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Database: UniProt
Entry: A0A095VPP8_9GAMM
LinkDB: A0A095VPP8_9GAMM
Original site: A0A095VPP8_9GAMM 
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
//
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