ID A0A426CI87_9BACT Unreviewed; 811 AA.
AC A0A426CI87;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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:RRJ95803.1};
GN ORFNames=Ga0100231_017515 {ECO:0000313|EMBL:RRJ95803.1};
OS Opitutaceae bacterium TAV4.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=278959 {ECO:0000313|EMBL:RRJ95803.1, ECO:0000313|Proteomes:UP000078325};
RN [1] {ECO:0000313|EMBL:RRJ95803.1, ECO:0000313|Proteomes:UP000078325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAV4 {ECO:0000313|EMBL:RRJ95803.1,
RC ECO:0000313|Proteomes:UP000078325};
RA Rodrigues J., Kotak M., Lin J.;
RT "Draft genome sequences of strains TAV3 and TAV4 (Verrucomicrobial:
RT Opitutaceae) isolated from a wood-feeding termite and in silico analysis of
RT their polysaccharide-degrading enzymes.";
RL Submitted (NOV-2018) 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:RRJ95803.1}.
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DR EMBL; LXWU02000003; RRJ95803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A426CI87; -.
DR STRING; 278959.Ga0100231_09720; -.
DR Proteomes; UP000078325; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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 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 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|HAMAP-Rule:MF_00969};
KW DNA repair {ECO:0000256|HAMAP-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:UP000078325}.
FT DOMAIN 246..407
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 416..582
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 811 AA; 90148 MW; 6022202FA6501480 CRC64;
MGATPATPSS APSPKTPKNT APANSSPPTP PLPAPPKKTP PPFRPRHRQR RLPPPLHPLD
LPPPPPLVFL TETELFGRQR TRHAASATLA RKTVHRAQVD QLLDFAELVE GDHVVHLQHG
IAIYRGLTRI DVNASIREVI TLEFDEGVTL HVPLQESHLI SRYVGLSKAR PQLGKIGSNR
WEKTRRAAEH ATIDLAAELL RIQAAREAQP GHAFDPDNDW QKEFEAAFPF TETPDQLRAI
TETKADMERP RPMDRLICGD VGFGKTEVAI RAAFKAVQSG RQVVLLVPTT VLAQQHLNTF
RERMAGYPLV VEMVSRFRTR GEITRILAAT AAGQVDILVG THRILNKDVV FRDLGLVIID
EEQRFGVQHK ERLKAMRATV DVLSMSATPI PRTLYMAMTG ARDMSVIETP PTNRHPIQTI
VKTYDEKLVT DAIRAELSRG GQVFYLHNRV QTIDLVAARL AQLLPDVKIA TGHGQMSEHA
LERMMTEFVA GDYQVLVCTT IIETGLDIPN CNTIIIEGAD RFGLSQLYQL RGRVGRFKHQ
AYAYLLLHRH TRLMDVARER LNALRTHNQL GAGFRIAMRD LELRGAGNLL GPQQSGHIVG
VGFELYCQLL RQSVARLKGE KTAARHRASV KLDFVYVGES GEARDQKPET KGQSSQTSYA
AIKAAESAAA GSVAVEPIQA RLPHAYIGET RLRIDFYRRL ALAETPAQLT QIETDLRDRF
GDYAPTPHSD PVRALLLLTE IRIRAEEKNL ILIETQGSIL KCVRAPAGPG RPGEFVQLGT
RFPRLTAPKP LLRLREILTF LQNLSDSPAT T
//
