ID C0MC68_STRS7 Unreviewed; 1164 AA.
AC C0MC68;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 102.
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=SZO_00070 {ECO:0000313|EMBL:CAW97563.1};
OS Streptococcus equi subsp. zooepidemicus (strain H70).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553483 {ECO:0000313|Proteomes:UP000001368};
RN [1] {ECO:0000313|EMBL:CAW97563.1, ECO:0000313|Proteomes:UP000001368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H70 {ECO:0000313|EMBL:CAW97563.1,
RC ECO:0000313|Proteomes:UP000001368};
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(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; FM204884; CAW97563.1; -; Genomic_DNA.
DR AlphaFoldDB; C0MC68; -.
DR KEGG; seq:SZO_00070; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_9; -.
DR Proteomes; UP000001368; 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}.
FT DOMAIN 626..787
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 808..962
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1164 AA; 132832 MW; 62ED8332C547835E CRC64;
MDILELFNQN KSIQTWQCDV TSLKRQLVMG LSGSSKAAAI ASAYLSFQGK LVVVTSTQND
MEKLAGDLSA LLDEGSIFQF FADDTAAAEF IFSSMDKTIS RIEALAFLSN PEARGILVIS
LAGLRILLPS PKTFQQGQID LAVGVDTDLD NVVKKLVKIG YQRVAQVLSP GEFSRRGDIL
DVYEVTQDLP VRIEFFGDEI DGIRSFDIES QKSLQRKDST SIKPASDMIF EPEDFDRASH
NLEKQLQLAK AEHKGYLEEL LTVTKEGLKH KDIRKFQSLF YDNEWTILDY LPKGTPVFFD
DFQKLVDRNA KFDLELAHLL TDDLQQGKSL PFLHYFADNY RELRHYKPAT FFSNFHKGLG
NIKFDKVYSL TQYAMQEFFN QFPLLIDEIK RYQKSGATVL LQVESHQAYE RLAKSLEAYQ
CQLPLVSADA IVLHQAQIII GHLAGGFYFA DEKLVLITEH EIYHKRLKRR ARRTNMSNAE
RLKDYNELSK GDYVVHSVHG IGRFLGIETI NIQGVHRDYV TIQYQQSDRI SLPVDQLESL
SKYVSADGKE PKINKLNDGR FQKTKQRVKK QVEDIADDLL KLYAERSQQK GFQFSPDDEL
QKAFEEDFAF VETDDQVRSI KEVKKDMESI KPMDRLLVGD VGFGKTEVAM RAAFKAIGDH
KQVAILVPTT VLAQQHYENF RERFENYPVE IAVLSRFRSK KEQSESLERL KKGQVDIIIG
THRLLSKDVI FSDLGLIVID EEQRFGVKHK ETLKELKTKV DVLTLTATPI PRTLHMSMLG
IRDLSVIETP PTNRYPVQTY VLENNPGLIR EAIIREMDRG GQVFYVYNKV DTIDKKVAEL
QELVPEASIG FVHGQMSDIQ LENTLMDFIN GDYDVLVATT IIETGVDISN VNTLFIENAD
HMGLSTLYQL RGRVGRSNRI AYAYLMYKPD KVLTEVSEKR LEAIKGFTEL GSGFKIAMRD
LSIRGAGNIL GASQSGFIDS VGFDMYSQLL EQAIASKQGR ALTRQKGNAE INLHIDAYLP
SDYIKDERQK IDIYKRIREI DSRAAYSDLQ DEIMDRFGDY PDQVAYLLEI GLLKYYLDTA
FAELVEKRDH QVMVRFEVAS LQYYLTQDYF EALSKTSLKA RISEHQGKIE IIFDVRRQKD
HVILEELILF GETLGEIKSR KASS
//
