ID A0A0L6UI26_9BASI Unreviewed; 1881 AA.
AC A0A0L6UI26;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=VP01_585g2 {ECO:0000313|EMBL:KNZ48173.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ48173.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ48173.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ48173.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-2015) 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:KNZ48173.1}.
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DR EMBL; LAVV01011118; KNZ48173.1; -; Genomic_DNA.
DR STRING; 27349.A0A0L6UI26; -.
DR VEuPathDB; FungiDB:VP01_585g2; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000037035; 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; 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 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; 2.
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:UP000037035};
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 270..562
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 172..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1735..1783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1761..1782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1881 AA; 208422 MW; 25AE330F67391C84 CRC64;
MNSNQFVHSS APTRRVRTIQ FGIMSPDEIK GFSVAKIEHP ETYEEGGIHP RVGGLSDPRM
GTIDRNMKCQ TCGEDVSSSD HQLDRCRRVP VTSPTSNLLV PSIMSVSDEE YVLLRFLNRV
KKILECVCIQ CAKLKADVAT DSALELIARR IKDPKKRFNA VHQLCRGKNI CEADPGDEKP
ENPDDQVVDD QTPKGHGGCG HAQPQIRKEG LKMFLQYSKR KGEEDEDGVG SLAGTERKPL
PASEAQAILR RISDEDLHIL GLHTDEARPE WMILTVLPIP PPPVRPSIAM DGGATRGEDD
LTYKLAEVIK ANQAVRKFES EGAPAHVITE FETLLQWHIA TYMDNDLPGQ PQALQKSGRP
IKSLRARLKG KEGRLRGNLM GKRVDFSART VITGDPNLQL DQVGVPYSIA RNLTYPERVT
PYNISYLQEL VQNGPTEYPG ARYVVRDTGD RIDLRYNKRA DTFLQYGWIV ERHLKDGDYV
LFNRQPSLHK MSMMSHRIKL MPYSTFRLNL SVTSKQYPTL GKETRAELAQ IAWVPRNIVS
PQANKPVMGI VQDTLCGVRK FTLRDCFMDR DFIQNILLWV PGWDGVVPPP AILKPKPLWT
GKQILSMCIP KGINLLRDDE NQTSIPIADK GLWIEDGEII YGVVDKKCVG ASQGGLIHVI
FREKGPQVTR GLFSGIQMVV NYWLLHHGFS IGIGDTVPDK ATMEAITNFI SEAKREVSET
IALAQEDKLQ AEPGMTIRES FEAKVNRALN TARDNAGRSA EQSLKDDNNV KQMVTAGSKG
SFINISQMSA CVGQQSVEGK RIPYGFKYRT LPHFTKDDYS PESRGFVENS YLRGLTPQEF
FFHAMAGREG LIDTAVKTAE TGYIQRRLLK ALEDVMVTYD GTVRNSLGDI VQFVYGEDGV
DGGTVEYQNL DSVRLSNEKF DKKFRVDVTD PKSDYKPGVL QVGLNGSSLS LQSILDAEWK
QLCEDRETLR KFIFTDGNGR KPLPVNIRRI IQNAQQIFHI DFRKPSDLPP QEIIQMVNDL
CDRIIVVRGD DALSRAAQEN CTLLFRILLR SNFATRRVLE EFHLNREAFE WVLGEIEARF
NQSLAAPGEM CGTLAAQSIG EPATQMTLNT FHYAGVSSKN VTLGVPRLKE IINVATNIKT
PSLTVYLNEN IANDIEAAKD IQTELAHTTL KTVTASTQII YDPNPKSTVV EEDLDFVDAF
FAVPDDEVES QLDHQSPWLL RLELDRAKML DKKLSMSFVA SKIAEVFKSD LFIIWSEDNA
EKLIIRCRAM QSSEADKDDD EGQVEEDVFL REINQMLGSI SLRGVEGIQR VFMLQHNVNY
INHTGEFERK TEWVLETDGV NLKEVLCVDG VDPVRTVSNN CVEILTVLGV EAARASLLKE
LRNVIEFDGS YVNYRHLALL CDLMTNRGAL MAITRHGINR TDTGPLMRCS FEETVEILMD
AAALGEKDHC TGVAENVLLG QLAPMGTGAF DVALDLDMLK DVVIDHRLPV AGEIMGGRFA
DGAMTPGGGM TPYAEFGDTR TPAGRFEDGP VPHAMFSPII TAGADDGFGG SNDIYGGYGG
QSPYGAGGGT SPGYSPSSPS YNPAASPAYT PTSPTWSGAS PWVASGTSPG YSPTSPRMGA
TSPRFSSASP PLSFVLVLPA SPNFVSFLLL LCFYPLCGRL HRPTLWSPAS PAFVRLLILL
FTPRQLLLHS RLPRPGFHQV VQTIRGSLVL ACLWRYLAEM IFIFSSPAGL ATSPRYSPTS
PAMSPSSPKY SPASPAFSPA SPKYSPATQR WSPQSPAFSP ASPKYSVSIG LFRQISQKDN
PCITGLQSNK STSELRVFWI IHPPLLKLRH NHPNGPRLIR TGPMDRLISL NNSSSNQTQA
PILMELILPT VLLLLGLVNS M
//
