ID C0VZL8_9ACTO Unreviewed; 1199 AA.
AC C0VZL8;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
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:EEH64137.1};
GN ORFNames=HMPREF0044_0608 {ECO:0000313|EMBL:EEH64137.1};
OS Gleimia coleocanis DSM 15436.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Gleimia.
OX NCBI_TaxID=525245 {ECO:0000313|EMBL:EEH64137.1, ECO:0000313|Proteomes:UP000010301};
RN [1] {ECO:0000313|EMBL:EEH64137.1, ECO:0000313|Proteomes:UP000010301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15436 {ECO:0000313|EMBL:EEH64137.1,
RC ECO:0000313|Proteomes:UP000010301};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEH64137.1}.
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DR EMBL; ACFG01000029; EEH64137.1; -; Genomic_DNA.
DR RefSeq; WP_006546068.1; NZ_DS999539.1.
DR AlphaFoldDB; C0VZL8; -.
DR STRING; 525245.HMPREF0044_0608; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_2_2_11; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000010301; Unassembled WGS sequence.
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:UP000010301}.
FT DOMAIN 663..824
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 842..999
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1199 AA; 130379 MW; 5FECFFB4476E409E CRC64;
MKLDGLLADL GTDLGIRHAK QLLNQAGIAA TVVVPAGLQA PLLATARQQR NAKPLLVVTP
TGRDAERLVN ALRCYTPGVE MLPAWETLPH ERLSPQKDTM ARRVAVMRRL KYGDGTLNAR
GGEIRVLVAP LRAFLQPIIG GLADIEPISL RLGSVVDLPS LTAQLVDYGY ARVDVVSARG
EIAVRGGIID VFPPTESHPV RVELFGNEVD DIRYFSVADQ RTIGVAEGGL WAPPARELLL
SEAVRSKAAS LQASLPGAQE MLELISQGHY VEGMETLSPA LVEKMETIFD LVPAGTSVVL
VDPERIEARA ADLVATTEEF LAAAWEAAAA GGEIPLSAQD ASFKTLDELR DLAANSQLAW
IRMTEIAPSE IADALISAGV SQHSGVVANP NLVQVGGRAV VPYRGKIDQA VADLRDLAAN
EWRLVVTTEG PGPAKRLREV FSEADLPARV VGELATEFAT GVVDILVASA GAGFVHEELK
VAVITESDLT GRTGPSTADM RKVPARSKRR GVDPLTLKPG DFIVHETHGI GKFKEMVTRT
VGTGAQAVTR DYLLVEYAAT RKGQPADLLY VPIDQLDQVS RYSGSDAPSL SKIGGAEWAK
TKAKARKAVR EIASELVRLY AARHATKGHA FAPDTPWQRE LEEAFPYVET PDQLATIDEV
KADMEKPTPM DRLLCGDVGY GKTEIAVRAA FKAVQDGKQV AVLVPTTLLV QQHLETFTQR
YAGFPVDIAS LSRFSSKKEA DEIKEKLLKG SIDVVIGTHS LVSGAVRFKN LGLVIIDEEQ
RFGVEHKETL KQLRTDVDVL SMSATPIPRT LEMAVTGIRE MSVLQTPPED RHPILTFVGA
HTDQQVVAAI KRELLRDGQV FYVHNRVEDI DKVAGKISEL VPEARVRVAH GKLNEHQLER
VIVDFWNREF DVLICTTIVE TGLDISNANT LIVDRADAMG LSQLHQLRGR VGRGRERGYA
YFLYPGEKVL TETAHERLRT IATNTDLGAG IAVAQKDLEI RGAGNLLGGE QSGHIAGVGF
DLYVRMVADA VAAFKGDYRG TREEIRIEIP VDGHIPAAYI KGEQLRLETY AKIAALATPE
DAKDIRDELT DRYGPIPENV LLLFALAGLK EHARSLGVHE LVAQGKYLRV GPVELGDAQS
ARLQRLYPGT IMKTAIRKIL VPLPLTSRLG GEPLVDQDLI DWIDNFLEVI VGYRTEAKS
//
