ID C7MNR0_CRYCD Unreviewed; 1155 AA.
AC C7MNR0;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
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 OrderedLocusNames=Ccur_08480 {ECO:0000313|EMBL:ACU94550.1};
OS Cryptobacterium curtum (strain ATCC 700683 / DSM 15641 / CCUG 43107 /
OS 12-3).
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Cryptobacterium.
OX NCBI_TaxID=469378 {ECO:0000313|EMBL:ACU94550.1, ECO:0000313|Proteomes:UP000000954};
RN [1] {ECO:0000313|EMBL:ACU94550.1, ECO:0000313|Proteomes:UP000000954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700683 / DSM 15641 / 12-3
RC {ECO:0000313|Proteomes:UP000000954};
RX PubMed=21304644; DOI=10.40456/sigs.12260;
RA Mavrommatis K., Pukall R., Rohde C., Chen F., Sims D., Brettin T.,
RA Kuske C., Detter J.C., Han C., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA Ovchinnikova G., Pati A., Ivanova N., Chen A., Palaniappan K., Chain P.,
RA D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Rohde M., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Cryptobacterium curtum type strain (12-3).";
RL Stand. Genomic Sci. 1:93-100(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; CP001682; ACU94550.1; -; Genomic_DNA.
DR RefSeq; WP_012803237.1; NC_013170.1.
DR AlphaFoldDB; C7MNR0; -.
DR STRING; 469378.Ccur_08480; -.
DR KEGG; ccu:Ccur_08480; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_11; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000000954; 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; 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:UP000000954}.
FT DOMAIN 624..785
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 806..960
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1155 AA; 126915 MW; 226CA18FBDAD1E01 CRC64;
MLIDALTYPL NACKDVHTFW GKLDSGADAT MGLAASARPF FTAARFARTP QPTLVIVAGE
ESAADFARTL SAYVGDNRVL RFFERKDYPT ASTPVDVHAV ACRLQALHAL VESRECIVVA
SSRALMRLMG PVRSRFYLPL TFTAGMDVQS GSGERTIASF EAATEELVAC GYLNTGELSG
PGTFCVGGGT IDVWPGNLSY PVRIDFFGDE VDEIRRIVPA TGQTIARIDK VDIYPLREYM
PDRAALDRAR RILFDPDTTD PVLRESLEAL EGGVYNEAAD ALLPYLYAHL ATLGDFLPSD
ALSVLVEPRS LIDDALHAAE ALSSLPVEHT RFVEDLICPP AKLDFGKNQR CTYQSIMRVA
SSVDAEIPVK RTEVAGDPEK LFGRLISLTQ ADFTVVFSAP SYRAREDMKL AFVERGLSIV
DLANADADTV PARLRRGVVN VVEADIPLGL IIPKAKIALI SLSDTQGATA IRHHRRVDIT
EITFPFNPGD YVVHAAHGIA FFRDVVRQEV GGSLRDYLLL EYAEGDKLYV PVEQLDRVTR
YVGPEGSSPR LTRLNTSDWS RAMGCARKAS KKLAFDLVDV YTRRSAVSGF QYSADTPWMR
QMEEDFPYQE TPDQLAAIAD VKADMRSARP MDRLICGDVG FGKTEVALRA AFKATQDGKQ
VMVLCPTTIL AQQHYTTFKD RFEEYGVTVE VLSRFRFSSE QAAALSGFAQ GTVDVLVGTH
RLLSRDVNPH DLGLVIIDEE QRFGVGHKEQ LKNLRESIDV LTLSATPIPR TMQMSLSGVR
DMSLIMTPPD DRKPIKVHVG EWDPDVVSDA IRRELARNGQ VYYVSNRVRT IDDAVARVGQ
AAGEARIGVA HGQMSKEQLE QVMEEFAAGE IDVLVATTII ESGIDNPHTN TLIIEDSQRL
GLAQMYQLKG RVGRSSLQAY AYFMFPENVP LTEEATARLE AVGEYQELGS GMKVAMRDLE
IRGAGSMLGA EQSGNMSAVG FDLFAQMLTE AVRATREGRA DTLHDLPPAL SDITVNVPDH
TYIPEEYVPD ADARVLAYRR VASADTPEVV DGIADELCAR YGAAPRAAQN FFAKARIKAR
AHQMGVTAVS IVAGKLNIEP IAQPPASLGT DIRRARGRYI VQSKKLQIPL TYFSYDDEHP
LIEAIDAFIA TLRAN
//
