ID C1F915_ACIC5 Unreviewed; 1189 AA.
AC C1F915;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 93.
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 ECO:0000313|EMBL:ACO34679.1};
GN OrderedLocusNames=ACP_2078 {ECO:0000313|EMBL:ACO34679.1};
OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS 7670 / NBRC 15755 / NCIMB 13165 / 161).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidobacterium.
OX NCBI_TaxID=240015 {ECO:0000313|EMBL:ACO34679.1, ECO:0000313|Proteomes:UP000002207};
RN [1] {ECO:0000313|EMBL:ACO34679.1, ECO:0000313|Proteomes:UP000002207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 /
RC NCIMB 13165 / 161 {ECO:0000313|Proteomes:UP000002207};
RX PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP001472; ACO34679.1; -; Genomic_DNA.
DR RefSeq; WP_015897179.1; NC_012483.1.
DR AlphaFoldDB; C1F915; -.
DR STRING; 240015.ACP_2078; -.
DR KEGG; aca:ACP_2078; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_0; -.
DR InParanoid; C1F915; -.
DR OMA; WAPPCRE; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000002207; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000002207}.
FT DOMAIN 654..815
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 835..990
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1189 AA; 132867 MW; 9A50C736EB965693 CRC64;
MILPFVRDLL ADLEHTASFE QAQRHLSLSR GRRRVSGLTS TARSLYIPLL ARAAKVPVVL
LVADNKAADA MHLALRAGCE LTGAIAAERV LKLPAHDVLP FENMSPHPEV QEQRATTLWK
IATGDAAIVI APVEAAAMKL FPAPFYGGLA QVLRRGEEID VDMLLTHLAS VGYEQVDVVE
MPGQYTRRGG ILDVYSPEAD RPVRMEFFGD EIETMRKFDP ESQRSQSPLD EARLLPLTET
PVTERLLAAV HARLSGARFE TNDEGEMVAE MVAAGGVSVF PGWEFFAGVA GANKTLLDLF
PRCVLFVEEP GMIKNQVERW WNKVEQRHDR SSIGTLIRPE DIYLRPELLE AQRKSHPGLD
IDQLGAVDVL EDDETLGEIA FSSRPTLRFH GSIPAFVEQI KNLMQQETRM LLAAPNQGEV
ERLATLLREY ELPYRLGSRV MHTGSETMYD EASHLGGDLR TPIILRAPIA TGVSLPDANL
VVFGANDLND EADVTARPAA RKSKTAAFIS DFRDLAVGDY VVHVEHGIAR YLGLKEIAQD
GTTLEFMILE FAEEAKLYVP LTRLDLIQKY RSTESGPAPV LHRLGTQQWA KTKARVKKAM
QDMADELLKL YAQRKAAQGH AYSADNEFQR EFEDSFDYNE TDDQLSAIAD IKRDMESTTP
MDRLLCGDVG YGKTEVAMRA AFKAVQDGKQ VAVLTPTTVL SFQHYETFKK RFRQFPIHIE
MLSRFRTAKE QKLIVERVEA GEIDILIGTH RLLSKDLKFH DIGLLIVDEE QRFGVRHKER
LKQLRAQLDV LTMSATPIPR TLHMSLVGLR DMSVIETPPK DRMAIQTIVA KFDEKLVRSA
VEVELERGGQ IYFVHNRVET IYEIAAKIQE LVPHARITVG HGQMGEAELE KVMLAFMNHE
YDVLVATSII ENGLDIPLAN TILINRADRH GLSELYQLRG RVGRSNRRAY AYLMIPPEQE
LTEIARRRLA ALKEFSDLGA GFKIAALDLE LRGAGNMLGG EQSGHIEAVG FELYTTMLEE
AVNKMKGQET VERPVTQLSL GIPLRIDDSY IPEENQRLRM YKHIAGAQDE RAIAGIRAEL
VDRYGALPTG VRHLLDAAEL RIACEHMGVA QVDRKRDQIH LKFTEKASID PGILMKLVSK
NAKRGAQFTP QGVLRFPLSG TDPESIFTEL RVLLDDLATQ PAAARQGAS
//