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Database: UniProt
Entry: R7F8B7_9CLOT
LinkDB: R7F8B7_9CLOT
Original site: R7F8B7_9CLOT 
ID   R7F8B7_9CLOT            Unreviewed;      1155 AA.
AC   R7F8B7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
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   ORFNames=BN623_00772 {ECO:0000313|EMBL:CDE11115.1};
OS   Clostridium sp. CAG:354.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262799 {ECO:0000313|EMBL:CDE11115.1, ECO:0000313|Proteomes:UP000018313};
RN   [1] {ECO:0000313|EMBL:CDE11115.1, ECO:0000313|Proteomes:UP000018313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:354 {ECO:0000313|Proteomes:UP000018313};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDE11115.1}.
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DR   EMBL; CBIG010000079; CDE11115.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7F8B7; -.
DR   STRING; 1262799.BN623_00772; -.
DR   Proteomes; UP000018313; 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}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000018313}.
FT   DOMAIN          628..789
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          798..964
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   COILED          560..587
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1155 AA;  133786 MW;  6C8D41403957FD42 CRC64;
     MNPVLAELTK SDKFNEYLER IKKSNAPISI LGLAGVGTLQ IVASTEENIK RPVCLITYNE
     LQAKKLAEEI RSYINGVFFF PKREILTYDY VAESKELPYE RIEVLKNIKN GKIKVLVCSI
     EALLQPIISE DILFKNKISV KVGETYDLEE LKRKISMLGY TKTEMIDGKG EFSSRGGILD
     LSFDDKYGIR IEFWGDEVDS IRKFDIQTQR SIEMIQEVEI NPLHEYLLEN SLEEVCNKIL
     NNITEYTENQ KNNVKEDIEL IKTGEYISKV DKYFKFFYSK KATLLDYITE KYILFLEEPK
     KILARGKNIL KDIEGIENAL VERERIIPNA LENYISIEEF SNNINELKKI YLISDDLGDS
     SEAEKYYFRF RTLNYNRSDF NKFIDDILKA KAEGKKLYLY VNSKEKAKKL QAVLDENEII
     SEYKEDLRYS EISNGIAVKI IVGSLEQGYE SYEANILVIV ANDLISIEKR KRRKASKLFN
     EAEKIIFSEL KQGDYVVHKI HGIGQFVGVN TIVTDKTTKD YIKIKYKNDD MLYVPTDQLD
     NVKKYIGGGD ALPKINRLGS KEWENTKERV KKNLREVAQE LIELYAKRQK SKGYAFSKDT
     PWQQEFENSF IYQETDDQLR CIEEIKKDME MQKPMDRLLC GDVGYGKTEV AIRAAFKAVM
     DQKQVAYLVP TTVLADQQYK SFKERMQDFP VNIEVLNRFR TKKEQQEIIR KLKLGEIDIV
     IGTHRILSKD IEFKDLGLLI IDEEHRFGVK DKEKIKEYKN SIDVLTMTAT PIPRTLHMSI
     VGVRDMSIIY EPPQNRKPVQ TYVLEYDEEV VKEAITKELE RDGQVFYLYN NVEGIERKAN
     EILKLVPEAK VSYAHGKMSG NELENIMLDF INGETNVLVC TTILESGIDI PNANTIIVEN
     ADRLGLAQLY QIRGRVGRSD AQAYAYITYK RDKLLSEVAD KRLKAMKEFT EFGSGFKIAM
     RDLEIRGAGS MLGEIQHGHM EQVGYDTYCN LLDQVIKEMK DIPQEEEEKD VQIDLNVSSY
     IPDSYITDSS QKIKIYQDIA LCRTEEDIQN IIDEMIDIYG EIPAEVENLL NIARIKSLAK
     KLHIFRIQQK ANGVVFSFEG ESFKFDIVDK LLKEYRNKIK FSPGKDPYIT YKIEELSDDK
     ILFSIKEFLK FLCEN
//
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