ID A0A1H7YXW2_9SPHN Unreviewed; 1190 AA.
AC A0A1H7YXW2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN05192583_0452 {ECO:0000313|EMBL:SEM50843.1};
OS Sphingomonas gellani.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1166340 {ECO:0000313|EMBL:SEM50843.1, ECO:0000313|Proteomes:UP000199206};
RN [1] {ECO:0000313|Proteomes:UP000199206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S6-262 {ECO:0000313|Proteomes:UP000199206};
RA Varghese N., Submissions S.;
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; FOCF01000001; SEM50843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7YXW2; -.
DR STRING; 1166340.SAMN05192583_0452; -.
DR Proteomes; UP000199206; 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.
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:UP000199206}.
FT DOMAIN 659..820
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 841..995
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1190 AA; 129871 MW; 25CA926F2A455A91 CRC64;
MGWAGHGKDA DADLRPPAPL IHKSTLPRCI GPDDLPDIKT ILSATRPLTL SGVPTGFLPS
LLADLARAAS GRAVFIAPDD AAMRAVASTA PFFAPELEVI QFPAWDCLPY DRASPTLRVM
AERIAALHRL QAKAKGPQLL LTTANAATQR VLTPFRIRQL VANLKPGERI DLNRLSALLQ
ANGYVRTDTV HDAGEYAVRG GIVDLFPSGE EQALRLDFFG DEIESVRTFS PEDQRTTGRI
DGFTLLPASE ALLDEESIKR FRTRYRETFG ATATGDPLYQ AVSDGRRLAG MEHWLSLFEE
RLATLFDHIG DGDVVVRDAG VPGAAQGRLE AIADYYENRK RAEGAQPGSY RPLPAKVLYL
DTAEWKDGLD ARRAHLTSPF HEPESATVLD FGVDGARDFA PERAASENVY EAVAKHVAKL
RKDGRKPILA SYSAGARERL AGLLKDHGLA GLKAVDGWQD ALGHADTSKT AGAALVVLPL
DHGFTAPGVA VLTEQDMLGD RLVRRAKRRK SADAFLAEIA SLTPGDLVVH TEHGIGRYNG
LTSVPVGKSP HDCVALEYAG GDKLYVPVEN LEVLSRYGSG EDGAALDRLG GEAWQRRKSR
MKERIREIAG ELIAVAAERA LRPGEVAEPD PSGYPTFVDR FPYQETEDQD RAIDDVLSDL
GAGKPMDRLV VGDVGFGKTE IALRAAFVAA LGGMQVAVVC PTTLLARQHY NNFKARFEGF
PIEIGRLSRL VTATEAKKTR DQLADGTIDV VVGTHAILAK AIDFKRLGLV IVDEEQRFGV
THKERLKALK ADVHMLTLTA TPIPRTLQMA MSGIRELSVI QTPPVDRLAV RTYIMPWDPV
VLREALLREH YRGGQSFLVT PRIADLPDIE EFLRNEVPEV RYVVAHGQMS PTEVEERMSA
FYDKKFEVLI STTIVESGLD IPSANTMIVN RADRFGLAQL YQLRGRVGRS KTRAYCYLVT
PPERQMTEAA DKRLKVLSDL DSLGAGFQLA SHDLDIRGAG NLLGDEQSGH IKEVGYELYQ
SMLEEAIMDA KAGGLTSNRP KDFSPQITVD APILIPEDYV PDLDLRMGLY RRLNDLDKAQ
EVEAFAAELI DRFGPLPDAT ENLVSVIQIK LNAKKACIAK MDVGQKGVLV SFHNDSPPNV
AGLIAYVDRL GGVAKLRPDA KLVLQRAWPD AKARLNGALS LSKGLAKAAG
//
