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Database: UniProt
Entry: A0A1G9RPT9_9SPHI
LinkDB: A0A1G9RPT9_9SPHI
Original site: A0A1G9RPT9_9SPHI 
ID   A0A1G9RPT9_9SPHI        Unreviewed;      1118 AA.
AC   A0A1G9RPT9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=SAMN05421813_108107 {ECO:0000313|EMBL:SDM25276.1};
OS   Daejeonella rubra.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Daejeonella.
OX   NCBI_TaxID=990371 {ECO:0000313|EMBL:SDM25276.1, ECO:0000313|Proteomes:UP000199226};
RN   [1] {ECO:0000313|Proteomes:UP000199226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24536 {ECO:0000313|Proteomes:UP000199226};
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; FNHH01000008; SDM25276.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9RPT9; -.
DR   STRING; 990371.SAMN05421813_108107; -.
DR   Proteomes; UP000199226; 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};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:SDM25276.1};
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:UP000199226}.
FT   DOMAIN          575..736
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          757..911
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1118 AA;  128071 MW;  7E2D3B22BFCE6DD1 CRC64;
     MNIRDILIQY KSDPRIAILA ETLNKGRKTR VHLKGLIGSS DSVIAIATYF LLHRHMIFVL
     PEREEAAYFL SDLESLLEKE VLFFPSSFRK SFEFTQVDSS NVLQRAEVLN ELNHASEFGK
     IIVTYPEALA EKVIDRQALE KNTLEISVGN KLSIEFINEF LIEYDFDRVD FVYEPGQFSV
     RGGIVDIFSF SHDLPYRIEF FADYIESIRT FEIEDQLSVE QVKSITVVPN VQSKFLTDHN
     ISLLEYIDQD SIIWFKDVEF TLDIVKTGFK KAVEFWNALA AEDKKQNPQW IDPKFNFTDE
     KMLADQLKDF DLLEFGKQFF YEADETIQFD TKPQPSFNKD FNLLIHNFKE NEKAGVENLI
     FTDSTKQIER LYSIFEDLKA GIQFKPIHLS LREGFIDHGQ KLACYTDHQI FDRYYKYKLK
     KGYIRSQAIT LKELRDLKPG DFITHIDHGI GKYAGLEKVD VNGRSQEMIR LVYADNDLLY
     VNINSLNRIS KYSGKEGTVP RMNKLGTDTW EKLKKTTKKK VKDIARDLIK LYAIRKSQTG
     TAFLPDTYLQ TELEASFIYE DTPDQVKATA DVKKDMESAH PMDRLVCGDV GFGKTEIAIR
     AAFKAVTDSK QVAILVPTTI LALQHFKTFT SRLKDFPCNI DYINRFKSAK QIRETLEKLA
     QGKVDIIIGT HRIVSKDVKF KDLGLLIIDE EQKFGVGVKE KLKQFRANVD TLTLTATPIP
     RTLHFSLMGA RDLSIISTPP PNRQPVVTEL HVFNEKLIKE AVEFEIDRGG QIFFIHNRVQ
     DLMQLGGLIN TLVPKARIGI AHGQLEGDAL EDVMLKFVGG EYDVLVATTI IEAGLDIANA
     NTILINHAHM FGLSDLHQMR GRVGRSNKKA FCYLLSPPLS TLTNEARKRL SAIEEFSDLG
     SGFNVAMRDL DIRGSGNLLG AEQSGFIAEI GFEMYHKILD EAIQELKDDE FKNLFSDEKP
     RPFISFTHVD TDLEVMIPDE YVTNIAERYN LYTELSNIED ELALDAFRQK MADRFGPVPQ
     QVIELINTWR LQHLGKMIGF EKISFKKGVL RGYFLTNKQS AYFETEQFGR VLSFLQAHPR
     ISNLKEVKNT LRLAIEHVQT LDIAIEMLQE IALIPEKI
//
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