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Database: UniProt
Entry: A0A2P8DB24_9BACT
LinkDB: A0A2P8DB24_9BACT
Original site: A0A2P8DB24_9BACT 
ID   A0A2P8DB24_9BACT        Unreviewed;      1160 AA.
AC   A0A2P8DB24;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=B0I18_101574 {ECO:0000313|EMBL:PSK94418.1};
OS   Taibaiella chishuiensis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Taibaiella.
OX   NCBI_TaxID=1434707 {ECO:0000313|EMBL:PSK94418.1, ECO:0000313|Proteomes:UP000240572};
RN   [1] {ECO:0000313|EMBL:PSK94418.1, ECO:0000313|Proteomes:UP000240572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12700 {ECO:0000313|EMBL:PSK94418.1,
RC   ECO:0000313|Proteomes:UP000240572};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (MAR-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:PSK94418.1}.
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DR   EMBL; PYGD01000001; PSK94418.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8DB24; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000240572; 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; 3.30.2060.10; 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; 3.
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:UP000240572}.
FT   DOMAIN          619..780
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          801..955
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1160 AA;  132970 MW;  4E05C44B4390269E CRC64;
     MNLQTLLGIY LNDNRLKQLA AGLSLPEPKM RISLRNLRGS SVNFIATAVW QQAETNHVFV
     LNDREEAAYF HNDLESLTQA LDICFFPDSF KKTGVYTGLN SSHIMLRTEA LAHLSESKTR
     SGANVKRKVL VTYPEALFEK VVNAQSLSSN MIHIKTSEIL KVDELMKRFV ELGFKREDFV
     YEPGQFAMRG GILDIYSFGN EHPYRIELFG NEVDSIRIFN PETQLSERKL LQVSILPNIE
     TRFETQEKIS LLDYLPEHTT FWFKDLDFTL GKLSKMELDL AEKLPQGNIT AVEQEEQWLK
     ELAADDFEIA SEWRDKLQHK HIIEWFATAD KNESTGSTEE TKSIADRERE RNNVIDLSTF
     KPINFSAYQP VSFSTEHQPV FNRNFEILTG NLKRYIDAGY TPYIFAENAK QLERLRTIFE
     DSNAQINFVP IPVSLSKGFI DHEHKILAYT DHQIFQRYHK YRIKQAYSKG KAITLKALKE
     LQPGDFVTHI DHGVGKYSGL QKIEVNGNMQ EAVRILYRDN DVLYVNINSL HKISKYTGKE
     GTVPKVNKLG SDAWEKLKNK TKKQVKDIAA DLIRLYARRK ASPGFAHSPD SYIQTELEAS
     FFYEDTPDQS KATADVKRDM EAPAPMDRLV CGDVGFGKTE IAVRAAFKTV GDSKQAAILV
     PTTILAYQHY QTFKERLKDF PANVDFINRF KSAKEKKETL KRVEEGKVDI IIGTHALLGK
     EVKFKDLGLL IIDEEQKFGV SAKEKLRERK ANVDTLTLTA TPIPRTLQFS LMNARDMSII
     NTPPPNRQPV HTEVMGFDEA TIRDAIYFET ERGGQVYFVH NRVQSLPAMA EKLRELCPDL
     EIGMAHGQME GSKLEKALLD FINYKYDVLC CTNIVESGVD ISNANTIIIN NAHHFGLSDL
     HQLRGRVGRN NKKAFCYLVA PSMITLPNDS RKRLQTLEQF NELGSGFQIA MRDLDIRGAG
     NILGGEQSGF IAEIGFEMYQ KILAEAMHEL RSTDFKEVFA EEMDRKKDFV TDCTIDTDLE
     ILIPDSYIEN ITERLSLYTQ LDDIEDEAEL QLFEEELRDR FGPIPAQVND LFRALRCRKM
     AKELGFEKLI LKNEQMRLYF VSNPDSPYFE SETFNYIMQY IQTQTNNARL KQVGKNFMLI
     VDHIKSMSDV EWFLQGMTKK
//
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