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Database: UniProt
Entry: A0A090M528_OSTTA
LinkDB: A0A090M528_OSTTA
Original site: A0A090M528_OSTTA 
ID   A0A090M528_OSTTA        Unreviewed;      1662 AA.
AC   A0A090M528;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   ORFNames=OT_ostta10g01360 {ECO:0000313|EMBL:CEF99340.1};
OS   Ostreococcus tauri.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=70448 {ECO:0000313|EMBL:CEF99340.1, ECO:0000313|Proteomes:UP000009170};
RN   [1] {ECO:0000313|Proteomes:UP000009170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX   PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA   Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA   Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA   Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA   Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA   Van de Peer Y., Moreau H.;
RT   "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT   unveils many unique features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC       subfamily. {ECO:0000256|ARBA:ARBA00007207}.
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:CEF99340.1}.
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DR   EMBL; CAID01000010; CEF99340.1; -; Genomic_DNA.
DR   STRING; 70448.A0A090M528; -.
DR   InParanoid; A0A090M528; -.
DR   OrthoDB; 7998at2759; -.
DR   Proteomes; UP000009170; Chromosome 10.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd02584; RNAP_II_Rpb1_C; 1.
DR   CDD; cd02733; RNAP_II_RPB1_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; 3.30.1360.140; -; 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; 2.
DR   Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR000684; RNA_pol_II_repeat_euk.
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; IPR007075; RNA_pol_Rpb1_6.
DR   InterPro; IPR007073; RNA_pol_Rpb1_7.
DR   InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
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:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 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   Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR   Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR   Pfam; PF05001; RNA_pol_Rpb1_R; 19.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SMART; SM00663; RPOLA_N; 1.
DR   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR   PROSITE; PS00115; RNA_POL_II_REPEAT; 11.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|RuleBase:RU004279};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009170};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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          219..525
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1531..1662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1531..1648
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1662 AA;  184590 MW;  0BD02DEE4E970169 CRC64;
     MSVHDRFPHS TAELCRVDAV QFGVLSPDEI RKMSVCAIES SDTYEKGRPK RGGLSDPRMG
     TMDRGAVCET DGCDSVQTPG YFGHLELAKP VYHHGFINVV LRVLRCVGYS SSQLLLHKDE
     DPKFAQLMRI KNPKNRLKKL TDACKTKSVC PYTGTAQPQY RLEGMKITAE FKHRDDELLP
     EGGERKVVVT AERALQILKG ISDEDCRVLG LDPEHARPDW MILQVMPVPP PPVRPSVSFD
     ASTRSEDDLT VKLMEIVRTN KNLERQEQNG APQHVILEFT ELLQYHIMTF MDNTVAGMPR
     ALTRSGRSIK SISERLKGKA GRIRGNLMGK RVDFSARTVI TPDPNLMLDE LGVPWSIALN
     MTYPETVTPY NIERLQRLVD NGPHPPPGET GARYIIREDG QRLDLRFLKK ASEKRLEYGY
     KVERHMVNGD VVLFNRQPSL HKMSIMGHRV RIMPYSTFRL NLSVTPPYNA DFDGDEMNMH
     LPQSYETKAE VKELMMVPKM IVSPQANKPV MAIVQDTLLG CRLITKRDTF IPKDVFMNII
     MWLEDWDGKI PKPAILKPQP LWTGKQVFSM MLPKVNLLRT SAWARDADDV TFSVDDTGVR
     IEQGELLTGT LCKKTMGSGG GGLIHVTWEE WGPIAARGLI SQTQTLVNYW LLHHGFTVGI
     ADTIADDETM FTINNTITKA KADVKEVIKQ AQNNELELQP GMTMQQSFEQ KVNQILNKAR
     DNAGNSAQNS LKDTNNVKMM VTAGSKGSFL NISQMIACVG QQNVEGKRIP YGFKGRTLPH
     FSKDDFGPES RGFVENSYLR GLTPQEFFFH AMGGREGLID TAVKTSETGY IQRRLVKAME
     DVVVKYDGTV RNSVGDVIQF LYGEDGMDAT MIESQVLDTL RLGAKEFAAV FQIDPDVSGF
     NKGWLSNEQA SDLAHSTKVR EIIDAEWERL QKDRVELRKV FPTGDPHVHL PVNMKRIIWN
     AQKQYGMYRP GGSEEELSVT HVIESVAELL PKLIVVAGTD PLSIEAQRNG TLLFFAHVRA
     NLAAKRVLKD HKLTRAGFDW VIGEVESRFK MALAPPGDGI GVVAAQSIGE PATQMTLNTF
     HFAGVSAKNV TLGVPRLKEI INIAKQIKTP SLTVALKPEF ASDRTKAKDV QASLEYTTLH
     SVAAVTEVHY DPDPTDTVIE EDREFVRAYY EMPDEDVDPS RMSPWLLRIE LNREMMVDKK
     LLMADVAERI NEDFGGDLSC IFNDDNSEKL VLRIRIMKAE GEKYDDSSIE DEVFLKRIET
     QMLSNLALRG IPDIKKVFIR EAKSNAVNPR TQLFEKHTEW MLDTEGVNLL EVMAHPDVDF
     TRTTSNHLIE VIQILGIEAV RNTLLRELRG VIEFDGSYVN YRHLAILVEV MTYRGHLVSI
     TRHGINRAET GALMRCSFEE TVDILMEAAA FSERDNMTGP SENIMLGQFC PIGTGEFKLH
     LDQEMLLDAV ELDLFETART PGHYGSMTPG REGTPGYGAK SPSFLLSPGG AMMSPFDTSM
     AFSPYSDGGM AFSPGGMSPG GGVGYSPTSP AYSPTSPAYS PTSPAYSPTS PAYSPTSPAY
     SPTSPAYSPT SPAYSPTSPA YSPTSPAYSP TSPAYSPTSP AYSPTSPAYS PTSPAYSPTS
     PAYSPTSPAY SPTSPAYSPT SPAYSPTSPA YSPKEEDGEE EE
//
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