ID A0A024GHH0_9STRA Unreviewed; 1850 AA.
AC A0A024GHH0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=BN9_068360 {ECO:0000313|EMBL:CCI45926.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI45926.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI45926.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI45926.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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:CCI45926.1}.
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; CAIX01000111; CCI45926.1; -; Genomic_DNA.
DR STRING; 65357.A0A024GHH0; -.
DR InParanoid; A0A024GHH0; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000053237; Unassembled WGS sequence.
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; 1.
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; 17.
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; 18.
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 Reference proteome {ECO:0000313|Proteomes:UP000053237};
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 269..572
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1537..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1594..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1619..1850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1850 AA; 203971 MW; 076DA5E9A6CCFC71 CRC64;
MSSTQFSYSS ARLRRVKYLQ FGVFSPEEVR AMSVTKQTKV NDRIIPDGIS RPETYLNGHP
VIGGIGDPRM GTCDFRARCK TCDCTYSGSG GKVNDCPGHF GHIELARPMY HLGFIKEVLK
ILRSVCFHCS KILSDERDHR FRSAMKIKDG KRRLKAVFEI CNGKKLCEYG EEVDMEKMRE
DLNLGLQGGL DDKTKSKEGG HGGCGGLQPI YKRQGIKILV EFPEQMEDVP GSGDRKQNLP
AAKVLSIFKN ISDADCYSLG LDPRWARPDW LILTLMPVPP PHVRPSVALD GMARGEDDLT
HNLASIVKAN LALLNCVRKG EPSHIIEQFE QLLQFHLATF INNEQPGLPQ AQQRSGKPLK
TLRQRLRGKE GRIRGNLMGK RVDFSARTVI TADPNLEIDQ VGVPLSIAMN LTVPERVTPF
NMAAMHRLIS NGPLEHPGAK YIIREDGNRI DLRYIKNKSD LALKCGWIVE RHLRDEDLVL
FNRQPSLHKM SIMSHRVKVF HWSTFRLNLS VTSPYNADFD GDEMNLHVPQ SLTARAEAQE
LMMVHKVIIT PQSNRPVMGI VQDSLLGVQK FTKRDIFIEK DVVMNLLMWV FNWDGRIPTP
AILVPKKGEI GKYRPIWTGK QIFSQVIPQI NFTGFSSTHS SKESFAKLSP IDSRVIVQRG
ELLAGIIDKK TIGSSAGGLI HTTMLEKGPE EARYFLGAVQ KLVNNWLVGR SFTVGVSDTI
ADVSTLKTIV DIITQAKVQV HDLVQRGQKG KLETQPGRTM VESFEQLVNK VLNTARDQAG
REAQGSLDET NNIKATVTSG SKGSFINISQ IIACVGQQNV EGKRIPYGFQ HRTLPHYGKD
DLGPESRGFV ENSYLKGLTP QEFFFHAMGG REGLIDTAVK TAETGYIQRR LVKAMESVMA
RYDGTVRNAQ GEIIQFLYGE DGMDAVWVEK QRFESHRLNK VEFEQKYMFD ISSDFLGCVP
KCPEQLFLDP EIIKDIRTNQ HTQHILRDEI AQLQKDRVNL RVILASRGQG QESDNAAQIP
VNVRRLIENA QQLFSVDLQK PSSLHPAHII DGVKELCKKI IVVQGNDPLS LEAQENATLF
FQILLRSALA SKCVTLEHRL TETAFEWLLG EIESKFTSSL VSAGEMAGVV AAQSIGEPAT
QMTLNTFHYA GVSAKNVTLG VPRLKEIMNI AKDVRTPSLQ IFLTPDCAHD ADKAKFIQSQ
LEYTTLADVT ANTAIYYDPD PMNTIIEEDQ EFVSTYYEMP DEDTPVARSP WLLRIELNRE
MMADKKLTMS EIASQIESEY GQDLSCIFTD DNADKLVLRI RIVSDEEEKM QRTGESTVGQ
EDDTFLKRVE HNMLTQMKLR GVQSVKKVYI REGRPTHWFD DVGFKMTTEW VLDTDGTNLL
DVLCFPQVDG TRTISNDIVE IIQVLGIEAV RRALLNEIRQ VISFDGAYVN YRHLACLADV
MTFRGHLMAI TRHGINRDDS GPLVRCSFEE TVEILMDAAM FSEGDPLTGV SENVMLGQLA
PLGTGITDLV LDAKKLTDAI EYEASEIQQV MRGINDEWRS PEQGPGTPMA TPFTSTPGFS
ASSPFSPGGG SFSPSAGTFS PMTSPTSPGF MSSPGFSVAS PARSPGASLD PASPAFSPMS
PAYSPTSPAY SPTSPAYSPT SPAYSPTSPA YSPTSPAYSP TSPAYSPTSP AYSPTSPAYS
PTSPAYSPTS PAYSPTSPAY SPTSPAYSPT SPAYSPTSPA YSPTSPAYSP TSPAYSPTSP
AYSPTSPAYS PTSPAYSPTS PAYSPTSPAY SPTSPAYSPT SPAYSPTSPA YSPTSPGYNP
SIPAYSPTSP AYSPTSPSYS PSSPQYNPTE GYDPNSSGYS PTDGREKAEE
//
