ID T1ZC42_STRIT Unreviewed; 1168 AA.
AC T1ZC42;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-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=trcF {ECO:0000313|EMBL:AGU75425.1};
GN Synonyms=mfd {ECO:0000256|HAMAP-Rule:MF_00969};
GN ORFNames=SIR_0007 {ECO:0000313|EMBL:AGU75425.1};
OS Streptococcus intermedius B196.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=862967 {ECO:0000313|EMBL:AGU75425.1, ECO:0000313|Proteomes:UP000016233};
RN [1] {ECO:0000313|EMBL:AGU75425.1, ECO:0000313|Proteomes:UP000016233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B196 {ECO:0000313|EMBL:AGU75425.1,
RC ECO:0000313|Proteomes:UP000016233};
RX PubMed=24341328; DOI=10.1186/1471-2164-14-895;
RA Olson A.B., Kent H., Sibley C.D., Grinwis M.E., Mabon P., Ouellette C.,
RA Tyson S., Graham M., Tyler S.D., Van Domselaar G., Surette M.G.,
RA Corbett C.R.;
RT "Phylogenetic relationship and virulence inference of Streptococcus
RT Anginosus Group: curated annotation and whole-genome comparative analysis
RT support distinct species designation.";
RL BMC Genomics 14:895-895(2013).
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; CP003857; AGU75425.1; -; Genomic_DNA.
DR AlphaFoldDB; T1ZC42; -.
DR KEGG; sib:SIR_0007; -.
DR PATRIC; fig|862967.3.peg.7; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_9; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000016233; 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:UP000016233}.
FT DOMAIN 630..791
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 812..966
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1168 AA; 135217 MW; D3D45AC4B6887F3F CRC64;
MDKEMDIIEL FNQNKQIADW QRNLNKSTRQ LLMGLSFSTK IITMASCVES NHKILILTST
YSEAEKLSSD LIGLVGEEKV YTFLADDTPL SEFIFFSQEK IFSRLEALDF LLNSQKSGFL
IVNVAASQLF LPNPVNFNSA YINLKIGQEY DLNDLIFQLS NSGYKRVLQV LNQGEFSLRG
DILDIFERSS QMPFRIEFFG DEVDSIRLFD PESQVSIQNV ESVCIHPATD VLFTTVDYKN
AQKKIETQIE KTVDSTLKSY LEEILDSIKK QIQHADVRKL LSIFYQNKWT ILDYLPKHSP
IFFDDFQKII NKHTQFQLEA ADLLTENLQN GKSVVKQSYF ADVYSVFRKY KPATFFSNFH
KGFGNLKFDS LYQFNQYPMQ EFFSQFQLLK EEISRYKKSN YTVILQSNSS LTFQSLHKAL
QEYNIPLDYV NDNKIHEHAI QLVKGSLIQG FNFVDEKIVL ITEYDILQKK VKRKVRRQNL
SNAERLKNYN ELEKGDYVVH NVHGIGRYLG IETIEISGIH RDYLTIQYQN ADRISIPVDQ
IHLLSKYVAS GGKEPKINKL NDGRFQKTKQ RVQHQVEDIA EDLIKLYAER SQLKGFAFSS
DDSYQQEFDN AFPYIETEDQ LRSIKEVKKD MESDYPMDRL LVGDVGFGKT EVAMRAAFKA
VNDHKQVAIL VPTTVLAQQH YTNFKERFND FPINIEVLSR FKSKSEQKII LEKLKKDQVD
IIIGTHRLLS KDVAFADLGL IVIDEEQRFG VKHKEKLKEL KTKVDVLTLT ATPIPRTLHM
SMLGIRDLSV IETPPTNRYP IQTYVLESNS TVIRDAVLRE MDRGGQIYYL YNKVDTMEQK
VSELKTLLPE ASIGYVHGQM SEILLESTLL DFINGEYDLL VTTTIIETGV DIPNVNTLFI
ENADHMGLST LYQLRGRIGR SNRIAYAYLM YHPDKSLTEI SQKRLETIKG FTELGSGFKI
AMRDLSIRGA GNILGSSQSG FIDSVGFEMY SQLLEEAIAK RQGKEIKRKK GNAEINLQID
AYLPTDYIAD ERQKIEIYKR IHEIDSRVNY EELQNELIDR FGEYPDVVAF LLEIGLIKFY
LDQVFVQLIE RKQQSVVVQF EKVSQRFFLT QDYFKALSVT DLKARITEDK GLIEVIFDVR
NKKDYKILEE VMKFSKKLIE IKNKKKDY
//
