ID A0A0Q9MCQ8_9MICC Unreviewed; 1216 AA.
AC A0A0Q9MCQ8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=ASG92_04610 {ECO:0000313|EMBL:KRE59140.1};
OS Arthrobacter sp. Soil736.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736395 {ECO:0000313|EMBL:KRE59140.1, ECO:0000313|Proteomes:UP000051775};
RN [1] {ECO:0000313|Proteomes:UP000051775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil736 {ECO:0000313|Proteomes:UP000051775};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE59140.1, ECO:0000313|Proteomes:UP000051775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil736 {ECO:0000313|EMBL:KRE59140.1,
RC ECO:0000313|Proteomes:UP000051775};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRE59140.1}.
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; LMSB01000023; KRE59140.1; -; Genomic_DNA.
DR RefSeq; WP_056629347.1; NZ_LMSB01000023.1.
DR AlphaFoldDB; A0A0Q9MCQ8; -.
DR SMR; A0A0Q9MCQ8; -.
DR STRING; 1736395.ASG92_04610; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000051775; 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}.
FT DOMAIN 676..837
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 862..1012
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1216 AA; 132032 MW; 3E841D974D4F12B8 CRC64;
MSPTGPSLTG LRRVLAADKT FARVQAEAAR SFGVRSEDYQ ISAPAGLRAV LLAEMADGLA
QAPGGDAAPG VVLAVTATGR EAEDLTAALR AYLPADAVAE FPSWETLPHE RLSPRSDTVG
RRLSVLRRLA HPESTTAGPL RVVVAPVRAV VQPIVAGLGE LVPVTLKVGQ EAPFSSVVKS
LADAAYARVD MVTRRGEFAV RGGMLDVFPP TEDHPIRVDF FGDEVDQMRW FAVADQRSLT
APGLHHPTEL HAPPCREILI TPSVMSRAAT LKSQLPAAAD MLEKIAGGIA VEGMESLAPV
LVDAMVPFME QLPAGSISVV VEPEKVRTRA HDLAATNEEF LEAAWSTASD GGTAPLDLSS
QASAALHSAS FRSLTETRSA ALGHEVSWWS ITSLATDEEL TQDINVLNLH AREPRGYQGD
VAEMMDFIGS HVRDQWRIVV ATEGPGPAQR LAELFHDADI PCARVDSLDH EPQAGIIEVT
TAAVGRGFVL DGLKTGLLTE ADLLGRTSAG STKDMRRMPS KRRNAVDPLQ LLAGDHVVHE
QHGIGRFVEL IQRKVAGGGD GVREYLVLEY APSKRGAPGD RLFVPTDQLD QVTRYVGGDT
PVLSKMGGSD WASTKSKARK AVKEIAGELI RLYSARMASR GHAFGPDTPW QRELEEAFPY
VETPDQLTTI NEVKADMERE IPMDRLVSGD VGYGKTEIAV RAAFKAVQDG KQVAVLVPTT
LLAQQHYETF TERFSGFPLK VKPLSRFQAS KEAKETAEGV KNGTVDVVIG THRLLSKDFA
FKDLGLVIVD EEQRFGVEHK EALKKMRTNV DVLAMSATPI PRTLEMSLTG IRETSTLATP
PEERHPVLTY VGPYTDKQTS AAVRRELMRE GQVFFVHNRV ATIERTAAKI RELVPEARVE
VAHGQMSESR LEQIIVDFWE KRFDVLVCTT IIETGLDISN ANTLIVDGAD KYGLSQLHQL
RGRVGRGRER AYAYFLYPSE KPLGEVALER LKAVATHNEL GAGMQLAMKD LEIRGAGNLL
GGEQSGHIQG VGFDLYIRLV GEAVADYRGE AEEKPAEMKI ELPVNAHLPH DYVPGERLRL
EAYRKLAAAI THEAIDEVLA ELVDRYGEPP LPAQNLVAVA RFRVGAREAG LSDVALQGNF
IKFSPAQLPE SKTMRLNRMY PGAQSKPALD AVLIPKPKTA KIGGRDLQDA EILEWANGVI
RNIFSDAPLA APAVGG
//
