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Database: UniProt
Entry: U5RU12_9CLOT
LinkDB: U5RU12_9CLOT
Original site: U5RU12_9CLOT 
ID   U5RU12_9CLOT            Unreviewed;      1173 AA.
AC   U5RU12;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 53.
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:AGY76220.1};
GN   ORFNames=CAETHG_2001 {ECO:0000313|EMBL:AGY76220.1};
OS   Clostridium autoethanogenum DSM 10061.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY76220.1, ECO:0000313|Proteomes:UP000017590};
RN   [1] {ECO:0000313|EMBL:AGY76220.1, ECO:0000313|Proteomes:UP000017590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY76220.1};
RX   PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA   Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA   Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT   "Comparison of single-molecule sequencing and hybrid approaches for
RT   finishing the genome of Clostridium autoethanogenum and analysis of CRISPR
RT   systems in industrial relevant Clostridia.";
RL   Biotechnol. Biofuels 7:40-40(2014).
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; CP006763; AGY76220.1; -; Genomic_DNA.
DR   RefSeq; WP_013240744.1; NZ_CP012395.1.
DR   AlphaFoldDB; U5RU12; -.
DR   KEGG; cah:CAETHG_2001; -.
DR   PATRIC; fig|1341692.11.peg.2026; -.
DR   HOGENOM; CLU_005122_1_3_9; -.
DR   Proteomes; UP000017590; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   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          642..803
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          812..978
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   COILED          240..279
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1173 AA;  135099 MW;  84E4A34DF12AA6D3 CRC64;
     MRLDGLIKPM RESREFRNII DGISKKKFPI GVFGLSESAK SYLIYGVYNE IDKPFLIVTH
     SDVEARKLYE DLSLYLAEVY YFPTKEMVFY NIDAISGDLR WERLKVIRKM IDTGRKIIIT
     CVESLASAYI PVGLYENYII NISVGEALNL KDISEKLVQS GYEKNEIVDS KGQFSIRGDI
     MDVYSPIAAE AYRIELFGDE VESIRTLNLE SQRSIDKLDS IEIFPAKEII LDKDKIQKGR
     KSIEDDAALV EKKLEKSKNK EALDRIDELT KKNLESLEEN WSFENIDSFL PYFYDKPASF
     LDYAKDYFVV MDDVQRCSGK LDSVYFEFEE NYKNLLERGN ILPKQSKMLC AKSDLFEELK
     NKEIMTLDAI AKSSKVIQPK TITNFSQITL NSYQGQIDLL IEDIKDKKSR GYKILILSGT
     RPRGERLVDT LREKGIESSY RDVIHEIKSG EVVITFGSQL KGFEYPDFKL GVISDKEVFG
     EAKKKNTRKV LKKGVSKIKS FTELKPGDFV VHVNHGIGIY KGIKQLEVQG HKKDYLELIY
     DSEDKLYVPV EQLDMVQKYI GSEGKSPKVS KLGGSDWAKA KKKVKKSIEE IAEDLVKLYA
     IRSTLKGYKY SKDTVWQKQF EDEFPYEETP DQLTTIQDIK QDMESDKVMD RLLCGDVGYG
     KTEVAVRAAF KAVMDGKQVA FLVPTTILAQ QHYNNFVQRF SDFPVKIDMI SRFRTTAQQK
     ASIKAVKVGD VDILIGTHRI LQKDVQFKDL GLLIIDEEQR FGVSHKEKIK KIRKNVDVLT
     LSATPIPRTL HMSLVGARDI SVIETPPEER YPIQTYVVEY NDQLIRDAIL REINRGGQVY
     FVYNRVESIK EMASYIAKLI PEAKVAVAHG QMQERELENI IVDFMKNEYN VLVATTIIET
     GMDIQNVNTM IIYDADKMGL SQLYQLRGRV GRTNRMAYCY LSYRRDKVLT EVAEKRLKAI
     KEFTELGSGF KIALKDLEIR GAGNMMGASQ HGHMAAVGYD LYCRMLEDTI KLIKGDIDKE
     PVETTVELKI DAYIPDNYIK SEVQKIEIYK KIAAISSYDD MLDIKEELED RFSDIPTSVY
     NLMDIAYIRS MSKKIGIEEI KEIKDEVVFS FQDQDRVDKN VLRELFKTYP HEFVLKMNKK
     PGFGYKLKNV KREDILHQIK EIVKYMLKIY EQK
//
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