ID A0A0N6ZXI9_9MICO Unreviewed; 1203 AA.
AC A0A0N6ZXI9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=NI26_03765 {ECO:0000313|EMBL:AIV39569.1};
OS Curtobacterium sp. MR_MD2014.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1561023 {ECO:0000313|EMBL:AIV39569.1, ECO:0000313|Proteomes:UP000069933};
RN [1] {ECO:0000313|Proteomes:UP000069933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR_MD2014 {ECO:0000313|Proteomes:UP000069933};
RA Mariita R.M., Bhatgnagar S., Hanselmann K., Hossain M.J., Dawson S.C.,
RA Korlach J., Boitano M., Liles M.R., Moss A.G., Leadbetter J.R.,
RA Newman D.K.;
RT "Isolation and characterization of species affiliated with family
RT Actinomycetaceae.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AIV39569.1, ECO:0000313|Proteomes:UP000069933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR_MD2014 {ECO:0000313|EMBL:AIV39569.1,
RC ECO:0000313|Proteomes:UP000069933};
RX PubMed=26722011;
RA Mariita R.M., Bhatnagar S., Hanselmann K., Hossain M.J., Korlach J.,
RA Boitano M., Roberts R.J., Liles M.R., Moss A.G., Leadbetter J.R.,
RA Newman D.K., Dawson S.C.;
RT "Complete Genome Sequence of Curtobacterium sp. Strain MR_MD2014, Isolated
RT from Topsoil in Woods Hole, Massachusetts.";
RL Genome Announc. 3:0-0(2015).
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; CP009755; AIV39569.1; -; Genomic_DNA.
DR RefSeq; WP_066652554.1; NZ_CP009755.1.
DR AlphaFoldDB; A0A0N6ZXI9; -.
DR STRING; 1561023.NI26_03765; -.
DR KEGG; cum:NI26_03765; -.
DR PATRIC; fig|1561023.3.peg.791; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000069933; 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; 3.40.50.11180; -; 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; 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:UP000069933}.
FT DOMAIN 662..823
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 848..998
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1203 AA; 130356 MW; DB36E904D8E46EAE CRC64;
MTISGIIPAL SRASAFDRVL RAAGRDADFS VVDGLRVPLL GALLAERNGP QCLFVVTATG
REAEAVRGAF TCTVPDAEVL EFPAWETLPH ERLSPSAQTV GTRIATLRKL AAWQDADPAD
RRTIVVVASV RAALQPIAGN LTSLAPVALA TGSRGNDLAA IASQLVDLAY ARVDLVTRRG
EFAVRGGILD VFPPGADHPV RVDFFGDEIE AIKAFSVADQ RTTDDDLGSV ELTASRELLL
SDDVRQRARE MLHEFPNLSQ MLAKIAEGIP VEGMESLAPA LVQDLVPITT YLPETATIAV
LSPERVAGRA HSLAETNTEF LQAAWSAAVA GAQAPIDLDA GNFLSVQQLK NTRGQRTWWT
VTPFDSGLDE GDRERVLTDA EAAAEAGEYI RVRAESIPSF AGSADGAVEH VKQLVDDGWG
VVVTAQGKGL VERAVQVLAD AGVAARAEDL TAPPEPGVAI VTTATVEAGF ATPDPRIAVL
SEAEFYGRSV QQGARTVKKL AARRKNVVDP LQLKPGDVVV HNTHGIGKFV ELVSREVSSG
GRNAVKTQRE YLVLEYAPSK RNYPGDKLFV PTDQLDQLSR YVGGENPTLS KMGGSDWSAA
KSKARKAVRD IAVDLVKLYS ARMASKGHAF GPDTPWQREL EEAFPFAETA DQLTTIDEIK
RDMESPIPMD RLLSGDVGYG KTEVAIRAAF KAVQDGKQVA VLVPTTLLVR QHMETFQERF
AGFPVHLRAL SRFQTEKESK ETIAGLADGT VDIVIGTHRI LSQNIAFKDV GLVIIDEEQR
FGVEHKDQLK KLKTNVDVLA MSATPIPRSL EMAVTGIREM STLATPPEDR HPILTFVGPQ
SDLQVAAAIR RELLREGQVF YVHNRVKDIQ SVASHLAEII PEARIQVAHG QMSEGTLEQV
MVDFWERKFD VLVSTTIVET GLDIANANTL IIDKADKYGL SQLHQLRGRV GRGRERGYAY
FLYDADKPLS ETAQDRLETI AANNELGAGM QVAMKDLEIR GAGNLLGGEQ SGHIAGVGFD
LYLRMIGEAV SQFRGDVAEG QTELRLEIPV DAHIPEDYVE SERLRLEAYQ KLSAASAPAA
QPEAIDMVLD ELTDRYGQPP QPVLTLVEVS RLRRMAQQVG LSDVVVMGSN LRIAGKELAD
SAQVRLKRMF PGARWFPQQD AASIPLPKPH GETLPDDGLI EWVESILTAV YGASKAPAEA
PAS
//
