ID D1B5L3_THEAS Unreviewed; 994 AA.
AC D1B5L3;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 87.
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 OrderedLocusNames=Taci_1072 {ECO:0000313|EMBL:ACZ19304.1};
OS Thermanaerovibrio acidaminovorans (strain ATCC 49978 / DSM 6589 / Su883)
OS (Selenomonas acidaminovorans).
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Thermanaerovibrio.
OX NCBI_TaxID=525903 {ECO:0000313|EMBL:ACZ19304.1, ECO:0000313|Proteomes:UP000002030};
RN [1] {ECO:0000313|EMBL:ACZ19304.1, ECO:0000313|Proteomes:UP000002030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49978 / DSM 6589 / Su883
RC {ECO:0000313|Proteomes:UP000002030};
RX PubMed=21304665; DOI=10.4056/sigs.40645;
RA Chovatia M., Sikorski J., Schroder M., Lapidus A., Nolan M., Tice H.,
RA Glavina Del Rio T., Copeland A., Cheng J.F., Lucas S., Chen F., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Chain P., Saunders E., Detter J.C., Brettin T., Rohde M.,
RA Goker M., Spring S., Bristow J., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Eisen J.A.;
RT "Complete genome sequence of Thermanaerovibrio acidaminovorans type strain
RT (Su883).";
RL Stand. Genomic Sci. 1:254-261(2009).
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}.
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DR EMBL; CP001818; ACZ19304.1; -; Genomic_DNA.
DR RefSeq; YP_003317586.1; NC_013522.1.
DR AlphaFoldDB; D1B5L3; -.
DR STRING; 525903.Taci_1072; -.
DR EnsemblBacteria; ACZ19304; ACZ19304; Taci_1072.
DR KEGG; tai:Taci_1072; -.
DR PATRIC; fig|525903.6.peg.1071; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_0_3_0; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000002030; Chromosome.
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; 3.40.50.300; 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 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; 2.
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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:ACZ19304.1};
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:UP000002030}.
FT DOMAIN 488..649
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 670..823
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 994 AA; 110479 MW; CA802CE67D8F4785 CRC64;
MIPRGIARAI GYGRLPVPDR FVVILPGWSD VVTLSSDLAC LGREVSPLLP PVPLGVKEGV
QAHLLHRGRV LEDWIRLGGG LITSAAGAVL PALSPSGHFQ LRKGDRCRSS LIHWISSQGY
ERVPVVWAPG QWALRGALVD LFPPGDRAIR VAFDDDLVEE IRVFSPETQR AVASLDSWEM
GGLKGGRSLT LLDVPVPFGL VVFEPGQVEI QCESAVWLWE QMREEIHSLP GAADWSSLAS
RVQGVIRVSS SQGDPSAMLE RVPNFAGRLK EAEGFVLDMR SKGFRTLFLG STRGYVEWAA
GCGMEVIRGS ASEGALDLSE RVLYLSEVDV AGVRPPSSPA GKPPADVLDS LISGDLMVHE
DYGVCRFLGI EMIEQGGVQQ DYIALEFAQG KRLLMPTYRI ARLYRYAGDP AEAELDSLKR
GRWSRSYQEA KEKAREAAER LLSAQARRHS ARGIAFDPLE REMEELRSTF PYRETVDQVR
CWEEIRADME RPVPMDRLLV GDVGFGKTEL ALRAAFKAAM SGYQVVVVTP TTLLASQHLS
TFASRLSPFP LRVEALYRFV PRSRQEEILN DFAEGRVDIL IGTHRILGDD VRARNLGLIV
LDEEHRFGVM QKERWRERFP GADVLMLSAT PIPRTLQLAL GGYKDISVMT TPPVDRRPVV
TVVSPWQDEL VKGAVLRELS RGGQVFWVHN RIQSMHRAFL RAKALLPGVR VEMAHGRMRD
SELESLMARF VEGRLDVLLC TTIIESGLDL PRVNTIIVED AHRMGLAQLY QLRGRVGRRS
DQAFALFLYP RGAEAGRALE RLEAIGSLEE LGSGFHLAMM DLSIRGGGEL LGTAQHGHVS
SLSPELYFQM LEREVTRLKG GAELPPVEWG YSPSIPEWYV EDQPLRVRLY RRLFLPMDAS
ELDQLRDEMV DRFGPVPHQV EELILAARLR VLLAGLASEI TIGRDQVQVR FRDSAAVPKG
LPPIWRVKGV VTVGPAGVRG LSELIEALSR WVTV
//
