ID A0A1G7S333_9RHOB Unreviewed; 1159 AA.
AC A0A1G7S333;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN04489759_10564 {ECO:0000313|EMBL:SDG16859.1};
OS Sulfitobacter delicatus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=218672 {ECO:0000313|EMBL:SDG16859.1, ECO:0000313|Proteomes:UP000199399};
RN [1] {ECO:0000313|EMBL:SDG16859.1, ECO:0000313|Proteomes:UP000199399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16477 {ECO:0000313|EMBL:SDG16859.1,
RC ECO:0000313|Proteomes:UP000199399};
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; FNBP01000005; SDG16859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7S333; -.
DR STRING; 218672.SAMN04489759_10564; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000199399; 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; 3.40.50.11180; -; 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; 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; 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 611..772
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 793..947
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1159 AA; 127745 MW; A6D88503445831DC CRC64;
MNDPRNITLS GVPEGFDARA ILNEVAKGGQ PVAHVARDDK RMAAMQAALR FFAPDMPVVT
FPSWDCLPYD RVSPNADISA QRMATLAALV HGMPEKFVLL TTLNAATQRI PARATLRDAA
FAAQVGSRID ESALRNFLVR MGFVQSPTVM EPGDYAVRGG IIDIYPPGDL GPVRLDLFGD
VLDGARRFDP ATQRTTEKLD MIELAPVSEV ILDDAAITRF RQNYRIEFGA AGTDDPLYEA
ISAGRKHQGA EHWLSFFQDD LETLFDYLPN ATVTLDDQLT PMRLARWDTI ADQYETRQLA
MKTRSKMDSV YKPAPPEGLY LTDDAWQQAL LGRRVIQFNP LPQPTGPGVL DAGARIGRNF
APERQQESVS LFGALASHIK AKLDAGPVLI ASYSEGARER LTGLIEDEGL AEAIPVTDAT
RIGKRGLHLA VWALEHGFEA PGMTVISEQD VLGDRLIRAP KRKRRAENFL TEAQSLSPGD
LVVHVDHGIG RYHGMEVVTA AGAAHECLVL EYAEQSKLYL PVENIELLSR YGHEEGLLDK
LGGGAWQSKK AKLKERIREM ADKLIRIAAE RALRKAPVLD PPPGMWDAFS ARFPYTETDD
QLRAIGDVID DLTSGNPMDR LVCGDVGFGK TEVAMRAAFV AAMSGVQVAV IAPTTLLARQ
HYKSFAERFR GFPIEVRQLS RFVSAKEAAA TRDGMAKGTV DIVIGTHALL AKGIRFKDLG
LLVIDEEQHF GVGHKERLKA LRTDIHVLTL TATPIPRTLQ LSLTGVRDLS VIGTPPVDRL
SIRTYVSEFD AVTIREALLR EHYRGGQSFY VVPRLSDLRE IEDFLQAQLP ELTYVVAHGQ
MAPGELDDRM NAFYDGKFDV LLATTIVESG LDIPTANTMV VHRADMFGLA QLYQIRGRVG
RSKTRAYAYL TTKPRAKLTD TAQKRLRVLG SLDTLGAGFT LASQDLDIRG AGNLLGEEQS
GQMRDVGFEL YQSMLEEAIA KIRTGEMEGL SEADEQWAPQ INLGVPVLIP EDYVPDLDVR
LGLYRRLSEL STKVELEGFA AELIDRFGKL PKEVNTLMLV VRIKAMCKRA GIAKLDGGPK
GATIQFHNDK FASPEGLVQF IQDQRGLAKV KDNKIVVRRD WKSDADKIKG AFAIARDLAE
HVVAKQKKAK KAKKAKAEG
//
