ID A0A158JBA9_9BURK Unreviewed; 1157 AA.
AC A0A158JBA9;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-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=AWB68_03686 {ECO:0000313|EMBL:SAL66087.1};
OS Caballeronia choica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=326476 {ECO:0000313|EMBL:SAL66087.1, ECO:0000313|Proteomes:UP000054770};
RN [1] {ECO:0000313|Proteomes:UP000054770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Peeters C.;
RL Submitted (JAN-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; FCON02000038; SAL66087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158JBA9; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000054770; 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}.
FT DOMAIN 620..781
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 802..956
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1157 AA; 128710 MW; B1923B08BBD4609F CRC64;
MPSKAVTSQS TSPIALVKAG QRFVFDGATG SSDALAIARY HLAHREQVPL LTVLCASAVD
AQRLAAEIPY FAPDARVRLL PDWETLPYDT FSPHQDLVSE RLATLHDLGV GRCDILLVPA
TTALYRMPPA SFLAAYTFSF TQGERLNEAK LKAQLTLAGY EHVSQVVRPG EYCVRGSLLD
LFPMGSPLPY RIDLFDDQVD SIRAFDPDTQ RSLYPVRDVR LLPGREFPFD EASRTAFRSR
WREVFEGDPS RSSIYKDIGN GVPSAGIEYY LPLFFDETAT LFHYLPEGAQ LVFIGDMDAS
IKRFTNDTRQ RYNFLGHDRE RPLLEPRRLF LTDDDFFAFA KPFAQLKFPP APEGGWAVPL
PGLALDRHAD EPLLALSHYL DQTPNRVMLV AESAGRRETI QQMLAEHGLR AALDDTFQQW
LAGDAKFSLG VAPLANGFAL PGEELAIVTE TELYGPLARR TGRRRQEQAS NVDSMVRDLS
ELKIGDPVVH TQHGIGRYMG LVSMDLGEGE TEFLHLEYQN ESKLYVPVAQ LHVISRYSGA
DPDSAPLHAL GSGQWEKAKR RAAQQIRDTA AELLNLYARR AAREGYAFKL EPRDYTKFAE
SFGFEETPDQ AAAITAVIGD MTSGKPMDRL VCGDVGFGKT EVALRAAFIA VMAGKQVAIL
SPTTLLAEQH TQTFTDRFAD WPVRIAELSR FKSTKEIAAS IAAINEGTID IVIGTHKLLS
SDVQFKRLGL VIIDEEHRFG VRQKEALKAL RAEVDVLTLT ATPIPRTLGM ALEGLRDFSV
IATAPQKRLA IKTFVRREED GVIREAMLRE LKRGGQVYFL HNEVETIENR RTMLEALVPE
ARIAVAHGQM HERELERVMR DFVGQRANVL LCTTIIETGI DVPSANTILL HRADKFGLAQ
LHQLRGRVGR SHHQAYAYLL VHDPAVLTKQ AQRRLEAIQQ MEELGSGFYL AMHDLEIRGT
GEVLGDKQSG EIQEIGFQLY TDMLNDAVKA LKEGREPDLN APLAATTEIN LHAPAILPAD
YCGDVQERLS LYKRLANCES SDSIDGILEE LIDRFGKLPP QAHALVETHR LRLAARPLGI
VKIDAAELVI GLQFIPNPPV DAMKIIEMVQ KHKHIKLAGQ DKLRIETRSP DLSVRIATVK
ETLRALGAPV RQAAPAR
//
