ID H0R5P4_9ACTN Unreviewed; 1241 AA.
AC H0R5P4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, 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 ECO:0000313|EMBL:GAB20395.1};
GN ORFNames=GOEFS_115_00350 {ECO:0000313|EMBL:GAB20395.1};
OS Gordonia effusa NBRC 100432.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB20395.1, ECO:0000313|Proteomes:UP000035034};
RN [1] {ECO:0000313|EMBL:GAB20395.1, ECO:0000313|Proteomes:UP000035034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB20395.1,
RC ECO:0000313|Proteomes:UP000035034};
RA Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL Submitted (DEC-2011) 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:GAB20395.1}.
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DR EMBL; BAEH01000115; GAB20395.1; -; Genomic_DNA.
DR AlphaFoldDB; H0R5P4; -.
DR STRING; 1077974.GOEFS_115_00350; -.
DR eggNOG; COG1197; Bacteria.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000035034; 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 CDD; cd18810; SF2_C_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; 3.
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:UP000035034}.
FT DOMAIN 702..863
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 881..1038
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1241 AA; 133069 MW; 908A99D8DE4EAE64 CRC64;
MVPPLDSPPL DSTPLDSRPS HPALSGLSRI ACADPAFAPI AARRESSLLT ITAPDAARPF
VVAAIDGIDD APLLVVSANG READDLAAEL AEMLDDPAAV AQFPSWETLP HERLSPSADT
VGQRLQVLHR LTDPAASGLR VIVTTVRSLV QPMAPGLGAL RTVTLAEGAE VDFDDLIVDL
VAMAYERVDM VGRRGEFAVR GGILDVFPTT AEFPVRVEFW GDEITDLRAF SVADQRTQEE
IDVDAVQIFP CRELILDESV RARSGNLAEE HADDPALAEM FTKISEGIPV EGMEALIPAL
VDGRMELLTE VVPSGTRVLL LDPEKIRTRA ADLSKTGAEF LEAAWSAAAL GAQAPLSSGS
GVGIDLQASA YRAMGEVEAA TLQAGRAWWT ISPLSAGDAD ELAVDLISGP APRGDEAEIA
STFTMLRAHA AAGGRAAIVV AGKGTAQRYH ERLAEAGVPS VVADAGAEPA PGTVSVYHGT
LRHGLVLPNG HGAGSGASGP NPTGGPNPTG AGSGASGPNP TSAGLVIVSE ADITGTRTVG
AKEGRKLPAK RRNQVDPLAL TAGDMVVHDQ HGIGKFVEMI ERTISGARRE YLVIEYAASK
RGQPGDRLYV PMDALDQLSR YVGGEQPSLS KLGGSDWQNT KRKARKAVRE IAGELVQLYA
ARHAAPGFAF SADTPWQREM EDAFDFTETA DQLTVISEVK SDMERPVPMD RVIVGDVGYG
KTEIAVRAAF KAVQDGKQVT VLVPTTILAQ QHLQTFTERM AGFPVRIKGL SRFTDAAESR
ATIEAMRTGE VDVVIGTHRL LQTGVSWKDL GLVIVDEEQR FGVEHKEHIK SLRTHVDVLT
MSATPIPRTL EMSMAGIREM STILTPPEER HPVLTYVGGY SGKQVAAAIR RELLRDGQVF
FVHNRVSSID KAAREISAMV PEARVVVGHG QMGEDQLERT VNGFWNREYD VLVCTTIIET
GLDISNANTL IVDRAENFGL SQLHQLRGRV GRSRERGYAY LLYSPEKPLT ETAYDRLATI
AQNNELGAGM AVALKDLELR GAGNVLGAEQ SGHVAGVGFD LYVRLVGEAV EAYRAAADGK
PVESTETVEV RIDLPVDAHI PVEYVDSDRL RLEGYRKLAA ATTDNDIAAV LTELTDRYGE
PPVETRRLAA IAGLRLRCRE RGITEVGGAG TQIKISPLPL LDSEQVRLKR LYSSAGYRAT
TSVVTLPIPR TGGVGSARLR DEELIDYLIT FLLQIKPIDA V
//
