ID S3Y526_9ACTN Unreviewed; 1194 AA.
AC S3Y526;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=HMPREF1531_01542 {ECO:0000313|EMBL:EPH03480.1};
OS Propionibacterium sp. oral taxon 192 str. F0372.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=1203605 {ECO:0000313|EMBL:EPH03480.1, ECO:0000313|Proteomes:UP000014567};
RN [1] {ECO:0000313|EMBL:EPH03480.1, ECO:0000313|Proteomes:UP000014567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0372 {ECO:0000313|EMBL:EPH03480.1,
RC ECO:0000313|Proteomes:UP000014567};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Socransky S.S.,
RA Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Propionibacterium sp. oral taxon 192 str. F0372.";
RL Submitted (MAY-2013) 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:EPH03480.1}.
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DR EMBL; ATFL01000012; EPH03480.1; -; Genomic_DNA.
DR RefSeq; WP_016669333.1; NZ_KE340297.1.
DR AlphaFoldDB; S3Y526; -.
DR STRING; 1203605.HMPREF1531_01542; -.
DR PATRIC; fig|1203605.3.peg.1595; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_11; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000014567; 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}; Reference proteome {ECO:0000313|Proteomes:UP000014567}.
FT DOMAIN 648..809
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 834..984
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1194 AA; 131595 MW; DE9980DE576DA5B2 CRC64;
MNVSGLFSAV ATDPGVANAL TEARSGLVSA ELTCAPAARQ VLLATMSRQI GRQMLVVTST
FREAEQLTAV LETLLDPHQV AFYPAWETLP HERLSPRSDT VGRRLEVLRR LAGYGELPAP
EIIVAPVRSV LQPQVAGLAE LPVVHLVRGQ EYPVAKLTTD LVAAAYQRVD LVERRGEFAV
RGGIVDIFPP TCPHPVRVDF FGDEIDTITW FQVSDQRSTD QTIDAVDASP CRELLITDRV
AERAAALVQD HPELAEMLEK IANHQGVEGM EALIPALVDH LELLVDVLSD DAMIVVNDPE
LVRARAEDLV RTSQEFLGAG WAAAASGGSA PIDLDASAYW ELGEVRSRAL DRGLQWWSLS
SFGMDDQQPM DIEEIAALAS SVPTRRLALT DAPNWHGDVE GFVSRISSDL AEGLRVLLSV
EGSGPASRMA DLLGEHDVPA RIVTEVTEIS DDPVVQIFRS GMRQGWRAEE IRLVVHTAAD
ITGAQAPRSS RAMPTRRRNQ VVPMELKPGD ALVHQQHGVG RYIEMVTRTV SGATREYLVL
EYAPAKRGQP GDRLYVPMDQ LNEVSRYVGG EAPSLDKMGG GDWKARKSRA RRAVREIASE
LIKLYAARQA TKGFAFAADT VWQRELEDAF NYTETPDQLA CINDVKHDME QIVPMDRLIC
GDVGYGKTEI AVRAAFKAVQ SGKQVAVLVP TTLLVQQHAA TFTERYAGFP INVAQLSRFQ
SDAEVRATLD GLVSGRVDIV IGTHRILSDK VQFKDLGLVI IDEEQRFGVE HKEALKKMRV
NLDVLSMSAT PIPRTLEMAV TGIREMSTIA TPPEERHPVL TFAGAYDHGQ VVAAIRRELA
REGQVFYVHN RVQDIDRVAA ELREAVPEAH IVTAHGKMSE RTLEQVMTDF WERRIDVLVC
TTIVEAGIDV SSANTLIVDR ADRMGLSQLH QLRGRVGRSR ERGYAYFLYP RDKPLTQTAH
DRLTALASNT DLGAGMAIAM KDLEIRGAGN LLGDEQSGHI ADVGFDLYIR MVGEAVSDFR
GEADAEEEAE MRIELPVDAH LPIDYVESER LRLEMYRRLA EVRSEQDITE VREELEDRYG
PLPQPTGMLL DVARFRLACR ASGITEVVAQ GNHIRFAPVN DRLLPGQQRV DLPESRRLRL
SRMYPGSLVK ATNIALVPRP RTTGVPSVPV EGADLLAWAA TLVEAVFAPV PVAK
//
