ID W9G618_9MICO Unreviewed; 1207 AA.
AC W9G618;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=N865_09945 {ECO:0000313|EMBL:EWT01596.1};
OS Intrasporangium oryzae NRRL B-24470.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Intrasporangium.
OX NCBI_TaxID=1386089 {ECO:0000313|EMBL:EWT01596.1, ECO:0000313|Proteomes:UP000019489};
RN [1] {ECO:0000313|EMBL:EWT01596.1, ECO:0000313|Proteomes:UP000019489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24470 {ECO:0000313|EMBL:EWT01596.1,
RC ECO:0000313|Proteomes:UP000019489};
RA Liu H., Wang G.;
RT "Intrasporangium oryzae NRRL B-24470.";
RL Submitted (AUG-2013) 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:EWT01596.1}.
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; AWSA01000020; EWT01596.1; -; Genomic_DNA.
DR RefSeq; WP_034805494.1; NZ_AWSA01000020.1.
DR AlphaFoldDB; W9G618; -.
DR STRING; 1386089.N865_09945; -.
DR PATRIC; fig|1386089.3.peg.2206; -.
DR eggNOG; COG1197; Bacteria.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000019489; 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:UP000019489}.
FT DOMAIN 657..818
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 836..993
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 484..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1207 AA; 132187 MW; 903869A3A2F363FC CRC64;
MPHALLPAFQ ALPDVQRVLA EVGRSRLVDV SASDGTRPFL VSALAERVAA EAAGTGAPVL
VVTATTREAE DLSDALGAFL PAERLAVFPS WETLPHERLS PRSDTVGRRL AVLRRVAHPD
PDDTAYGPLS VVVAPVRAIL QPVTRGLGEL VPVALRAGDE RPLGDVVEAL VGAAYTRTDL
VERRGEFAVR GGILDVFPPT EEHPVRVEFW GDTVEEVRWF KVADQRSLEI AEHGLWAPPC
REVLLTESVR ARAKALADQL PGVADMLSKV AEGIAVEGME SLAPALVDGM EPVLDVLPAE
SIIVLADPER IRRRAHDLVA TSDEFLEASW ANAAAGNAVP VDLQSLLGSA SYWTLAQVRA
HAIAHDRAWW TLTPFAADEE LVIEDDDVDA RLAVRTVDPE AFRGDTERAV GHLRERAAEG
WRVAVVTEGP GLAKRVEEVL REQEVPVRAL AGGELEAGIV SVCTAPLGRG FVHEGERLEV
LTETDLTGQP GGGPSTKDMR RMPSRRRNQV DPLQLRPGDF VVHEQHGVGR FVEMMQRTVA
GATREYLVIE YAASKRGQPG DRLFVPTDQL DQVTKYVGGE EPTLNKMGGS DWTKTKSRAK
RYVKQIAADL IRLYSARQAT KGHAFSADTP WQRELEEAFA YVETPDQLSS IDEVKADMEK
QVPMDRLICG DVGYGKTEIA VRAAFKAIQD GKQVAVLVPT TLLVSQHFQT FSERYAQFPV
KVAALSRFQT DREAKDVLDG IADGTIDLVI GTHRLLAKEV RFKDLGLVII DEEQRFGVEH
KELLKTMRTA VDVLSMSATP IPRTLEMAVT GIREMSTLAT PPEERHPVLT FVGGYDEKQI
TAAIRRELLR EGQVFFVHNK VSSIEKAAAR LRELVPEARI ATAHGQMGEH KLEAVVEDFW
QKRFDVLVCT TIVETGLDIS NANTLIVERA DMLGLSQLHQ LRGRVGRGRE RAYAYFLYPP
EKPLTETAHD RLRTIASHTD LGAGMQVAMK DLEIRGAGNL LGGEQSGHIA GVGFDLYVRL
IGEAVADFRG ETTDVPAEIK IELPVDAHLP HDYVPGERLR LEAYKKLATV ETFEAVDEIE
AELRDRYGAP PEPVQNLLEV ARLRVVARRA KIGDIGLQGK VVRFGPVKDL RESQQLRLMR
LYPGTLVKEA LGTMLVPVPM TARVGGKPLR NTEILMWARQ LISAVLLDDI AAGAMASAAA
TSAAGAP
//
