ID D4C8Z1_9CLOT Unreviewed; 1187 AA.
AC D4C8Z1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 64.
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:EFE13978.1};
GN ORFNames=CLOM621_05864 {ECO:0000313|EMBL:EFE13978.1};
OS Clostridium sp. M62/1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=411486 {ECO:0000313|EMBL:EFE13978.1, ECO:0000313|Proteomes:UP000004936};
RN [1] {ECO:0000313|EMBL:EFE13978.1, ECO:0000313|Proteomes:UP000004936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M62/1 {ECO:0000313|EMBL:EFE13978.1,
RC ECO:0000313|Proteomes:UP000004936};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-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}.
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:EFE13978.1}.
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DR EMBL; ACFX02000008; EFE13978.1; -; Genomic_DNA.
DR AlphaFoldDB; D4C8Z1; -.
DR HOGENOM; CLU_005122_1_3_9; -.
DR Proteomes; UP000004936; 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}.
FT DOMAIN 646..807
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 816..982
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1187 AA; 135403 MW; D4574E9C31F937FB CRC64;
MKMGVIFANP LEELVEFQEM NRDLEQGKGP LQVSGCVDSQ KVHLISETAG SLRWKLIVTY
DDSRAREIYE DYRTFDPAVF LYPAKDLLFY SSDIHGNLLT RQRMQVFKHL MEDEAGTIVT
TVDGLMDRLL PLSEIRNSRI AVVSGESLKT EEMKEALAGL GYERVGQVDG MGQFSVRGGI
IDIFPLTEEL PVRIELWGDE VDSIRSFDPE SQRSVEELER VEICPATELL LEKSRVEKGL
SKIEKEMKKY GKALRDQMKN EEAHRIEGLV RELSEEIREG FKVHGLGGFI QYFAEKTVSF
LEYFPKEELA VFLDEPLRIR EKAEAVELEF RESMAHRLEG GYLLPGQTDF LYSAKATAAM
MSGSHTLLVS GLDQRMTGFS VKKKYSIEAK SMGSYQNGFE MLIKDLTRWQ KEKYRTVLLT
GSRTRASRLA GDLREYGLKA YLPDEDGGQV KAGEIMVTYG NLHRGFEYPL LKFAVITEGD
MFGSGQGKKR KKKKTAYEGR KIQSFSELSV GDYVVHENHG LGIYRGIEKI EQDKVVKDYI
KIEYADGGNL YLPATKLEGI QKYAGADAKR PKLNRLGGSE WNKTKTRVRG AVKEIAKDLV
KLYAARQEQE GFQYGPDTVW QREFEEMFPY EETEDQLEAI DAVKRDMESR KIMDRLICGD
VGYGKTEIAL RAAFKAIQEG KQVVYLVPTT ILAQQHYNTF VQRMKDFPVR VDMLSRFRTP
AEQKRTLEDL KKGFVDVLIG THRVLSKDVE FKSLGLLIID EEQRFGVAHK EKIKKLKENV
DVITLTATPI PRTLHMSLIG IRDMSVLEEP PVDRLPIQTY VMEYNDEMVR EAINREVARG
GQVYYVYNRV NNIEEIANHV ASLVPDAQVT FAHGQMREHE LERIMLDFVN GDIDVLVSTT
IIETGLNIPN ANTIIIHDAD RLGLSQLYQI RGRVGRSSRT SYAFLMYRRD KLLREEAEKR
LQAIREFTEL GSGIKIAMRD LEIRGAGNIL GAEQHGHMEA VGYDLYCKLL NEAVLALKGE
TEEGAEFETT VDCDIDAYIP ASYIKNEYQK LDIYKRISGI ESEEEYMDMQ DELIDRFGEI
PGPVENLLRV AALKALAHRA GVTDVFINRQ EVRLVMFKKA EIDVTGIPEL IGKYRGDLKL
RPGDAPEFLY QDQRSRNKDC MKMTEKAKEL LTELFSLCER AREGVKR
//