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Database: UniProt
Entry: D4C8Z1_9CLOT
LinkDB: D4C8Z1_9CLOT
Original site: D4C8Z1_9CLOT 
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
//
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