ID A0A017HGB2_9RHOB Unreviewed; 1189 AA.
AC A0A017HGB2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 ORFNames=Rumeso_04638 {ECO:0000313|EMBL:EYD73517.1};
OS Rubellimicrobium mesophilum DSM 19309.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=442562 {ECO:0000313|EMBL:EYD73517.1, ECO:0000313|Proteomes:UP000019666};
RN [1] {ECO:0000313|EMBL:EYD73517.1, ECO:0000313|Proteomes:UP000019666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19309 {ECO:0000313|EMBL:EYD73517.1,
RC ECO:0000313|Proteomes:UP000019666};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYD73517.1}.
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DR EMBL; AOSK01000130; EYD73517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A017HGB2; -.
DR STRING; 442562.Rumeso_04638; -.
DR PATRIC; fig|442562.3.peg.4568; -.
DR HOGENOM; CLU_005122_3_3_5; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000019666; Unassembled WGS sequence.
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; 3.40.50.11140; -; 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:UP000019666}.
FT DOMAIN 612..773
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 794..948
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1144..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1189 AA; 131059 MW; B81E5236D23C57C4 CRC64;
MATSPNHITV GGAPEGFDAR LVLKELEAAG VPVLHVARDD RRLAAMREAL RFFDPSVPVF
EFPAWDVLPF DRVSPNPEIA AQRMATLAAL THGMPERFVL LTTLNAATQR VPARETLRGA
AFSAGVGDRV DEQQLRGFLT RMGFTQSPTV TEPGDYAVRG GLIDVWPPGH PSPVRLDFFG
DTLDGARRFD AVTQRTTEKL SVVEFAPVSE VILDEASITR FRQNYRIEFG AAGTDDPLYE
AVSAGRKHAG MEHWLAFFHE RLETLFDYLP KASVTLDDQV GPSRLARWAA IEDAYEARRS
AMRERGRVDT VYKPAPPGLL YLDEAAWDAA LKGLRVLQFN PLKQPTGYGV IDAGGRIGRD
FAPERQQEKI SLFGALAAHV KARLAEGPVL VASYSEGSRE RMEHLLEEEG TGETIPVPDF
SRVGRNGIHL AVWPLEHGFE APGLTVISEQ DVLGDRLIRP TRKKRRAENF LTEVNALTPG
DLVVHVDHGV GRYHGLEVLQ ALGAAHECIA LEYAENTRLY LPVENIELLS RFGHEEGLLD
KLGAGAWQAR KAKLKERIKI AAERLIRTAA ERALRKAPEL EPPEDIWDQF LARFPYVETD
DQLQAIEDVL GDMDSGNPMD RLICGDVGFG KTEVAIRAAF VAAMSGVQVA VVAPTTLLAR
QHYKTFAERF RGFPLEVRPL SRFVSAKEAA QTREGLAKGT VDIVVGTHAV LAKQVRFANL
GLLVIDEEQH FGVSHKERLK ELRSDIHVLT LTATPIPRTL QMSLSGVRDL SVITTPPIDR
LAIRTYVSEF DTVTIREALL RERYRGGQSF VVVPRIADLP EMEDWLKREV PEASYVVAHG
QMAATELDDK MNAFYDGKFD VLLATSIVES GLDIPTANTM VVWRADAFGL AQLYQIRGRV
GRSKTRAYAY LTTRPRQKLT PQAERRLRVL GSIDSLGAGF QLASQDLDIR GAGNLIGEEQ
SGQIREVGFE LYQQMLEEEI DRLRSGQGEL VETAGQWAPQ LNLGVPVLIP EAYVPDLDVR
LGLYRRLSAL STKVELEGFA AELIDRFGTL PREVNTLLLV VRIKAMARKA GVARLDAGPK
GATLVFHNDR FASPAGLVEY IQAQAGQARI KDNKLVVLRD WPSEADRIKG AFAIVRDLAE
KVAEASPRKG KEAVDAEAGP KASKPAALPG MKAETASSAK PSPVARRRG
//
