GenomeNet

Database: UniProt
Entry: S5THF5_9CORY
LinkDB: S5THF5_9CORY
Original site: S5THF5_9CORY 
ID   S5THF5_9CORY            Unreviewed;      1225 AA.
AC   S5THF5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
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=B841_04410 {ECO:0000313|EMBL:AGS34361.1};
OS   Corynebacterium maris DSM 45190.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1224163 {ECO:0000313|EMBL:AGS34361.1, ECO:0000313|Proteomes:UP000015388};
RN   [1] {ECO:0000313|EMBL:AGS34361.1, ECO:0000313|Proteomes:UP000015388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Coryn-1 {ECO:0000313|Proteomes:UP000015388};
RA   Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT   "The complete genome sequence of Corynebacterium maris Coryn-1 (=DSM
RT   45190).";
RL   Submitted (NOV-2012) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003924; AGS34361.1; -; Genomic_DNA.
DR   AlphaFoldDB; S5THF5; -.
DR   STRING; 1224163.B841_04410; -.
DR   KEGG; cmd:B841_04410; -.
DR   PATRIC; fig|1224163.3.peg.881; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_2_0_11; -.
DR   Proteomes; UP000015388; 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:UP000015388}.
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"
FT   REGION          1206..1225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1225 AA;  134714 MW;  28F03DCAC467C032 CRC64;
     MAAKTTKADP AMLAGLLKVA ATDPKLKGLA GNVGQRRLHI EAIDQARPWT IGTLAHHAPV
     LVVTATGREA EDLAAELRAM MGDKVAWFPS WETLPHERLS PGADIVGRRA EILHNLADYR
     VVVTAARGFC QPILERAEGR APIVLAEDEE HDLGEITDQL VFRAYSHVDL VAKRGEFAVR
     GGILDVFPTT LDHPVRVEFW GDEITDVRQF SVADQRTLDD VEVGRVEIYP ARELPVTDDV
     AARARALSTQ YPGNATLVEL LTKLGDRIPA DGMEALIPVL SDSPLVTLPD FLPEDAHVLL
     IAPEKIRTRI ADLESTDAEF LAAGWEAAAM GASGPIAAEG LDLSASSYRS FEELEEAARD
     NGTPWWTFAP PGMFAADEAA TLPLEYEPGP APRGADQEIA AMMAELRAHT TAGGRAAFIA
     PAEGAIKRMV ERFREQGVPA KVATPGWEPT PGEITLYQAL SHAGLVFPKV RKHKDAEALP
     LVVVTETDLT GNRVGDIAGA KRRPAKRRNR VDPLALKTGD YVVHETHGIG RFLKMAERTI
     NTGDETSRRE YIVLEYAPAR RGQPADQLWV PMESLDILSK YSGGEAPTLS KMGGSDWKNT
     KKKARAAVRE IAGELVELYA KRQAAPGRKF GPDTPWQAEM EDNFPFVETE DQMEAIEAVK
     HDMERTTPMD RVIVGDVGYG KTEVAVRAAF KAVQDGTQVA VLVPTTLLAQ QHTKTFIQRM
     DGFPITIREL SRFTSTAESK EILSGLADGS VDVVIGTHRL LQTGVNWKNL GLIIVDEEQR
     FGVEHKEHIT ALRSHVDVLT MSATPIPRTL EMSMSGIREM TTMLTPPEDR HPVLTYVGAY
     EDKQVAASIR RELLRDGQVF FIHNKVADIE KKARELRDLV PEARIVVAHG QMSEEQLERT
     VQGFWDREYD VLVCTTIVET GLDIANANTL IVENAHHMGL SQLHQLRGRV GRSRERGYAY
     FLYPKGATLS ETSYDRLATI AQNNDLGAGM AVAQKDLEMR GAGNVLGAQQ SGHIAGVGFD
     LYVRLVGEAV EAYKALAKGE TIDATDQAPK EIRIDLPVDA HIPESYINSE RLRLEIYRKI
     ASSKDNTDLQ LIVEEMEDRY GPVPEEVSRL LAVARLRHQA RRAGVTDIGV QGTRIKVHPV
     ELADSKQVRL KRLFPGSNYR AAAKAIQLSF PKAGRNVTAP KLRDEELLQW MADFLSSMFD
     VDATDVTGGE GKKKARKGKV FSVSE
//
DBGET integrated database retrieval system