ID E1VTU0_GLUAR Unreviewed; 1204 AA.
AC E1VTU0;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 79.
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 ECO:0000313|EMBL:CBT75043.1};
GN OrderedLocusNames=AARI_08170 {ECO:0000313|EMBL:CBT75043.1};
OS Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM 15318 /
OS JCM 13566 / NCIMB 14258 / Re117) (Arthrobacter arilaitensis).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Glutamicibacter.
OX NCBI_TaxID=861360 {ECO:0000313|EMBL:CBT75043.1, ECO:0000313|Proteomes:UP000006878};
RN [1] {ECO:0000313|EMBL:CBT75043.1, ECO:0000313|Proteomes:UP000006878}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC {ECO:0000313|Proteomes:UP000006878};
RX PubMed=21124797; DOI=10.1371/journal.pone.0015489;
RA Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B.,
RA Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., Irlinger F.,
RA Vallaeys T.;
RT "The Arthrobacter arilaitensis Re117 genome sequence reveals its genetic
RT adaptation to the surface of cheese.";
RL PLoS ONE 5:E15489-E15489(2010).
RN [2] {ECO:0000313|Proteomes:UP000006878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC {ECO:0000313|Proteomes:UP000006878};
RA Genoscope.;
RT "Complete genome sequence of Arthrobacter arilaitensis (strain DSM 16368 /
RT CIP 108037 / JCM 13566 / Re117).";
RL Submitted (JUL-2010) 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}.
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DR EMBL; FQ311875; CBT75043.1; -; Genomic_DNA.
DR RefSeq; WP_013348189.1; NC_014550.1.
DR AlphaFoldDB; E1VTU0; -.
DR STRING; 861360.AARI_08170; -.
DR KEGG; aai:AARI_08170; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_0_3_11; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000006878; 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:UP000006878}.
FT DOMAIN 663..824
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 849..999
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1204 AA; 132615 MW; 3BE49C21734FF07E CRC64;
MSLTGLHDFL REEPSFRRIR QSATHEYATR SEALEIAAPQ GMRSLLSAHI SQALGESKNP
GVTLIVTATG REAEEISTSL GAYLPAEQIA EFPSWETLPH ERLSPRSDTV GRRLEVLRRL
HDRDQALNII IAPIRAVLQP LVAGLGQLRP VRLELDDEPG FDAVIKDLAA AAYARVDMVT
HRGEFAVRGG IIDVFPPTLD HPVRIDFFGD QIDSMRYFSI ADQRSTAEDG PQRIIATPCR
EMLITPKVMS RAANLKNHFP AAQEMLTKIA GGIAVEGMES LAPLLVDQMV PLLSLLPECS
IALVMEPERV RARAHDLNAT NAEFLAAAWA SASDGASAPL DLNTADSERK LASGDFASLA
ETVQHAHQAK VSWWALTSMG ADEELELGSS TIRIPAREPL GYQGDIEAMM EFIAGRVKDQ
WRFVVATEGP GPAARLSELF ADFKIPAHRV EDISATPTAG LIEITQATAG RGFVFEELKL
GLLTEADLLG RSSAYPNRKG RKLTVKRKRN AVDPLSLQAG DFIVHEQHGI GKFVELMARK
VNGSGKDAKR EYLVVEYASS KRGAPGDRLF VPMDQLHMVT RYVGGEAPTL SKMGGSDWSS
TKSKARKAVK EIAGDLIKLY SARMASRGHA FGPDTPWQNE LEEAFAFIET PDQLTAINEV
KSDMEKEIPM DRLISGDVGF GKTEIAVRAA FKAVQDSKQV AVLVPTTLLA SQHHQTFTER
YSGFPVRVKT LSRFQTAKES KEILAGLKDG SVDIVIGTHR LLSKNVEFKN LGLVIVDEEQ
RFGVEHKEEL KKMRTNVDVL AMSATPIPRT LEMSLTGIRE TSTLATPPEE RHPVLTYVGP
RSDKQISAAI KRELMRDGQV FFVHNRVSSI ERVAAELREL APEARIEVAH GKMSESRLER
IIQDFWEKKF DVLVSTTIIE TGLDISNANT LIVDRANNYG LSQLHQLRGR VGRGRERAYA
YFLWDVEKPL GEVALERLKA VAAHNELGSG YQLAMKDLEL RGAGNLLGGE QSGHIAGVGF
DLYLRLVGEA VADYKGEGEE ESTEMKIDLP VNAHLPHNYV PGERLRLEAY RNIAQAETNE
ALAEVREELE DRYGKLPEPV ENLLRVAALR IRARAVGLHD IQQVGNHIKV SPAKIEDLPA
SRQVRLERLY PGSANKPALN SIFIPKPKTS PVGGRDLADE AMLDWAENLV YAIFEPTPVA
AAKG
//
