ID A0A2P8KGI2_9BURK Unreviewed; 1187 AA.
AC A0A2P8KGI2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
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:PSL82050.1};
GN ORFNames=C7T35_23685 {ECO:0000313|EMBL:PSL82050.1}, GXN78_00725
GN {ECO:0000313|EMBL:NDZ11405.1};
OS Variovorax sp. WS11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1105204 {ECO:0000313|EMBL:PSL82050.1, ECO:0000313|Proteomes:UP000241151};
RN [1] {ECO:0000313|EMBL:PSL82050.1, ECO:0000313|Proteomes:UP000241151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS11 {ECO:0000313|EMBL:PSL82050.1,
RC ECO:0000313|Proteomes:UP000241151};
RA Crombie A.T., Mejia-Florez N.L., Murrell C.;
RT "Isoprene degraders from the Poplar phyllosphere.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NDZ11405.1, ECO:0000313|Proteomes:UP000479786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS11 {ECO:0000313|EMBL:NDZ11405.1,
RC ECO:0000313|Proteomes:UP000479786};
RA Dawson R.A., Larke-Mejia N.L., Crombie A.T., Ul-Haque M.F., Murrell J.C.;
RT "Isoprene oxidation by the Gram negative model bacterium Variovorax sp.
RT WS11.";
RL Submitted (FEB-2020) 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:PSL82050.1}.
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DR EMBL; JAAGOW010000001; NDZ11405.1; -; Genomic_DNA.
DR EMBL; PXZZ01000035; PSL82050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8KGI2; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000241151; Unassembled WGS sequence.
DR Proteomes; UP000479786; 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 649..810
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 831..985
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 338..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1187 AA; 131295 MW; 295DF02A5B82824E CRC64;
MDLPALTAGK RFTLPRPPLS ADALLLAQLA EREKSAGRAS AVFTADANDA QRLIDELAFF
APELRCALFP DWETLPYDSF SPHQDLISER LATLWRISQK EADVVLVPAT TALYRLAPPA
FLAGYTFHFK TKQKLEESKL KAQLTLAGYS HVTQVVSPGE YAVRGGLIDL FPMGSQVPFR
VDLFDDEIDS IRTFDPDTQR SLYPVPEVRL LPGREFPMDD EARARFRSRW RELLEGDPTR
SRLYKDMGNG VATAGIEYYL PLFFEETATV FDYLGADTTV VLHGELEPAF QHFWQDTGER
YRLVRGDPER PALPPEALFL SAEQFYQRAK PHAQLAIRGG GRPHPSPLPE GEGAKADLPP
LPLGEGGGEG SPYVEFTPLP PIAVVRGADD PLVKLKAHIA ATPHRVLVLA ESDGRRESLL
DFLRASGVSP PAFDSLAEFE ASPDEKIGIA TAALVAGFAW TEQGIDFVTE TELFATAPSA
RRRNRKQEQV SDVEALIKDL SELAVGDPVV HSAHGIGRYR GLVHMDLGQG TDAEGKPMLQ
EMLHLEYADK ATLYVPVAQL HLVSRYTGVS ADEAPLHKLG SGQWEKAKRK AAEQVRDSAA
ELLNIYARRA AREGHAFRFS AADYEVFAND FGFDETADQK AAIHAVIQDM ISPQPMDRLV
CGDVGFGKTE VALRAAFVAV TGGKQVAFLA PTTLLAEQHH QTLMDRFGKW PVKVAEMSRF
RSTKEINAAA KGLADGSVDI VVGTHKLLSG TVKFKNLGLL IIDEEHRFGV RHKEAMKALR
AEVDVLTLTA TPIPRTLGMA LEGLRDLSVI ATAPQRRLAI KTFVRNEGTG VIREAVLREL
KRGGQVYFLH NEVETIENRR QKLEQMLPEA RIAVAHGQMP ERELERVMRD FVAQRYNLLL
CSTIIETGID VPSANTIVMS RADKFGLAQL HQLRGRVGRS HHQAYAYLMV PDIEGLTKQA
AQRLDAIQQM EELGSGFYLA MHDLEIRGAG EVLGENQSGN MMEIGFQLYN EMLAEAVRSL
KAGQEPDLLA PLSVTTEINL HAPALLPENY CGDVHLRLSF YKKLATAKTS DQIDTLLEEI
VDRFGKLPPQ AQTLIDVHRL RVLARPYGVV KVDAAPGVIH ISFKKDPPVD SMAIIQLIQK
NKHIKLAGNE KLRIERELKE PKERAQMVRD VLRSLGQPKV AEASAAV
//
