ID A0A258NW64_9BURK Unreviewed; 1156 AA.
AC A0A258NW64;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=B7Y60_15740 {ECO:0000313|EMBL:OYY34535.1};
OS Polaromonas sp. 35-63-35.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1970418 {ECO:0000313|EMBL:OYY34535.1, ECO:0000313|Proteomes:UP000216365};
RN [1] {ECO:0000313|EMBL:OYY34535.1, ECO:0000313|Proteomes:UP000216365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35-63-35 {ECO:0000313|EMBL:OYY34535.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
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}.
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:OYY34535.1}.
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DR EMBL; NCFQ01000012; OYY34535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258NW64; -.
DR Proteomes; UP000216365; 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 618..779
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 800..954
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1156 AA; 128803 MW; CCB1FBAC753CDED4 CRC64;
MDLPKLLPGK RYTLPQPAGS ADALLLAQLG LREKAAGRLT AIVTADAATA QRLLDELAFF
APALRCALFP DWETLPYDTF SPHQDLISER LATLWRISQH DKETGADVVI VPATTALYRL
APPSFLAGYT FHFKVKQKLD EAKLKSQLTL AGYTHVSQVV SPGEYAVRGG LIDLFPMGSA
VPYRVDLFDD EIDSIRTFDP DSQRSLYPVP EVRLLPGREF PMDDEARTKF RNRWRELLDG
DPTKSRIYKD IGNGVATAGI EYYLPLFFDD TATVFDYLGS DATVVLHGDL EPAFQRFWQD
TKDRYRLVRD APDRPALPPE ALFLGTEQFY ARANEYAQLA IRPAVEDVAD NANFQKLGEM
SVVRGAEDPL ARLKAHIRNT PQRVLLLAES DGRRESLLDF LRASSVSPPA FDSLEDFQHS
SEKLGIATAA LNTGFSWLAG DIDFVTETEL FAAGVVTRRR NRKQEQVSDV EALIKDLSEL
NVGDPVVHSA HGIGRYKGLV NMDLGQGNTE FLHLQYADDA TLYVPVSQLQ QISRYTGVSA
DEAPLHRLGS GQWEKAKRKA AEQVRDSAAE LLNIYARRAA REGHAFRYSP DDYESFANDF
GFEETADQRA AIHAVIQDMI SPRPMDRLVC GDVGFGKTEV ALRAAFIAIT GGKQVALLAP
TTLLAEQHYQ TLVDRFAKWP VKVAEMSRFR SGKEITAAIK GIADGSIDIV VGTHKLLSQD
VKFQRLGLLI IDEEHRFGVR HKEAMKAMRA EVDVLTLTAT PIPRTLGMAL EGLRDLSVIA
TAPQRRLAIK TFVRSESNGV IREAVLRELK RGGQVYFLHN EVETIQNRRE KLEALLPEAR
IAVAHGQMPE RELEKVMKDF VAQRYNLLLC STIIETGIDV PSANTIVMSR ADKFGLAQLH
QLRGRVGRSH HQAYAYLMVP DIEGLTKQAS QRLEAIQQME ELGSGFYLAM HDLEIRGTGE
VLGENQSGNM MEIGFQLYNE MLNEAVASLK AGREPDLLAP LNVSTEINLH APALLPSDYC
GDVHLRLSFY KKLATAKNTD QIDSLLEEIV DRFGKLPAQA QTLIDVHRLR VIAKPYGVVK
VDAAPTLINI TFRKDPPIDS MAIMHLIQKN RHIKLAGNDK LRIERELKEP KDRAQMVRDV
LKSLGQPKTT TEATPA
//
