ID E3GZW7_ROTDC Unreviewed; 1229 AA.
AC E3GZW7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 78.
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:ADP40937.1};
GN OrderedLocusNames=HMPREF0733_11480 {ECO:0000313|EMBL:ADP40937.1};
OS Rothia dentocariosa (strain ATCC 17931 / CDC X599 / XDIA).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=762948 {ECO:0000313|EMBL:ADP40937.1, ECO:0000313|Proteomes:UP000000387};
RN [1] {ECO:0000313|Proteomes:UP000000387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17931 / CDC X599 / XDIA
RC {ECO:0000313|Proteomes:UP000000387};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RT "The complete genome of Rothia dentocariosa ATCC 17931.";
RL Submitted (OCT-2010) 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}.
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DR EMBL; CP002280; ADP40937.1; -; Genomic_DNA.
DR RefSeq; WP_013398674.1; NC_014643.1.
DR AlphaFoldDB; E3GZW7; -.
DR GeneID; 29743659; -.
DR KEGG; rdn:HMPREF0733_11480; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_2_2_11; -.
DR OMA; WAPPCRE; -.
DR Proteomes; UP000000387; 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 686..847
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 872..1022
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1229 AA; 135199 MW; 2016D8B7666415C1 CRC64;
MKLTGLSRLL AEQPSYRHIL EACDVPAAER PVQTLIGAVA GVQAPLIADL AVAVRRQSRT
GKTPLTLIIT PTERQAEDTA HALHSYLPDH HIESFPAWET LPHERLSPRS DTVGKRLNVL
RSITHLETPT PQVVIAPVRA VIQPLVAGIE NLEPVSLARG EEYSFKDVIK GLTDAAYSRV
DLVAKRGEYA VRGGIIDVFA PTAQHPVRLE FFGDELDEIR YFSTADQRTL GQEADHPTHV
TLLPCRELLI TPEVMGRAAR LKTDYPAASS MLEKIAGGIY VEGMESLTPL LVDKMQTLVS
LLPEESLIIS LEPERVRARA EDLVATNEEF LAAAWDASAD AGSRAPIDLG QLRVSDSGFH
TIAATQQESL DRNLSWWEIT ELVDSVDLLN NALDDDIPTM TVAAQAPASF TGSVEQMLHE
VGSLVRDGWT VLALTNGRGS TDRLIELFRE SISGEDPIPA IRRETLDGGT EGALQPGVVE
VCETPASAGF LIPEARLAVL TEGEILGRRG TYAPRGASGK KLKPRKRRNA VDPLALTPGD
YVVHERHGIG KFIEMASRPV AGVSSKHGET PLKEYLVIEY APSKRGGAPD RLFVPSDQLD
LISHYVGSET PTLSKMGGSD WAKTKSRARK AVKEIAADLV KLYSARQASR GHAFSEDTPW
QRELEESFPY NETPDQLTAI HEVKADMEKE IPMDRLISGD VGFGKTEVAI RAAFKAVQDG
KQVAVLVPTT LLAQQHFETF TERFSGFPIK IKVLSRFQKA KETRAIVEDI ASGSIDVVIG
THRILSENVK FKDLGLVVID EEQRFGVEHK EKLKQMRTNV DVLAMSATPI PRTLEMSLTG
IRETSTLATA PEERHPVLTF VGPRTDAQIT AAIRRELMRE GQVFFVHNRV ANIDTVAAEI
GKLVPEARIA TAHGRMSESR LEQIIVDFWE RRFDVLVCTT IVETGLDISN ANTLIVDNAQ
NYGLSQLHQL RGRVGRGRER AYAYFLYPTD KSLGEVAHKR LKAVATHNEL GAGLQLAMKD
LEIRGAGNLL GGEQSGHIAG VGFDLYLRLV GEAVANFRGE QENTEAEVKV DLPVNAHIPH
DYIDAERLRL QAYRQIASAD TEQKIAEARE ELHDRYGALP EPVENLLQVA VLRREAREAG
IHEITAPGPK LRVVSGEPLP ESRQMRLKRV YPGSTHTQPK GLSTWLTLVP RPKTLPVGGV
DLIDGPMLEW CSKFINSIYS ADPKALEES
//