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Database: UniProt
Entry: A0A097EC63_9SPHN
LinkDB: A0A097EC63_9SPHN
Original site: A0A097EC63_9SPHN 
ID   A0A097EC63_9SPHN        Unreviewed;      1160 AA.
AC   A0A097EC63;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=MC45_00520 {ECO:0000313|EMBL:AIT05164.1};
OS   Sphingomonas taxi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1549858 {ECO:0000313|EMBL:AIT05164.1, ECO:0000313|Proteomes:UP000033200};
RN   [1] {ECO:0000313|EMBL:AIT05164.1, ECO:0000313|Proteomes:UP000033200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55669 {ECO:0000313|EMBL:AIT05164.1,
RC   ECO:0000313|Proteomes:UP000033200};
RA   Zhou Y., Ma T., Liu T.;
RT   "Using Illumina technology Improving SMRT sequencing Genome Assembly by
RT   RASTools.";
RL   Submitted (SEP-2014) 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; CP009571; AIT05164.1; -; Genomic_DNA.
DR   RefSeq; WP_038658269.1; NZ_CP009571.1.
DR   AlphaFoldDB; A0A097EC63; -.
DR   STRING; 1549858.MC45_00520; -.
DR   KEGG; stax:MC45_00520; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_1_3_5; -.
DR   Proteomes; UP000033200; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000033200}.
FT   DOMAIN          630..791
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          812..966
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1160 AA;  126999 MW;  EA855BABE3B67561 CRC64;
     MPDLKTILSA KSPLTLAGVP AGFQPSLLAD LARAAAHSGK GGRAVFVAPD DAAMRAVAAT
     AAFFAPELEV ISFPAWDCLP YDRASPTLRI MAERIAALWQ LQRPKKTPQL VLTTANAATQ
     RVLTPFRIRQ LVATLEPGAR IDRDDLARLL QANGYVRTET VHDQGEYAVR GGILDLFPSG
     EEQALRLDFF GDEIETVRTF SPEDQRTTGR IDGFTLLPAS EALLDEESIK RFRTRYRDKF
     GATATGDPLY QAISDGRRLA GMEHWLPLFE EKLATLFDHL SADDVVVRDF GVTGAAEGRM
     ESIADYYENR QRAEAAQPGS YRPLAAKTLY LDAKEWAASL DAARAHLTTP FHEPESATVL
     DFDVDGPRDF GPERSASANV YEAVVDHLKG LRKAGKKPVL ASYSVGARER LGNLLKDHGL
     HGGKAADSWQ EALGVADTGK SAGVALVVLP LDHGFTAPDV AVLTEQDMLG DRLVRRAKRK
     KSADAFLAEI AALTPGDLVV HSDHGIGKYL GLTSIPVGKS PHDCVAVEYA GGDKLFVPVE
     NLEVLSRYGS NEEGASLDRL GGEAWQRRKS KMKERIREIA GELIKTAAER ALHPGDVLEP
     DVSGYPSFVD RFPYAETDDQ DRAIEDVLGD LSAGKPMDRL IVGDVGFGKT EIALRAAFVA
     AMAGKQVAVV CPTTLLARQH YNNFSARFEG FPMNMGRLSR LVPAGEAKAV KEGLAGGTVD
     VVIGTHALLA KNIDFKRLGL VIVDEEQRFG VTHKERLKAL RADVHMLTLT ATPIPRTLQM
     AMSGIRELSV IQTPPVDRLA VRTYVIPWDP VVLREALLRE HYRGGQSFIV TPRVADLPDL
     EEYLRNEVPE IRYVVAHGQM SPTEVEERMS AFYDKKFEVL VSTTIIESGI DIASANTIIV
     NRADRFGLAQ LYQLRGRVGR SKTRAYAYLV TPPERQMTET AEKRLKVLSD LDSLGAGFQL
     ASHDLDIRGA GNLLGDEQSG HIKEVGYELY QSMLEEAIMD AKAGGMALRP RDFSPQITVD
     APILIPDDYV PDLDLRMGLY RRLNELEDNR EIEAFAAEMI DRFGPLPDAT DNLIRVIEIK
     LNARKACIAK MDVGPRGVLV GFHDDTPPNV PGLLAYVERL NGVAKLRPDS KLVLQRAWPD
     AKSRLHGALQ LSKGLAKAAG
//
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