ID A0A0D8IAV6_9CLOT Unreviewed; 1173 AA.
AC A0A0D8IAV6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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:AKL93626.1};
GN ORFNames=CACET_c01080 {ECO:0000313|EMBL:AKL93626.1}, TZ02_09070
GN {ECO:0000313|EMBL:KJF27209.1};
OS Clostridium aceticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=84022 {ECO:0000313|EMBL:AKL93626.1, ECO:0000313|Proteomes:UP000035704};
RN [1] {ECO:0000313|EMBL:AKL93626.1, ECO:0000313|Proteomes:UP000035704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1496 {ECO:0000313|EMBL:AKL93626.1,
RC ECO:0000313|Proteomes:UP000035704};
RA Poehlein A., Schiel-Bengelsdorf B., Gottschalk G., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium aceticum DSM 1496.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KJF27209.1, ECO:0000313|Proteomes:UP000032372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1496 {ECO:0000313|EMBL:KJF27209.1,
RC ECO:0000313|Proteomes:UP000032372};
RA Song Y., Hwang S., Cho B.-K.;
RT "Draft genome sequence of Clostridium aceticum DSM 1496, a potential
RT butanol broducer through syngas fermentation.";
RL Submitted (FEB-2015) 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; CP009687; AKL93626.1; -; Genomic_DNA.
DR EMBL; JYHU01000009; KJF27209.1; -; Genomic_DNA.
DR RefSeq; WP_044824621.1; NZ_JYHU01000009.1.
DR AlphaFoldDB; A0A0D8IAV6; -.
DR STRING; 84022.CACET_c01080; -.
DR KEGG; cace:CACET_c01080; -.
DR PATRIC; fig|84022.5.peg.3973; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000032372; Unassembled WGS sequence.
DR Proteomes; UP000035704; 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}; Reference proteome {ECO:0000313|Proteomes:UP000035704}.
FT DOMAIN 641..802
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 824..977
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1173 AA; 134925 MW; 17E3A7F9A3CAE26C CRC64;
MKKNVLLSPL ENSLQYMQLA QILREERSSI SLHGLDDSQR GHVTYSLYEG LGRQICLLTY
SEIEAQQIHQ DLKFYLEDQA SFFPTKDIVF YDVEATSEEV SEERIKALNK LARGEVCVVV
ASIEALLLKL TPVDIYKKYQ HTFTVGQRIQ LQEIMKSFVL QGYEKVERVD TKGQFSTRGG
IIDIFPPSEE NPLRIELFDD EVDSIRHFEV ETQKSIDKIE EVKVYPAIEI IIEANHYEKT
IPRLTQELKN TLKKLDTVTG EKLQKKIAEV VEKFSNFGNF KGIQRFLPYI YEKSASLIDY
LAEDAIIILD EPDRGKEKIK GYWEEFRENF KTLLERGEVL PNQAHLLFTY EEILEKLKNR
SLVTSSLLPK NHPDIMPKKI INFISRPVQS FYGKINLFTK EIKSLQQKGY TIRIVTTTKE
KAMKLLETIR EEGILASFLV QDRIDESYAG KVIILQGNLH RGFEYVDVKY ILFTDYEIYG
AHKKKKQKSA RKDTAPIKSF IDLQVGDYVV HEGHGIGKYI GIEELKVEGV KKDYLKIRYS
GEDNLYLPTD QMDLIQKYIG ADDKVPKLNK LGGTEWVKTK AKAKKAIEDM AKDLLKLYAE
REKSKGYAFA PDTDWQKQFE YLFPYEETPD QLKCIEEVKR DMEKERPMDR LLCGDVGYGK
TEVAIRGAFK AVMDGKQVAV LVPTTILAQQ HYNNFKERFS GFPVTVEMLS RFRTPTQQKH
TIENVRTGNI DVLIGTHRLL SKDVAFKDIG LLIVDEEQRF GVKHKEALKQ LKKAVDVLTL
TATPIPRTLH MSMIGVRDMS VIEDPPEERF PVQTYVATYN EALIADALIR EMARGGQVYY
VYNRVQGIHQ IAAKLGNFVP QARVGVAHGQ MSERQLEKLM LEYYHGEYDV LVCTTIIETG
LDIANVNTII IQDADRLGLS QLYQLRGRVG RSNRQGYAYL LYEKDKILSE VAEKRLKAIK
EFTEFGSGFK IAMRDLEIRG AGNLLGSEQH GHMASIGYDL YVKLLEEAVG ELKGEKIEKY
EDTMMELNVD AYISEKYIAN QSHKIEIYKK IASIRDEEDL YAIEEEIEDR FGDIPLSVRN
LLLISYIKAL AKSLKVQYIS QKEKNIRIQF KEAKVLRPEN VAEVMEGYRW KVTIHGGQQP
YITYKIQTQD QYKVLLDLKG LIEKISGLKK VAS
//
