ID A0A1W6CW28_9RHOB Unreviewed; 1049 AA.
AC A0A1W6CW28;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=B0A89_05090 {ECO:0000313|EMBL:ARJ69093.1};
OS Paracoccus contaminans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1945662 {ECO:0000313|EMBL:ARJ69093.1, ECO:0000313|Proteomes:UP000193017};
RN [1] {ECO:0000313|EMBL:ARJ69093.1, ECO:0000313|Proteomes:UP000193017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKI 16-01929T\LMG 29738T\CCM 8701T\CIP 111112T
RC {ECO:0000313|Proteomes:UP000193017};
RA Aurass P., Karste S., Trost E., Glaeser S.P., Kaempfer P., Flieger A.;
RT "Genome sequence of Paracoccus contaminans isolated from a water
RT microcosm.";
RL Submitted (MAR-2017) 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}.
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DR EMBL; CP020612; ARJ69093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6CW28; -.
DR STRING; 1945662.B0A89_05090; -.
DR KEGG; pcon:B0A89_05090; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000193017; Chromosome.
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 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 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; 2.
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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:ARJ69093.1};
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:UP000193017}.
FT DOMAIN 534..694
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 715..869
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1049 AA; 110839 MW; CA67EE3044E22A41 CRC64;
MTTSPAAHAE RPGEAEIATA LAALLAEGDV IHVAPAEGAA IAVYRALQIA CPAASCVLVP
EADALPGSGI RATPANVGLR AAGLAGLAER GEAGPVALIT TAEALAQGWP APQAAPRMLD
VQVGEQTPLE SLRDTLVAMG YRDDDRVDEP GEVALHGRVL DVFPTQAANP VRIDAEDGRI
AAIRRFDLLD QRTLNMIDMA RIAPAEDSPR EGPAVSLLDH LPGARLVMDD LADTRRRNML
ALARDIGGTV AAGVLADEAW EAALAGHERV ALPPAGKAPD RFVEGRRPLD AFAQAARAAF
DAGEKVALVG GERDLRFIAR RAGQALGCAA TPAQDWAQIV AADPGTLWTL PMPAGRGFHR
DGVLVVAAAD LLGSRAQRGD AAVAGLNGLL DVAMIRIGDV VVHTEHGIGV VEGIEPLPSA
DGTDGGDAIR LTYHDGGVRL VPVLQADRIW RYGGEPESVT LDKLDGSSWL KRRGEVEAAV
AQTAAALTEL AAEQAQIEAP VLDPEPAAYE RFAAGFPYAE TPDQSRAIEA VRDDLASGRP
MDRLVIGDVG FGKTEVALRA AALAVLAGKQ VAVAVPTTVL ARQHLDSFTR RFAPLGVAVG
GLTRLDSAAE KKRVKAGLAD GSIRIVIGTA TVAGKGIAYD DLGLLVIDEE QRFGTADKRK
MRALGAKHVL TMTATPIPRT LQQALVGLQQ LSVIATPPAR RQPIATRVAP YDTGALRTAL
LREKARQGQS FVVVPRIGDM EAIAATLARL VPELTVLRVH GEMQAAEIDD AMIGFANGDG
DVLLATNIIE AGLDVPRANT MIVTRADRFG LAQLHQLRGR VGRGAQRGQM LMFTDPGAQI
PERTLRRLQT LETLSHLGAG FEISARDLDL RGAGDLLGAE QAGHMKMIGI DLYQQLLSDA
IRAQRGEPPA GRQPDLQLGS EGRLPEDWIA DADTRLGVYM RLSRLNEADE IDLIVDELED
RFGPLPEPAE RLMATVRIRL EARAAGVERV AAGPAGISIY PREGLVLDTQ GLEPREGGVF
VLPEAIDDPA ARFARAGALM RGLAERAEA
//