ID F6HL45_VITVI Unreviewed; 1691 AA.
AC F6HL45;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN OrderedLocusNames=VIT_08s0007g08090 {ECO:0000313|EMBL:CCB55152.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB55152.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|RuleBase:RU004279}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000256|ARBA:ARBA00024550,
CC ECO:0000256|RuleBase:RU004279};
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|RuleBase:RU004279}.
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DR EMBL; FN595991; CCB55152.1; -; Genomic_DNA.
DR RefSeq; XP_010653802.1; XM_010655500.2.
DR STRING; 29760.F6HL45; -.
DR PaxDb; 29760-VIT_08s0007g08090-t01; -.
DR EnsemblPlants; Vitvi08g01871_t001; Vitvi08g01871_P001; Vitvi08g01871.
DR GeneID; 100250406; -.
DR Gramene; Vitvi08g01871_t001; Vitvi08g01871_P001; Vitvi08g01871.
DR KEGG; vvi:100250406; -.
DR eggNOG; KOG0262; Eukaryota.
DR HOGENOM; CLU_000487_2_2_1; -.
DR InParanoid; F6HL45; -.
DR OrthoDB; 7998at2759; -.
DR Proteomes; UP000009183; Chromosome 8.
DR ExpressionAtlas; F6HL45; baseline and differential.
DR GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IEA:GOC.
DR CDD; cd02735; RNAP_I_Rpa1_C; 1.
DR CDD; cd01435; RNAP_I_RPA1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.70.2850; -; 1.
DR Gene3D; 6.10.250.2940; -; 1.
DR Gene3D; 6.20.50.80; -; 1.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR InterPro; IPR047107; DNA-dir_RNA_pol1_lsu_C.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu_N.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF11; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA1; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 356..674
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 769..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1418..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1369
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1403
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1691 AA; 188516 MW; A620A8C6A754F49C CRC64;
MAHVIEGTTE FVEAVKFSFF TDEEVRKYSF KKITSPLMLD SVQRPVPGGL YDPALGSIDE
NTPCQSCGQR SFYCPGHCGH IDLVSSVYNP LLFNLLHNLL QKTCFFCHHF KTSSSLVQKY
VSQLELISKG DVVGAKNLDS ISPSESSYPE DSDGSHVSCS STVNSSARDN CSVHLKQQEW
TSLQCIEAMS VMDNFLKLKH RDCKNCKAKS PQVTKPTFGW FHMAGLSDAQ TRANVIRGSK
LERPLSRVAE EKSSSEVENV NDMFPWGDGV DTDETHSSIA PTDGIQDTVT KRLERKGAQA
PIEFIKQKSF FSGPLLPSEV RDIMERLWEN EAELCSFISD ILQERLGASG NKAGYSMFFL
ETILVPPIKF RPPSKGQISV MEHPQTVLLG KVLQANIALG NAHANNSERS KIISRWMDLQ
QSINVLFDGK TAAGQGQRDT GSGICQLLEK KEGVFRQKMM GKRVNFACRS VISPDPYLAV
NEIGIPPYFA LRLTYPEKVT PWNVVKLRDA IINGPEIHPG ATHYVDKLST VKLAVNKKMR
ISISRKLPSS RGVVAQPGRS SDNEFEGKIV YRHLQDGDIV LVNRQPTLHK PSIMAHVVRV
LKGEKTLRMH YANCSTYNAD FDGDEMNVHF PQDEISRAEA YNIVNANNQY IVPSRGDPIR
GLIQDHIVSA VLLTKKDTFL TREQYNQLLY SSGLSSGSGS FIGKPGKKVS VLDSEDEMQP
LLPAIWKPEP LWSGKQVITA VLNHITRGRK PFTTEKDGKI PREYFGSEID EKKSGKGKDP
GSDRRKEKRI EKKHGEYKLL IHKNELVRGV IDKAQFDKYG LVHMVQELYG SNTAGILLSV
LSRLFTVFLQ MHGFTCGVDD LLISPNYDIA RKIELDKSEN IGELVHCKFI GSNHGKIDPV
KLQVEVEKII LSNGEAAITR LDRMMKNELN ELTSKVNKDL LLKGLVKPFP KNCLSLMTTT
GAKGSTVNFS QISSFLGQQD LEGKRVPRMV SGKTLPCFPP WDCAARAGGF ISDRFLTGLH
PQEYYFHCMA GREGLVDTAV KTSRSGYLQR CLIKNLECLK VCYDYTVRDS DGSIVQFNYG
DDGVDVHQTS FITEFEALAV NEEVVCEKFG QDGKFNGYIQ KLPKELRKKT KKFIEGFMEE
RQDFDNMKKQ KDFVNLVKQK YISSLAQPGE PVGVLAAQSV GEPSTQMTLN TFHLAGRGEV
NVTLGIPRLQ EILMTAANDI KTPIMTCPLQ MGRSKDDAER LAAKLKKVTV ADITESMEVS
IVPFTVQDHQ TCSIYKLKMK LYEPALYPPH TGISLEDCEE TLEAVFVREL EDAIQNHLLL
LSKISGIKNF LPDSRSMASK ETDEDASGDG LAGGNGDEDD DGEDDGGAED LGLDAQKRKQ
QASDEMDYGD SEGEPDEGEP SAGLTEEIDL VEDEVEISNN EEVGISDPKD EDSKVPSKSK
SSKNKKAKTE AKRKKRFRAI KKDFDRAILV KAKGTYFEVH FRFTNEPHIL LAQIAQKAAN
KVYIRSSGKI DLCQVIDCNK DQVIYYGRDP KKRENIPGEE KKKLPALQTA GVDFTAFWKM
QDELDVRYVY SNNVHAMLNT FGVEAARATI IKEVFNVFNA YGVKVNIRHL SLIADFMTHS
GGYRPMNRHG GIAESVSPFS KMTFETASKF IVEAASHGMT DNLESASARI CLGLPVKMGT
GCFDLMQKIE I
//
