDPVAVTA LGRDVQRLTA WASTTVSGDR DDLKPGVGDR
SWSQVSVSAR ECLGVARCPF GSECFSERAR GAAGLADVVV TNHALLAIDA VAESAVLPEH
RLLVVDEAHE LADRVTSVAA AELTSATLGM AARRITRLVD PKVTQRLQAA SATFSSAIHD
ARPGRIDCLD DEMATYLSAL RDAASAARSA IDTGSDTTTA SVRAEAGAVL TEISDTASRI
LASFAPAIPD RSDVVWLEHE DNHESARAVL RVAPLSVAEL LATQVFARAT TVLTSATLTI
GGSFDAMATA WGLTADTPWR GLDVGSPFQH AKSGILYVAA HLPPPGRDGS GSAEQLTEIA
ELITAAGGRT LGLFSSMRAA RAATEAMRER LSTPVLCQGD DSTSTLVEKF TADAATSLFG
TLSLWQGVDV PGPSLSLVLI DRIPFPRPDD PLLSARQRAV AARGGNGFMT VAASHAALLL
AQGSGRLLRR VTDRGVVAVL DSRMATARYG EFLRASLPPF WQTTNATQVR AALRRLARAD
AKAH