ID Q8FRH1_COREF Unreviewed; 1024 AA.
AC Q8FRH1; C8NLR2;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196164 {ECO:0000313|EMBL:BAC17600.1, ECO:0000313|Proteomes:UP000001409};
RN [1] {ECO:0000313|EMBL:BAC17600.1, ECO:0000313|Proteomes:UP000001409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395
RC {ECO:0000313|Proteomes:UP000001409};
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(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; BA000035; BAC17600.1; -; Genomic_DNA.
DR RefSeq; WP_006769527.1; NZ_GG700687.1.
DR AlphaFoldDB; Q8FRH1; -.
DR STRING; 196164.gene:10741192; -.
DR KEGG; cef:CE0790; -.
DR eggNOG; COG0210; Bacteria.
DR eggNOG; COG2887; Bacteria.
DR HOGENOM; CLU_004900_0_0_11; -.
DR OrthoDB; 5240387at2; -.
DR Proteomes; UP000001409; 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:UP000001409}.
FT DOMAIN 26..308
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 279..578
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1024 AA; 112134 MW; C94469E54B8647A2 CRC64;
MSEYQPFIPQ DPRVRLVPAR ARVTPRTWSG PSRELIDAGT STWRVTGVAG SGVSSLVIDT
VVERIRQGWD PSSILIVAAS KEAASRLRRE LSELVSDLDY VSEGPMVRSV HSLAFALIRD
SCDEDVRLIT GAEQDAVVRE LLRGHADDDR GVWPPEQREG LRMVGFARQL RDFLLRAVER
GVGPDDLVRY GQQYNRPAWV SAGEFLREYQ QIMRLAGSHS YSASELVTGA LACGDPRTTY
RGVFVDDAQH LDPKSAELIT RFIPAAELAV IAGDPEQSVF HFRGANPDFL LDFEANRSIH
LGEGRRTPLI SIAVTETASA HNDLLADTVR RAHLLDGVDW SDIAVIVRSA GMIAPVRRVL
LAAGVPVHIS PTDVVLSEQR IVAAMILGLR ALTEELTPLE LEDLLLGPIG GADPVTLRRL
LRGLRQAEMR ADGHRRAIEV LRGLLNTDAD EELLAFLTDR ELELLERVRS VLRAGREAMA
GGSTEEILWA VWEATGLSSH LSAVSLRGGA AGSQADRDLD AIMALFDAAG DYVERYPTAG
IRSFIVHISE QELPTGVRER RGVSPEAVTV TTAHATTGRE WRHVIVAEVQ EGSWPSLGET
GTLLGQEELI DLLDENIDPD TIISRSVDRL AEERRLFHVA TSRACDQLLV TAVNTPDSDE
VREPSRFLEE LAEAHRVEIT HIEGPGETPL AEPEVLGHRL LSVPALVAEL RRVVTDPGEL
GSRRRQAARQ LNRLAGAGIP GADPDTWLAL REPSTTAELI PEGRVWLSPS RIEALMNCPL
RASLDRLDSE DETPIAMLRG TLVHAFAEAV ARGADPERAG EMVTEAYMDL ANVPSWSRET
TEQDFRRTIT RTHTWLQTSR VTFDLVGTEM EVEVGISTEV GIRGRMDRLE RNHAGELVIV
DLKTGRQAAV QKDMGEHAQL ASYQLALSRG VLHGDRVEDP APGETPEPVG GGVLVYPAHD
AKGITTRDQA AKTPEELDEL AALLPELAHL RRGPNLLARV NPTCGNCPVK SLCPVQPEGR
LIHG
//
