ID K9P3C5_CYAGP Unreviewed; 1196 AA.
AC K9P3C5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=Cyagr_0694 {ECO:0000313|EMBL:AFY27882.1};
OS Cyanobium gracile (strain ATCC 27147 / PCC 6307).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Cyanobium.
OX NCBI_TaxID=292564 {ECO:0000313|EMBL:AFY27882.1, ECO:0000313|Proteomes:UP000010388};
RN [1] {ECO:0000313|Proteomes:UP000010388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27147 / PCC 6307 {ECO:0000313|Proteomes:UP000010388};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003495; AFY27882.1; -; Genomic_DNA.
DR RefSeq; WP_015108336.1; NC_019675.1.
DR AlphaFoldDB; K9P3C5; -.
DR STRING; 292564.Cyagr_0694; -.
DR KEGG; cgc:Cyagr_0694; -.
DR PATRIC; fig|292564.3.peg.645; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_0_3; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000010388; 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:0009432; P:SOS response; IEA:UniProtKB-KW.
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}; SOS response {ECO:0000256|ARBA:ARBA00023236}.
FT DOMAIN 640..801
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 810..978
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1196 AA; 131209 MW; D173B257E3D86B57 CRC64;
MPLHALVRQL QAATLTAEVR ARCERPERLR LSGAGRAARA LVASAMAGSS EAPLLVVVPT
LEEAGRWASL LELMGWPLCQ LYPTSEGSPY EPFDPTSEIT WGQLQVLAEL VGDGEGASGA
GGGGRFAVVA TERALQPHLP PPPQLAARCL TLRRGDRLDL EQLALILAGL GYEKVPTIEQ
EGTWSRRGDI VDVFPVSAEL PVRLELFGED LEKLREFDPA TQRSLDVIER VRLTPTSYAP
LIAEALRQRM PDGLERLLEP AALDQLLEGG TPEGMRRLMG LAWETPASLL DYLPAGTLVA
IDERRQCLAH GQQWFDHATE HHGEVVKAAE GEPPLPLPGL LHRPIAAALA EAEAFTGFDL
AELHESDRHP NVLDLASRPV PAHPNQFGRL AEQIKGHLRE KARLWIVSAQ PSRAVALLEE
HDCVTRFVPN ARDFPAIERL VEQATPVALK LRGTAELEGF QLPAWKLVLF TDREIFGQHS
LAAGGYVRRR RKAASRTVDP NKMLPGDFVV HRNHGIGRFL KLEKLAIGGE ARDYLVVQYA
DGLLRVAADQ LGSLGRYRAS SDSPPELNRM GGTAWTKAKE RARKAVAKVA MDLVKLYAER
HKAPGFAFPP DGPWQGELED SFPYDPTPDQ LKAIVDVKRD MERDQPMDRL VCGDVGFGKT
EVAIRAIFKA VTAGKQCALL APTTVLAQQH WRTLSERFAP YPLKVALLNR FRTAAERKTI
LDDLAKGNTD VVVGTHQLLG KGTAFRQLGL LVVDEEQRFG VNQKEKIKAL RKDVDVLTLS
ATPIPRTLYM SLSGVREMSL ITTPPPLRRP IKTHLASLDE EAVRSAIRQE LDRGGQVFYV
VPRVEGIEEV AGQLRAMLPG LRLQVAHGQM PEGELESAMV AFNAGEADVM LCTTIIESGL
DIPRVNTILV EDAHRFGLAQ LYQLRGRVGR SGIQAHAWLF YPGDASLSEA ARQRLRAIQE
FAQLGSGYQL AMRDMEIRGV GNLLGVEQSG QMEAIGFDLY MEMLQDCLAE IQGQDIPAVD
ETQIDLPVTA FIPADWITEA DEKMAAYRAA AECGGKAALV ELAAGWADRY GPIPAPVQSL
LELMELKLLA RRCGFSRIKP EKPNIALETP MEEPAFRRLR QALPQHLHGR LVYQGGAGST
AKVLARGLGA LSPAQQVEQL MAWLSAMAGQ IPEANGRTPE QRDEAQQAKN EAVLVV
//
