ID S9RPS9_9RHOB Unreviewed; 1156 AA.
AC S9RPS9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=Salmuc_00671 {ECO:0000313|EMBL:EPX76019.1};
OS Salipiger mucosus DSM 16094.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX76019.1, ECO:0000313|Proteomes:UP000015347};
RN [1] {ECO:0000313|Proteomes:UP000015347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX PubMed=25197501; DOI=10.4056/sigs.4909790;
RA Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT clade.";
RL Stand. Genomic Sci. 9:1331-1343(2014).
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:EPX76019.1}.
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DR EMBL; APVH01000061; EPX76019.1; -; Genomic_DNA.
DR RefSeq; WP_021120933.1; NZ_KE557285.1.
DR AlphaFoldDB; S9RPS9; -.
DR STRING; 1123237.Salmuc_00671; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_5; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000015347; 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:UP000015347}.
FT DOMAIN 614..775
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 796..950
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1156 AA; 127396 MW; CABBEF0227E6CDC5 CRC64;
MSQTKLTIGG APEGFDATLV LAEAEKAGGP VIHVARDDKR MAAMAEALAF FAPDMPVLHF
PAWDCLPYDR VSPNPDISAA RMATLAGLVH GMPERFVLLT TLSAATQYIP AREVLREAAF
SARVGNRVDE AALRAFLVRM GFVQAPTVTE PGDYAIRGGI IDIYPPGEGG PVRLDLFGDV
LDGARRFDPV SQRTTEKLET VELAPVSEVI LDESAITRFR QNYRVEFGAG TSDDPLYEAV
SAGRKQQGME HWLPFFHERL ETLFDYMPQA PVLMDDQLTP ARLARWESIE DQYDTRRHAM
SQKGRMDSVY KPVPPDQLYL DDDAWESALA DRRAVQFHPL AQASGPGVVD AGGRIGRNFA
PERQQENVNL FSALADHIKA KLQEGPVLIA SWSEGARERL SGLLEDEGLA EAIPVANGTR
MGRRGLHLAV WALESGFEAP RGDDRMTVIS EQDVLGDRLI RAPKKRRKAE NFLTEAQALT
PGDLVVHVDH GIGRYHGLEV VTAAGAAHEC LLLEYAEGAR LYLPVENIEL LSKYGHDEGL
LDKLGGGAWQ AKKARLKERI KEIADRLIRV AAERALRKAP AIDPPPGAWE SFCARFPYNE
TDDQLGAIHD VVEDMTSGQP MDRLICGDVG FGKTEVAMRA AFIAAMSGVQ VAVIAPTTLL
ARQHYKSFAE RFRGFPINVA PLSRFVSSSQ AAKTREGISK GTVDIAVGTH ALLAKNIRFQ
NLGLLIIDEE QHFGVSHKER LKQLRTDIHV LTLTATPIPR TLQLSLSGVR ELSIIGTPPV
DRLSIRTYVS EFDAITIREA LLREHYRGGQ SFFVVPRLTD LPEIEEFLRE QVPEVSFVVA
HGQMPAGELD DKMNAFYDGK FDVLLATTIV ESGLDIPTAN TMVVHRADMF GLSQLYQIRG
RVGRSKTRAY AYLTTRPRAK LTDSAQKRLR VLGSLDTLGA GFTLASQDLD IRGAGNLLGE
EQSGQMRDVG YELYQSMLEE AISKIKSGET EGLTDDDGQW APQINLGVPV LIPEDYIPDL
DVRLGLYRRL SELTTKVELE GFAAELIDRF GPLPKEVNTL LLVVRIKAMC KRAGIAKLDG
GPKGATIQFH NDKFARPEGL VEYIKAQDGL AKIKENKIVV RRDWKKDSDK IKGAFAIARD
LAEKAGAIKT REPAKA
//
