ID A0Z9F2_9GAMM Unreviewed; 1150 AA.
AC A0Z9F2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 83.
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=MGP2080_12287 {ECO:0000313|EMBL:EAW39396.1};
OS marine gamma proteobacterium HTCC2080.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX NCBI_TaxID=247639 {ECO:0000313|EMBL:EAW39396.1, ECO:0000313|Proteomes:UP000004719};
RN [1] {ECO:0000313|EMBL:EAW39396.1, ECO:0000313|Proteomes:UP000004719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2080 {ECO:0000313|EMBL:EAW39396.1,
RC ECO:0000313|Proteomes:UP000004719};
RX PubMed=20472793; DOI=10.1128/jb.00511-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the
RT OM60/NOR5 clade of the Gammaproteobacteria.";
RL J. Bacteriol. 192:3842-3843(2010).
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:EAW39396.1}.
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DR EMBL; AAVV01000021; EAW39396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0Z9F2; -.
DR eggNOG; COG1197; Bacteria.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000004719; 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}; Reference proteome {ECO:0000313|Proteomes:UP000004719}.
FT DOMAIN 618..779
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 792..954
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1150 AA; 127588 MW; A1BE8295E5FFC021 CRC64;
MFSTLVASTP WPEKQGSRSA LGPCPGTATA MAVAELAKQQ ALLVVVVPSS ASAAALEREL
PLFSAADLNV LTLPDWETLP YDNFSPHQDI VSERLSTFHQ LKDIASGILI VPITTLMQRT
PPVHYVAGNS LVLDVGQALD SKTLIHNLTL NGYRAVDTVY EHGEYAVRGS LLDIFPMGSQ
VPYRIDLFDA EIESLRTFDP ENQRTISKVE SIRLLPAREF PLTEEGIRRF KLNWYRKFDG
DPEACPLFNE ICAGRVPGGA EYFLPLFFDS CGTVFDYIPD HAALITLGDH YQAASQFWTE
ITSRHTEYGV DVRRPLLPPS EVFIPTEVLY EDLRSYAVLE LRTEQDAPVH QKTGLLPPPN
LNDTYQGATA LERLAAFIEK HEGPVLLCAE SPGRREVLLE GLNELGLHPE PVAEWPEFIA
QGISLGITVA PVDRGLYQGK GQPTLIVENQ IFGARVAQRR RRRTVEENNA DAIVRDLTEL
RPGVPVVHLQ HGVGRYMGLQ SLEIDGAPAE FLLLQYADAD KLYVPVGSLH LIARYTGADP
DTAPLHRLGS EQWEKARRRA REKANDVAAQ LLEVYARREA RQGFQCELDE TAWQRFSEEF
PFEETPDQSA AIEAVRADMC ATKVMDRLVC GDVGFGKTEV AMRAAFIAIQ NNKQVAILVP
TTLLAQQHYN SFRDRFADWP VKVEVVSRFQ SNSDITSVQK RVASGDVDLL IGTHKLLQST
FAFEDLGLLV IDEEHRFGVK QKEAIKALRA QVDILTMTAT PIPRTLNMAL GGLRDLSIIA
TPPARRLSIK TFVREHSISL VKEAILRETL RGGQVYYLHN EVKTIEETAS RLREMLPNLS
VGVGHGQLRE TALEGVMTDF YHLRHHILVC STIIETGIDI PNANTIIIDR ADKFGLAQLH
QLRGRVGRSH HQAYAYLLCP PRSTMTSDAE KRLEAIEAAG ALGAGYLLAT HDLEIRGAGE
LLGDEQSGQI HSVGFGLYLD MLNNAVRALK RGEIPDVDGP LDSGTEVKLH IPALIPDDYL
PDITSRLVLY KRIAASMTHE ALREIQVEMI DRFGLLPDAT KNLFTQATIR VRAQRLGIAE
IEVGDGGGSI AFTDKTQVEP MTLVKLVQGD PKTYGLAGSN KLRFSCELPE LPERQSFIES
LLEKLDQETS
//
