ID A0A327ZHR1_9ACTN Unreviewed; 1206 AA.
AC A0A327ZHR1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=B0I29_103376 {ECO:0000313|EMBL:RAK40343.1};
OS Actinoplanes lutulentus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1287878 {ECO:0000313|EMBL:RAK40343.1, ECO:0000313|Proteomes:UP000249341};
RN [1] {ECO:0000313|EMBL:RAK40343.1, ECO:0000313|Proteomes:UP000249341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7090 {ECO:0000313|EMBL:RAK40343.1,
RC ECO:0000313|Proteomes:UP000249341};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUN-2018) 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:RAK40343.1}.
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; QLMJ01000003; RAK40343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327ZHR1; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000249341; 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:UP000249341}.
FT DOMAIN 667..828
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 846..1003
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1206 AA; 132326 MW; C305B9CA4E2C4CE9 CRC64;
MQLAGLIPAA LRDRGLARAR DLARKGFVDS DSLDLTAPAS LRPFVVATVA GASEAGGAQR
PVLAVTATSR EADDLADALG CLIDADRIAV YPSWETLPHE RLSPRSDTVG KRLAVLRRLA
HPDEHPLQVI VAPVRSLLQP QLKGLGDLEP VELVTGRGAE LEDVARRLSD MAYARVDLVT
KRGEFAVRGG ILDVFPPTDE HPSRVEFWGD DVEEIRTFAV ADQRTIDKVE RLWAPPCREL
LLTPDVRAKA AELAAEHPEL AEILDKLAEG IPVEGMESLA PALLHGTDSM ELLIDCMPAG
THVLLCDPER IRTRAHDLTR TSDEFLEASW AAAAVGGQAP IDVGAVAFRT LAEIRAHAAT
LKQPWWTLSP FGLVSSEAAA ESLPWEDSSE AVEVSPDAGD AIALAAQPVP LYHGDTAKLA
GDLAEWARAG WAIALVFEGK GTAQRATELL RDAGLGVTPV DSIATPIEDG QLLVTCGGLN
HGFVDEASRL AVITGNDISG GRGASTKDMR KMPARRRNTI DPLELKTGDF VVHEQHGIGR
YIELVQRTVN GADREYLVIE YAASKRGQPG DRLYVPTDQL DQLSRYVGGE SPSLHKMGGS
DWQKSKARAK KAVKEIAAQL IQLYAARQAS QGHSFGPDTP WQQELEDAFP YTETPDQMAA
IIEVKHDMEL QVPMDRLICG DVGYGKTEIA VRAAFKAVQD GKQVAVLVPT TLLAQQHFNT
FTERMSQFPV QIKQLSRFQT PKEAALTLEL AAEGTADIVI GTHRLLAKST RFKNLGLIIV
DEEQRFGVEH KEQLKALRAS VDVLTMSATP IPRTLEMAIT GIREMSTIAT PPEERHPVLT
YVGAQDDKQV AASIHRELLR DGQVFYLHNR VESIDRAARK LRELVPEARV AVAHGQMSEE
QLEKVMVGFW EKEFDVLVCT TIVESGIDIP NANTLIVERA DLLGLAQLHQ IRGRVGRGRE
RAYAYFLYPR EKPLTEHAHE RLATIAQHTE LGAGMYVAMK DLEIRGAGNL LGGEQSGHIE
GVGFDLYVRM VGEAVAQFKG ERPEEEPEVK IDLPIDAHLP TEYIAVERLR LEMYRKLAEA
RDDARLTEVV AEMTDRYGEP PAQVANLIAV ARFRQVARAY GLTDVTMQGK HIRFSPLPLP
DSKQMRLKRY HPDSVYKTVN DQVSVPRPST RRVGGEPLRD QALLEWCAQL LKDVLGDVPA
PAGATR
//
