ID A0A0T2QFK0_9SPHN Unreviewed; 1163 AA.
AC A0A0T2QFK0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=ASD76_05690 {ECO:0000313|EMBL:KRA83532.1};
OS Altererythrobacter sp. Root672.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=1736584 {ECO:0000313|EMBL:KRA83532.1, ECO:0000313|Proteomes:UP000051125};
RN [1] {ECO:0000313|EMBL:KRA83532.1, ECO:0000313|Proteomes:UP000051125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root672 {ECO:0000313|EMBL:KRA83532.1,
RC ECO:0000313|Proteomes:UP000051125};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA83532.1, ECO:0000313|Proteomes:UP000051125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root672 {ECO:0000313|EMBL:KRA83532.1,
RC ECO:0000313|Proteomes:UP000051125};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRA83532.1}.
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DR EMBL; LMHH01000001; KRA83532.1; -; Genomic_DNA.
DR RefSeq; WP_055919697.1; NZ_LMHH01000001.1.
DR AlphaFoldDB; A0A0T2QFK0; -.
DR STRING; 1736584.ASD76_05690; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000051125; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000051125}.
FT DOMAIN 621..782
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 803..957
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 553..580
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1163 AA; 128881 MW; 309A686875B1EC10 CRC64;
MADFSRIISA RHPLSLTSVA RGSQPLVLAD LARAAKGRAV FVAPDEQAMR AVTDAARWFA
PELQVIEFPA WDCLPYDRAS PALSVSSRRL AALHQLQAGK TTSQLLVTTV NAVLQRVLTP
FRIREAVREL KPGIQIGYES LTALLQRQGY SRTDTVIDTG EFAVRGSIFD VFPAGLEQGL
RLDFFGDELE SLRLFDPTTQ RTTSTVDGHL LLPASEALID DDSIKRFRSN YRERFGANAT
QDPLYQAVSD GRRLAGMEHW LPMFEDRLAT LFDHLSADDL IVIDSSAVAA GEERLTDVED
YHRQRMETAG QAAGSYRPLP ADALYLTRSE FTNALEAHPV HRAVIFAEPE SDKVIDFGFR
SARDFTPERS QGANVYEAAA AHFKALGKSG KRPLLAAYSE GSRSRITSIL GESGTEMKLA
GSWQEALGLS AKGAPVAMVL PLDTGFSNDE LELVTEQDLL GDRLVRRRKR KKDSDAFLAE
LSALNRGDLV VHLDHGIGKY LGLEPITVGK SQHDCVMLEY AGGDKLYIPV ENIDVLSRYG
SGEDGAVLDR LGGEGWQKRK ARLKERIREI ANELLRTAAA RALRRAPVLE PEENAFNQFV
ERFPWQETED QEQAIDDVLR DLSEGKPMDR LVCGDVGFGK TEVALRAAFV AAMNGQQVAV
VAPTTLLARQ HFQGFAERFN GFPLRIGRLS RLVPANEMKA TRDGLTDGTM DVVVGTHAIL
SKTTKFKRLG LVIVDEEQRF GVAHKEALKQ LRADVHVLTL TATPIPRTLQ MAMSGLRELS
TIQTPPVDRL AVRTYVMEWD DMVMREALLR EHHRGGQSFI VVPRIADMEQ VAEWLHKYVP
EIKVVTAHGQ MAPSEVEERM SAFYEKRYEV LLSTTIVESG LDIPSANTII IHRADRFGLA
QLYQLRGRVG RSKLRAYAYL TTPKDRQMSE VAEKRLKVLG DLDSLGAGFQ LASHDLDIRG
AGNLLGDEQS GHIREVGFEL YQSMLEDAIL AAKAGDMGIE REREGLSPQI TVDAPIMIPD
DYVPDLAVRM ALYRRLNDAK DKAEIEAMAA EMIDRFGPLP DATANLIKLI EIKHQAIEAC
IAKIEVGARG TLVSFHNDQF PDPVGLIAYV ERLKDTARLR PDMKLVINRA WGDPQSRLNG
LVQLTKGLSA IVRKAAKREK AAA
//
