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Database: UniProt
Entry: Q0FGQ8_9RHOB
LinkDB: Q0FGQ8_9RHOB
Original site: Q0FGQ8_9RHOB 
ID   Q0FGQ8_9RHOB            Unreviewed;      1151 AA.
AC   Q0FGQ8;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 87.
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=OM2255_03615 {ECO:0000313|EMBL:EAU52581.1};
OS   Rhodobacterales bacterium HTCC2255.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX   NCBI_TaxID=367336 {ECO:0000313|EMBL:EAU52581.1, ECO:0000313|Proteomes:UP000009381};
RN   [1] {ECO:0000313|EMBL:EAU52581.1, ECO:0000313|Proteomes:UP000009381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2255 {ECO:0000313|EMBL:EAU52581.1,
RC   ECO:0000313|Proteomes:UP000009381};
RA   Giovannoni S., Cho J.-C., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (SEP-2006) 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:EAU52581.1}.
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DR   EMBL; AATR01000001; EAU52581.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0FGQ8; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_1_3_5; -.
DR   OrthoDB; 9804325at2; -.
DR   BioCyc; RBAC367336:G1GNW-168-MONOMER; -.
DR   Proteomes; UP000009381; 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:UP000009381}.
FT   DOMAIN          615..776
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          797..951
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1151 AA;  128892 MW;  9C0FA90B13FD6296 CRC64;
     MNSFSKNIIN LSGAPDGFDA NILSNFITEK QKSIIFVARD DKRLDLMRKS LWFFSPNIPI
     LDFPSWDCLP YDRVSPNADV SSARMATLAA LSSGFEAPIV LLTTLNAITQ YIPNRTIVSN
     NSFVAIVGRT INVKELRAYF SKMGFVQTPT VTEPGDYAIR GGIIDVFPPG ESGPVRMDLF
     GDELESARRF DPVTQRTVEN LDRIEFAPVS EVILDDVSIN RFRNNYRKEF GSAGLDDPLY
     EAISAGRKHQ GYEHWAPYFH DGMETIFDHL PNAVIFMDEN IERIHTSRWD GINDQYEARL
     EALNSKNRLE TVYKPIKPEL FYVSPDDLFD LLNNREQRKF IVLPQPTGPN SLDMRARIGR
     NFAPERQNEE LGLFEEFAKH IIEKRKSTSV IIASMSLGAR ERLYGLLQDQ GLSGMVNIKT
     WKDINQSIGS ISLAVWHLEH GFEAPGLTII SEQDVLGELI IRKTNKKRRA KDFLTEASSL
     SVGDLVVHVD HGVGRYRGLE TVKAAGAPHD CLLLEYANND RLYLPVENVE LLSRYGHETG
     LLDRLGGSAW QAKKAKLKER IREMADKLLR IAAERSLRKS EILEVSPDKW NAFCARFPYV
     ETDDQLNAIE DVVSDMSSGK PMDRLICGDV GFGKTEVALR AAFIAASAGT QAAIIAPTTL
     LARQHFKSFE ERFRGTGIRV KQLSRFVTTS QMKKNREALR DGAVEIIIGT HALLAKDIKF
     ANLGLLIIDE EQKFGVGHKE RLKQLRSDIH VLTLTATPIP RTLQLSLSGV RELSVIGTPP
     IDRLAIRTYV SEFDTVTLRE ALLREHYRGG QSFFVVPRIS DLPEIEAFIE EQVPEINHVV
     AHGQMPAGEL DERMNAFYDG KFGILVATTI VESGLDIPTA NTIIIHRADM FGLSQLYQIR
     GRVGRSKTRA YAYLTTKPRQ KLTHAAIKRL RVLGSLDSLG AGFMLASQDL DIRGAGNILG
     EEQSGNVREV GYELYQEMLE DAIAKIKSGQ MEGLTDEGSW SPQINLGVPV LIPETYVQDL
     DVRLGLYRRL SALAKKIELE AFAAELIDRF GKLPTEVDML LRVVRIKGMC RAAGIAKFDS
     GPKGAVIQFY QDKFISPSGL AQYLLDSRGT AKIKDNKLIV LRDWTNDDKK VKGAYIIARE
     LAVMAKSQKT N
//
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