ID D0MGR1_RHOM4 Unreviewed; 1112 AA.
AC D0MGR1;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Transcription-repair-coupling factor {ECO:0000256|HAMAP-Rule:MF_00969};
DE Short=TRCF {ECO:0000256|HAMAP-Rule:MF_00969};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00969};
GN Name=mfd {ECO:0000256|HAMAP-Rule:MF_00969};
GN OrderedLocusNames=Rmar_2754 {ECO:0000313|EMBL:ACY49624.1};
OS Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS obamensis).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC Rhodothermus.
OX NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY49624.1, ECO:0000313|Proteomes:UP000002221};
RN [1] {ECO:0000313|EMBL:ACY49624.1, ECO:0000313|Proteomes:UP000002221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43812 / DSM 4252 / R-10
RC {ECO:0000313|Proteomes:UP000002221};
RX PubMed=21304669; DOI=10.4056/sigs.46736;
RA Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL Stand. Genomic Sci. 1:283-291(2009).
CC -!- FUNCTION: Couples transcription and DNA repair by recognizing RNA
CC polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent
CC release of RNAP and its truncated transcript from the DNA, and
CC recruitment of nucleotide excision repair machinery to the damaged
CC site. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC RecG subfamily. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC {ECO:0000256|HAMAP-Rule:MF_00969}.
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DR EMBL; CP001807; ACY49624.1; -; Genomic_DNA.
DR RefSeq; WP_012845234.1; NC_013501.1.
DR AlphaFoldDB; D0MGR1; -.
DR STRING; 518766.Rmar_2754; -.
DR KEGG; rmr:Rmar_2754; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_10; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000002221; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR CDD; cd17991; DEXHc_TRCF; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.11180; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR Gene3D; 3.90.1150.50; Transcription-repair-coupling factor, D7 domain; 1.
DR HAMAP; MF_00969; TRCF; 1.
DR InterPro; IPR003711; CarD-like/TRCF_RID.
DR InterPro; IPR036101; CarD-like/TRCF_RID_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR004576; Mfd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047112; RecG/Mfd.
DR InterPro; IPR037235; TRCF-like_C_D7.
DR InterPro; IPR005118; TRCF_C.
DR InterPro; IPR041471; UvrB_inter.
DR NCBIfam; TIGR00580; mfd; 1.
DR PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR Pfam; PF02559; CarD_TRCF_RID; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF03461; TRCF; 1.
DR Pfam; PF17757; UvrB_inter; 1.
DR SMART; SM01058; CarD_TRCF; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00982; TRCF; 1.
DR SUPFAM; SSF141259; CarD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF143517; TRCF domain-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00969};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Reference proteome {ECO:0000313|Proteomes:UP000002221}.
FT DOMAIN 570..731
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 752..906
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1112 AA; 126004 MW; E8699BD184D57883 CRC64;
MKLTDLHHRL ASAAFFEPLH AHLESLTPST RLHLRGLAGS LPAFVLYELS RHLRRPVLCL
TPDEEQAAYL FSDLEQLLGV SDRLLRFPAT GQKPYDPEQI PDSAPLIERT DVLRRLAEGF
DGLLLASAEA IAERVPPPDR VRQETLVLSP GMVIDPAQLL AHLIARGFER VEFVEAPGEV
ALRGGILDVY PFTGTHPIRV EFFGDEIDTI REFDPRTQRS ISRLTSAQIV PNLSAADSEE
AAHTLFEHLP DHALLVLFEE GALFDAVQAR FAEAEQAYAR LNAPDEQPRP EARYLPPAEL
AAHLNRYPAL LFGTLAEAER TLTWDTHPQP AFHGNLNLLR ERLHENARRG WETVILCDSR
SQEARLHDLL QEEIEAGGVR LLVESLHEGF EVPEARLAVY TDHQIFGRYH RPTTRRRRHL
LGGLSLRALQ NLQPGDYVVH VDFGIGQFAG LQRITIRGKQ QEVVRLHYAD GDVLYVSVNA
LHKLHRYTGR EGHQPRLTKL GSGQWEKVKA RTKKRVKDIA RDLIRLYAKR KASRGFAFSP
DTVWQREMEA AFEYEDTPDQ AAAAEAVKRD MEQPVPMDRL VCGDVGFGKT EIAIRAAFKA
VQDGKQVAVL VPTTILADQH YETFTRRLAP YPVRIEVLSR FRSPARQRAV LRDLAAGKVD
IIIGTHRLLS KDVQFKDLGL LIIDEEQRFG VAAKERLRQL RVEVDTLTLT ATPIPRTLQF
ALMGARDLSI ISTPPPNRQP IVTEIHTFDE TLIRDAIRYE ISRGGQVFFI HNRVQSIYEM
AARLQAIVPD VRIAVAHGQM KPRELERVMH DFMARKYDVL VSTNIIESGL DIPNANTIII
NHAEQFGLAD LHQLRGRVGR SDRKAFCYLL VPSIHGLTRE ARQRLQAIEE FSELGSGFSI
AMRDLDIRGA GNLLGAEQSG FIEEIGFETY QQILDEAIRE LREEEFADVL GAPPPKPPET
SVDVEADAFI PETYVSSNVE RLNLYRRLSE ATDEAAIEAF REELADRFGP VPPEVDNLLW
AARLKLLGQA LRLPKVLFKN RRLFLEFPLQ DEDPHFYAHH FMPLLERLSQ LDRRYVLKDQ
NRKLRAIVQD VPDLETAYQV LRQLQPAEVP VS
//
