ID G2ECZ4_9FLAO Unreviewed; 1118 AA.
AC G2ECZ4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
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 ECO:0000313|EMBL:EGV43691.1};
GN ORFNames=BZARG_1264 {ECO:0000313|EMBL:EGV43691.1};
OS Bizionia argentinensis JUB59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Bizionia.
OX NCBI_TaxID=1046627 {ECO:0000313|EMBL:EGV43691.1, ECO:0000313|Proteomes:UP000003730};
RN [1] {ECO:0000313|EMBL:EGV43691.1, ECO:0000313|Proteomes:UP000003730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUB59 {ECO:0000313|EMBL:EGV43691.1,
RC ECO:0000313|Proteomes:UP000003730};
RX PubMed=18842857; DOI=10.1099/ijs.0.65599-0;
RA Bercovich A., Vazquez S.C., Yankilevich P., Coria S.H., Foti M.,
RA Hernandez E., Vidal A., Ruberto L., Melo C., Marenssi S., Criscuolo M.,
RA Memoli M., Arguelles M., Mac Cormack W.P.;
RT "Bizionia argentinensis sp. nov., isolated from surface marine water in
RT Antarctica.";
RL Int. J. Syst. Evol. Microbiol. 58:2363-2367(2008).
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:EGV43691.1}.
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DR EMBL; AFXZ01000019; EGV43691.1; -; Genomic_DNA.
DR RefSeq; WP_008636593.1; NZ_AFXZ01000019.1.
DR AlphaFoldDB; G2ECZ4; -.
DR STRING; 1046627.BZARG_1264; -.
DR PATRIC; fig|1046627.3.peg.1397; -.
DR eggNOG; COG1197; Bacteria.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000003730; 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:UP000003730}.
FT DOMAIN 573..734
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 743..909
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1118 AA; 127870 MW; 1AFBBDA8641F1605 CRC64;
MSKSILAQKY AQALQMQNLQ VAIAQTENRT HLKGLVGSAF SLVISEAFKK ADKPFLLVFN
DKEEAAFYLN DLEALLNDKD VLFYPGSYRR PYQIEETDNA NVLLRSEVLN RINSRKKPAI
IITYPDALFE KVVTRRELEK NTLKIAINDN LSIDFVNEVL FEYKFKRVDF VTEPGEFSVR
GGIVDVFSFS NDEPYRIEFF GDDVDSIRTF DVETQLSIDQ IKKISIIPNV ANKFLDESRQ
SFLKYIAQKT VIFTKNTQLV FDRIDDFYTK AEDAFKNLTS ELKHAQPEEL FCNATLLKKQ
LLDFNIVEFG SKAVFINSEK AEQTISFNTT PQPSFNKQFN LLIEDLNLHH DRGYTNYIAC
VSEQQAKRFH DIFDDAEETV HYKTIVLTLY QGFVDHDNKI TCYTDHQIFE RYHKFHLKNG
YAKKQAITLK ELTNLDIGDY VTHIDHGIGK FGGLQKIDVE GKKQEAIKLI YGERDILYLS
IHSLHKITKF NGKDGKPPKV YKLGSKAWKT LKAKTKSRVK EIAFNLIQVY AKRKLERGYQ
YHPDSHMQHE LEASFIYEDT PDQSTATADV KADMESERPM DRLVCGDVGF GKTEVAIRAA
FKAVDNGKQV AILVPTTILA YQHSRTFRER LKEFPVTVDY LNRFRTAKEK RETLANLEAG
SVDIIIGTHQ LVNKNVKFKD LGLLIVDEEQ KFGVAVKEKL KTLKDNVDVL TLTATPIPRT
LQFSLMAARD LSVITTPPPN RYPIESHVVR FSEETIRDAV TYEIQRGGQV FFIHNRIENI
KEVAGLIQRL VPDAKIGIGH GQMEGKKLEQ LMLAFINGEF DVLVSTTIVE SGLDVPNANT
IFINNANNFG LSDLHQMRGR VGRSNKKAFC YFITPEYSAM TEDARKRITA LEQFSELGSG
FNIAMKDLEI RGAGDLLGGE QSGFINDIGF DTYQKILNEA IDELKQTEFA DLYEDDGKEK
EYVKDITIDS DFELLFPDDY VNNIAERLNL YTKLNEVKTE AELVKLESEI RDRFGEFPTQ
VVDLLNSVRI KWVATKMGLE KVVMKQGKLI GYFITDQKSG FYQSPNFTRV LQFVQSHPQA
CKMKEKQTRN GLRLLLTFEN IKTVDKALKA LKPILNVD
//
