ID A0A095VPP8_9GAMM Unreviewed; 1153 AA.
AC A0A095VPP8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-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=HRUBRA_02056 {ECO:0000313|EMBL:KGE03370.1};
OS Pseudohaliea rubra DSM 19751.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Pseudohaliea.
OX NCBI_TaxID=1265313 {ECO:0000313|EMBL:KGE03370.1, ECO:0000313|Proteomes:UP000029640};
RN [1] {ECO:0000313|EMBL:KGE03370.1, ECO:0000313|Proteomes:UP000029640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19751 {ECO:0000313|EMBL:KGE03370.1,
RC ECO:0000313|Proteomes:UP000029640};
RX PubMed=25414506;
RA Spring S., Fiebig A., Riedel T., Goker M., Klenk H.P.;
RT "Genome Sequence of Gammaproteobacterial Pseudohaliea rubra Type Strain DSM
RT 19751, Isolated from Coastal Seawater of the Mediterranean Sea.";
RL Genome Announc. 2:e01208-14(2014).
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:KGE03370.1}.
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DR EMBL; AUVB01000057; KGE03370.1; -; Genomic_DNA.
DR RefSeq; WP_035517313.1; NZ_KN234777.1.
DR AlphaFoldDB; A0A095VPP8; -.
DR STRING; 1265313.HRUBRA_02056; -.
DR PATRIC; fig|1265313.6.peg.2028; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_0_3_6; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000029640; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000029640}.
FT DOMAIN 617..778
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 799..953
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1153 AA; 127125 MW; BACFB66A09E2A5BD CRC64;
MFRDKLLATP WPARAGTRTA IGPFPGSAAS ACIAELADDS RLLLVVAEDT QAALALEREL
PFFVTPGTEV LALPDWETLP YDHFSPHQDI VSERLETLYR LPSLATGILI VPIATLMHRL
PPRDYVLGAS LLLELGSALD VDRFRRRLER SGYRHVETVY EHGEFALRGA LVDIFPMGSP
LPYRIDLLDE EVDTLRTFDP ETQRTVDRMD AVRLLPAREF PLTREAISCF QQQWYEQFEG
DPDQSTVFTE VSAGRVPGGC EYYLPLFFEH CETLFEYLPD DTAVITVGRH YEAAQRFWGE
ITERHSEYGI DLRRPLLPPP AGFLPVEELY GQLKGHAVLE LRLDSDAPVH VDSAVLEPPR
SEDDSRTELP SRLTALTEGH SGPVLLCAES AGRREVLLEA LAANGLAPVA VDSWPAFLAD
PVPLAIAVAP IDRGLYLGPG APMLLCEAQL YGTRVAQRRR RKREAAVDPD AVFRDLNELR
PGAPVVHLEH GVGRYVGLSN LAVDGADAEF LTLEYADGAR LYVPVAALHL ISRYSGSEPE
LAPLHRLGSG QWERARRKAS EKASDVAAQL LEVYARREAR AGFAFGCPRE DYERFAAAFP
FEETPDQEAA IAAVLSDMES ERVMDRLVCG DVGFGKTEVA MRAAFVAVAA GKQVAMLVPT
TLLAQQHHSS LADRFADWPH RVEVLSRFRT ATEVRQIGER MAAGEIDILV GTHKLLQSDF
RFKDLGLLII DEEHRFGVKQ KEAIKALRAQ VDILTLTATP IPRTLNMALG GMRDLSIIAT
PPARRLSIKT FVREQSAALV KEAVLRETLR GGQVFYLHNE VRTIEETARK LRELLPDLSI
AVAHGQLRET ELERVMADFY HKRAHVLVCT TIIETGIDIP NANTIILERA DRFGLAQLHQ
LRGRVGRSHH QAYAYLLCPP RSAMTADAAK RLDAIEAAGD LGAGYQLATH DLEIRGAGEL
LGDEQSGQIQ SVGFGMYLEM LQRAVAALRR GEIPDLDAPL SAGTEINLHV PALIPEDYLP
DTNTRLVLYK RIAAAGAEAA LRDLQVEMID RFGLLPAPVK QLFIIARLRI AAEPLGISSL
ELGPEGGTIE FRESTTIDPM SLVTLVQGDP AGYQLAGATR LRIRAALPEP TQRVTLAEQL
FDRFAAGVNA PAA
//