ID A0A1G8PA28_9FLAO Unreviewed; 1122 AA.
AC A0A1G8PA28;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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 ORFNames=SAMN05421846_11815 {ECO:0000313|EMBL:SDI89145.1};
OS Chryseobacterium taeanense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=311334 {ECO:0000313|EMBL:SDI89145.1, ECO:0000313|Proteomes:UP000198869};
RN [1] {ECO:0000313|Proteomes:UP000198869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17071 {ECO:0000313|Proteomes:UP000198869};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FNDW01000018; SDI89145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8PA28; -.
DR STRING; 311334.SAMN05421846_11815; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000198869; 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; 3.40.50.11180; -; 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 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; 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; 3.
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:SDI89145.1};
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}.
FT DOMAIN 573..734
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 743..909
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1122 AA; 128669 MW; E1CD84B814213C0C CRC64;
MQLKTISEKF LPDLLQKEFG KEIFIQLENH QHISVKGSAG SAVSVFVAEL FLTHKKHILY
IIDDKEDALY ANTEMEDLLG KDKVLYFPAT HMEPYQVEKT QNANLVLRTE AINKITSEKS
PKVIVAYAGA LSEKVLKKED FKAISHHIKT GDQLDFDFVD ELLNHYNFQQ TDFVSEPGEF
SVRGGIVDVF SFSNEKPYRI TFFGNEIESI KTFDIETQLS VDKVKDFQLV SNMNFTVTGS
RVSLLQLLPK ESIVVSKNGI TAMQKLKTFY ERALEKYDTL NKDIAHRTPQ ELFISDQEFL
FDYKKFKTVD FGSFSIEGLI ELEEIKIDQI PQPSFHKNFE LLIEDLEEKQ GEGFDTWISF
SGEKQKERLE SIFEELEHQL PFKSFKSELH EGFVDHGHKL LVYTDHQIFD RYQRYKAKNT
FAKSEQLTLK DLMSLKIGDY IAHIDHGIGK FMGLVKVNND GKIQECFKLT YKNGDLLYVS
IHSLHKISKY NGPEGREIVL SKLGSPSWKS LKQKTKAKVK QIAFDLIRLY AQRKTAKGFA
YTPDSYLQNE LEASFIYEDT PDQEKATIDV KKDMEADTVM DRLVCGDVGF GKTEVAIRAA
FKAATDGKQV AVLVPTTILA FQHYRSFKER LKDFPVNVDY INRFRTAKQK SETMQALKDG
KVDIVIGTHQ LAGSSVKFKD LGLLIIDEEH KFGVSVKDKL KTLKSNVDTL TLTATPIPRT
LQFSLMAARD LSVIKTPPPN RQPVETQLVG FNEEIIRDAV SYELQRDGQV YFINNRIENL
KDIAGLIQRL VPDARVITGH GQMEGKQLEK NVLDFMEGKY DVLVSTTIVE SGVDVPNANT
IFINDAQRFG MADLHQMRGR VGRSNRKAFC YLITPPYDMM TSDARKRLEA IEQFSDLGSG
FQIAMKDLEI RGAGDLLGAE QSGFINEMGF ETYQKLMQEA LEELKDDKEF ENLFENEEER
NKLFKTTKDI NIDTDLELML PDWYIYNTEE RLLLYQKLAE IDNEKSLEKF ESELKDRFGN
LPEEAINLLK SVSLKWLASE IGFEKIVMKN GVFLGYFPGN PQDKFYQTDK FRHIINYLTK
NPAEAQLKEK VGKEGNQLMM RKDRIQNVDE VNKLLKSMLT TN
//
