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
//