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Database: UniProt
Entry: A0A0W1DPN1_9SPHN
LinkDB: A0A0W1DPN1_9SPHN
Original site: A0A0W1DPN1_9SPHN 
ID   A0A0W1DPN1_9SPHN        Unreviewed;      1164 AA.
AC   A0A0W1DPN1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=ATE67_11890 {ECO:0000313|EMBL:KTE20080.1};
OS   Sphingopyxis sp. H050.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1759072 {ECO:0000313|EMBL:KTE20080.1, ECO:0000313|Proteomes:UP000053439};
RN   [1] {ECO:0000313|Proteomes:UP000053439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H050 {ECO:0000313|Proteomes:UP000053439};
RA   Gomez-Alvarez V., Revetta R.P.;
RL   Submitted (NOV-2015) 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:KTE20080.1}.
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DR   EMBL; LNRZ01000005; KTE20080.1; -; Genomic_DNA.
DR   RefSeq; WP_058816888.1; NZ_LNRZ01000005.1.
DR   AlphaFoldDB; A0A0W1DPN1; -.
DR   STRING; 1759072.ATE67_11890; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000053439; 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; 3.40.50.11140; -; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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}.
FT   DOMAIN          629..790
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          811..965
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1164 AA;  126866 MW;  EFA1A57533946479 CRC64;
     MTRPAADIFA AIASAPAPLT LARAADGFLP LLLADLARAS DTRLVYVATD DAAMQAVADA
     APFFAPDLSV HRFPAWDCLP YDRAGPSMRI SADRLATLSA LQAPPKRGEL ILTTVAAITQ
     RTLTPFRIRQ LATTLAAGQR IDRDALAELL VSNGFSRVDT VADQGEFAVR GGILDLFPAG
     EETGLRVDFF GDEIESIRRF DPADQRSLGP AKALQLLPAA ETLLDESTIK RFRSSYREIF
     GAQATGDPLY QAVSEGRRQA GMDHWLPLFE ERLATLFDHI DPATPVLRGH RTDATAETRF
     DAITDYHANR VAAEREQAGS YRPLAPETLY LTRDEWADAE RTRPVHVVSP FDVPPSASVI
     DLESFAARDF TPERTADLNV YDKVADHLSD ERRKGRRTII ASYSGGARER LSGLLRDHGV
     TSLAPADSWQ DALGTASSES GGATAMVVLP LDHGFASDAI SLLTEQDILG ERLVRRSKRR
     KSADAFLAEL ATLSVGDLVV HLDHGIGRYE GLTQIPVGSS PHDCVALTYA GGDKLYVPVE
     NLDVLSRYGG ESEGVALDRL GGEAWQRRKA RMKERIREIA GELLATAAQR ALRPGEVLAQ
     DAAYPAFADR FPYQETDDQD RAIGEVLEDL ASGRPMDRLV CGDVGFGKTE VALRAAFVAA
     MAGVQVAVVV PTTLLARQHY TNFVERFKGF PVNIGRLSRL VPANEAQKTR DGLASGQIDI
     VIGTHAVIAK SVEFKHLGLV IVDEEQRFGV VHKERLKQLK ADVHVLTLTA TPIPRTLQMA
     MSGLRELSVI QTPPVDRLAV RTYVAPWDPV VMREALLREH DRGGQSFFVV PRIKDLPDIE
     EFLRNRVPEI KYVVAHGQMT PTEVEDRMSA FYDRKYDVLL STTIVESGLD IPSANTLIIH
     RADRFGLAQL YQLRGRVGRA KTRAYAYLTT PEGGAITDTA EKRLKLLGDL DTLGAGFQLA
     SHDLDIRGAG NLVGDEQSGH IREVGFELYQ SMLEEAILAA KAEGMGAAPP REALSPVITV
     DAPILIPEDY VPDLPLRMAL YRRLNEADDR PALDAFAAEM IDRFGPLPPE TANLIQLMEI
     KANAKTAGIA KLDVGTKGAL VSFHGDAFAN VPGLIAYVER LKGRARIRPD NKLSISGDWA
     STGARLNGAL QLSKGLGKLA RQVA
//
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