ID A0A0G9MX70_9SPHN Unreviewed; 1165 AA.
AC A0A0G9MX70;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=AAW00_02820 {ECO:0000313|EMBL:KLE35387.1};
OS Aurantiacibacter luteus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=1581420 {ECO:0000313|EMBL:KLE35387.1, ECO:0000313|Proteomes:UP000053464};
RN [1] {ECO:0000313|EMBL:KLE35387.1, ECO:0000313|Proteomes:UP000053464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA37 {ECO:0000313|EMBL:KLE35387.1,
RC ECO:0000313|Proteomes:UP000053464};
RA Zhuang L., Liu Y., Shao Z.;
RT "The draft genome sequence of Erythrobacter luteus KA37.";
RL Submitted (APR-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:KLE35387.1}.
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DR EMBL; LBHB01000001; KLE35387.1; -; Genomic_DNA.
DR RefSeq; WP_047002788.1; NZ_LBHB01000001.1.
DR AlphaFoldDB; A0A0G9MX70; -.
DR STRING; 1581420.AAW00_02820; -.
DR PATRIC; fig|1581420.6.peg.566; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000053464; 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; 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:UP000053464}.
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"
SQ SEQUENCE 1165 AA; 128474 MW; 28AA61D2D965B2C2 CRC64;
MPDLSRILTA QQPLTLAQVA RGAQPLVMAD LARAAKGRAV FVAADDAAMH AVAEAARFFA
PELQVIEFPA WDCLPYDRAS PALSVSAARL SALYQLQAGK KGAQLLVTTV NALLQRALTP
FRIRESVREF KVGIEIGHES LAALLRRQGY TRVDTVVDTG EFAMRGSIVD IYPSGLEAGL
RLDFFGDELE SLRLFDPSTQ RTTGVIDQHL LLPASEALLD EDSIKRFRSR YRETFGAAAT
QDPLYEAVSD GRRLAGMEHW LPLFEEKLAT LFDHLGKDDV VVIDNAAMAA GEERLTDIAD
YYRQRGETAG QKKGSYRPLD PARLYLTGEE FHAALADWPI HRANIFAEPE SERVVDFSFR
SARDFTPERS QGANVYEAAA AYLKSVGKAG KRPLLAAYTK GSLSRIASII EEAGTKVATV
ETWQEALGKA AKGTAAAMVL PLDTGFANDE LELVTEQDLL GDRLVRRRRK KKDADAFLAE
LQALSRGDLV VHVDHGIGKY IGLEPVPVGQ SQHDCVMLEY KGGDKLFIPV ENIDVLSRYG
SSEEAVMLDK LGGEAWQRRR ARLKERIREI AGELMRVAAA RALRKAPVLP ADESSYGQFL
DRFPWEETDD QEAAIADVLR DLESGRPMDR LVCGDVGFGK TEVALRAAFV AAMNGQQVAV
VAPTTLLARQ HFQNFSQRFA GFPLKVGRLS RLVPSGEMKA TREGLESGDI DVVIGTHAIL
SKNTKFKNLG LVIVDEEQRF GVTHKEKLKQ LRADVHVLTL TATPIPRTLQ MAMSGLRELS
TIKTPPVDRL AVRTYVMEWD DMVVREALLR EHHRGGQSFI VVPRISDMEQ VEGWLREFVP
EVKAVSAHGQ MGASEIEERM SAFYEGKYEV LLSTTIVESG LDLPSANTII IHRADRFGLA
QLYQLRGRVG RAKIRAYAYL TTPADTQLSE VAEKRLKVLG DLDSLGAGFQ LASHDLDIRG
AGNLLGDEQS GHIKEVGFEL YQSMLEDAIL AAKAGDAGID TERRGLSPQI TVDAPIMIPE
DYVPDLAVRM ALYRRLNETQ DQAEIEGLAA EMIDRFGELP QATKNLIRLI EIKAQAVDAC
IAKVDVGARG TLVTFHEDRF PDPAGLIAYV ERLNEGRAES AKLRPDMKLQ INRAWGDPQS
RLNGLFQLTK GLSGIVKRAE KKKAA
//