ID Q6NIP6_CORDI Unreviewed; 1060 AA.
AC Q6NIP6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=DIP0722 {ECO:0000313|EMBL:CAE49244.1};
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=257309 {ECO:0000313|EMBL:CAE49244.1, ECO:0000313|Proteomes:UP000002198};
RN [1] {ECO:0000313|EMBL:CAE49244.1, ECO:0000313|Proteomes:UP000002198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis
RC {ECO:0000313|Proteomes:UP000002198};
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.,
RA Bentley S.D., Besra G.S., Churcher C., James K.D., De Zoysa A.,
RA Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S.,
RA Jagels K., Moule S., Quail M.A., Rabbinowitsch E., Rutherford K.,
RA Thomson N.R., Unwin L., Whitehead S., Barrell B.G.Parkhill.J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; BX248356; CAE49244.1; -; Genomic_DNA.
DR RefSeq; WP_010934505.1; NC_002935.2.
DR AlphaFoldDB; Q6NIP6; -.
DR STRING; 257309.DIP0722; -.
DR KEGG; cdi:DIP0722; -.
DR HOGENOM; CLU_004900_0_0_11; -.
DR Proteomes; UP000002198; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF59; DNA HELICASE; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000002198}.
FT DOMAIN 50..367
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 306..608
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 71..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1060 AA; 116985 MW; 336CFEF9C386DE1F CRC64;
MDAFSTPQDS PTTSAQVIGE DLTAGIPPLQ QSFVYAQRPR VEIVYNDHSE PIREWDNQLF
QEQRGTWRVT GAAGAGVSTL LMDTVAERIR RGVSPESIIV VAASRESAAR LRAGIAHRIA
DGSYTSPASL VRSVHSLAFA LLRSLSDEQL RLITGAEQDA VIRELLQGHV DNPSLAAMWP
AEARQALGLI GFAREVRDFL LRSGERGLEP EDLEELGARY GRPMWASAGK FMREYQQVMN
LGGTHSLNAS ELVSKLLCFD IPDMGWRTII IDDAQHLDPQ SAQLLQALMR YTDFTVIAGD
PQQSVFHFRG ASPEFLLHAP VDHELTLYSS FRQPTVEAKV LGSTGDQSEF VADLLRRSHL
LEGIRWNDMA VIVRSTADIP SLRRALLSAG VPVQEDPSDI ILSEQRIVSA LILAVRAIYQ
ELSAQELEEL ALGPIGGADT VTLRRLFRGL RKAEMHAGGN RRAIEIMREL IDPKESEEQT
QLREQVEAVL TDRELAVVDK IRAVLVRGAQ PGSVEEILWE IWDASALSSH LQTVSLRGGV
RGAQADRDLD AVMALFDAAG DWVERRPTAS ITSFVRHIAE QELPTGVRDR RLATADAVRI
VTAHGSLGQQ WHTVIVAGVQ EGTWPSLQET GTLFGQEDLI DLIDSGIEPN TYISRSAEKL
KEEKRLFHVA RTRGTHRVVI TAVESPESDT AAEPSRFLQG IAESKVQGPT TDPETASVQS
EIDTETVHLD QYVRLLSVPS IVAELRRELA NPDSPQRRRE QAARQLARLA LHQVPGARPE
QWWGYGGPSE TTSLDISKVS PSLIENALLC PLRARLERLV EEENTPIHML KGTLAHAFAE
AVGRGVDPNE AEQLVTQAFE ALLDAPAWSL PHHMSQWSTM LQRLAHWIDV SHAQRELVGV
EVPVNVVVAP GVELRGRIDR LERNDAGEFH IVDFKTGKQA VTKDEANENK QLLAYQLALH
RGKLMQRNGE PAINTTAEQP GLTVDQAVLV YPATDTKTVT TREQAPKDAE ELEKFSATLP
ALLESLSGPQ LVARINTRCD QCKIKTMCPA QPEGKMVPEC
//
