ID H1Q1V0_9BACT Unreviewed; 1147 AA.
AC H1Q1V0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
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=HMPREF9140_00888 {ECO:0000313|EMBL:EHO71570.1};
OS Prevotella micans F0438.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=883158 {ECO:0000313|EMBL:EHO71570.1, ECO:0000313|Proteomes:UP000016023};
RN [1] {ECO:0000313|EMBL:EHO71570.1, ECO:0000313|Proteomes:UP000016023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0438 {ECO:0000313|EMBL:EHO71570.1,
RC ECO:0000313|Proteomes:UP000016023};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA Blanton J.M., Wade W.G., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella micans F0438.";
RL Submitted (DEC-2011) 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:EHO71570.1}.
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DR EMBL; AGWK01000027; EHO71570.1; -; Genomic_DNA.
DR RefSeq; WP_006952012.1; NZ_JH594521.1.
DR AlphaFoldDB; H1Q1V0; -.
DR STRING; 883158.HMPREF9140_00888; -.
DR PATRIC; fig|883158.3.peg.895; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_10; -.
DR Proteomes; UP000016023; 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; 3.40.50.11180; -; 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:UP000016023}.
FT DOMAIN 603..764
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 785..939
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1147 AA; 130889 MW; 8B790B36BAA919C1 CRC64;
MNIQDIKNRY ATSAEAMALQ TMLAKNSKET LYLRGLVASS APMLFATIAG KINRTILFVL
NDNDEAGYFY NDLKTIIASE SDDSIARVLC LPSSYKRSVK YGQRDSANEI LRTEVMAALG
AFNNKSRTSL FIVTEPSAIA ELVVSKKRID EQTISLRKGG RKDIVDLEKQ LLKLGFRRVD
YVYEPGHFAL RGSILDVYSF SSELPFRIDF FGDEIDSIRT FEIENQLSLE QRERIEILPE
LSSTPSGKVP FFELLPKDAL LVTKDFKYMC QAVGRIYEEG FSAKALDEQL ANHTETEQQE
IRKELQRELQ LVSPTWFTEL AEHFRRVEFG ASSTIEASKR EENNAVLTFD IMAQPLFHKN
FELLARTLRD YIAKGYKLYI LADSKKQTDR LHDIFDTMDS SHRATPIPFT PINQTLHEGF
INNTQKECFF TDHQIFDRFH KYNLKSDKAR LGKAALTMKE LQEMDPGDFL VHIDFGIGKF
AGLVRVPSGE SYQEVIRLVY QRGDIVDVSI HSLYKISKYR RAESNEPPQL SVLGSGAWER
LKEKAKKNIK NIARDLIKLY ARRQHEKGFA FSPDSFMQHE LEASFFYEDT PDQLKATNEI
KQDMESSRPM DRLVCGDVGF GKTEVAIRAA FKAAADNKQV AVLVPTTVLA FQHYRTFTYR
LENMPVRVDY FSRARTARQT KQVLTDLAEG KIDILIGTHK LISKNIVWKD LGLLIIDEEQ
KFGVTTKEKL RQLRTNIDTL TLSATPIPRT LQFSLMGARD MSIMRIPPPN RHPVWTEIST
FSHEVIADAI NFEMSRNGQT FIVNRRISQL PQLASMIKKY VPDCRVAIGH GQMKPEELED
IVMGFINHDY DVLVSTTIVE SGVDIPNANT IIINDAHQFG LSDLHQMRGR VGRANKKAFC
YLIAPPLAAL SVDARRRLEA LETFSELGSG FSIAMQDLDI RGAGNLLGTE QSGFMQELGY
ETYQKILRQA VNELRNDEFQ DLIESNASGN STTDFVDDCA IESDLEMYFP ETYVPGSSER
MLLYRELDTI ECDDDLLQYR KRMEDRFGPI PKQGEELLQV VLLRRIGKKL GCEKIILKQN
FMQLQFVSIP TSFYYRSKAF GKILTFITSQ PRRCNLKEKN NKRSMLITEV PTVTAAVEIL
KEIESLD
//
