ID A0A1H2CGS2_9SPHI Unreviewed; 1130 AA.
AC A0A1H2CGS2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN05216490_5045 {ECO:0000313|EMBL:SDT69641.1};
OS Mucilaginibacter mallensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=652787 {ECO:0000313|EMBL:SDT69641.1, ECO:0000313|Proteomes:UP000199679};
RN [1] {ECO:0000313|EMBL:SDT69641.1, ECO:0000313|Proteomes:UP000199679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP1X4 {ECO:0000313|EMBL:SDT69641.1,
RC ECO:0000313|Proteomes:UP000199679};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; LT629740; SDT69641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2CGS2; -.
DR STRING; 652787.SAMN05216490_5045; -.
DR Proteomes; UP000199679; Chromosome i.
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 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; 3.
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:UP000199679}.
FT DOMAIN 588..749
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 770..924
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1130 AA; 128786 MW; 80573F2AD9A721FA CRC64;
MSGNAFFAYL RIVLNIRDIL DRYKADERIK ALAQALNASK SPRVQLRGLV GSSDSAMAVA
LYFLQHQHMV FVLPDREEAG YFQADLENLT GKEVLLFPSS YRKAFEFTQP DSSNVLARAE
VLNELNHSSE FGQLIVTYPE ALAEKVIDRA SLEKNTLEIS VNNKLSIDFI NEFLVEYDFD
RVDFVYEPGQ FSVRGGIVDI FSFSHELPYR VEFFGDLIES IRTFEIESQL SVEQVKSITI
VPNVQSKFLT ESNISLLEYV DAGTQIWIKD VQFTLDIIQD GYKKATQLWK ALSADEKNQN
PDWIDPKFGF TDEKLISSQL GDFPVVEFGK QFFYQPDAAI NFDMRPQPSF NKDFSLLIHN
FKNNEAEQIE NFILTDSARQ VERLYAILED LDKTVKFTPI SISIREGFVD HEQKLACYTD
HQIFDRYYKY KLKKGYQRSQ AITLKELREL KPGDYVTHID HGIGKYNGLE KIEVNGKMQE
MIRLLYADND LLYVNINSLN RISKYSGKEG AVPKMNKLGT DTWERLKKTT KKKVKDIARD
LIKLYAVRKT QLGNAFSPDS YLQTELEASF LYEDTPDQEK ATSDFKKDME SPHPMDRLIC
GDVGFGKTEV AVRAAFKAVA DSKQVAILVP TTILAAQHYK TFSDRLKGFP CNIDYVNRFK
SSKQIKETLE KLKEGKVDII IGTHRLVSKD VKFKDLGLMI IDEEQKFGVS TKEKLKQMRA
NVDTLTLTAT PIPRTLHFSL MGARDLSIIS TPPPNRQPVV TELHVFNDKL IKEAVEFEIN
RDGQVFFIHN RVADLPQLGG MIHKLVPKAR VGIAHGQLEG DALEDVMLKF VNGEYDVLVA
TTIIEAGLDI PNANTIIINH AHMFGLSDLH QMRGRVGRSN KKAYCYLLSP PLSTLTSEAR
KRLSAIEEFS DLGSGFNVAM RDLDIRGSGN LLGAEQSGFI AEIGFEMYHK ILDEAIQELK
EDEFKGVFPE DKPRPFIAFT QIDTDLEILI PNEYVTSLSE RYNLYSEMAK LENEFDLEAF
QQQLHDRFGP IPRQVNDLLN TMRLQWLGKA IGFEKISLKK NVLRGYFITN QQSPYFETPV
FRQVLNFVQA NPRRTNLKEV KNTLRLSIEG VNGIDEAIEL LSDIVEPVGV
//
