ID S8AIQ1_PENO1 Unreviewed; 1734 AA.
AC S8AIQ1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=PDE_00582 {ECO:0000313|EMBL:EPS25648.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS25648.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS25648.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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}.
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DR EMBL; KB644408; EPS25648.1; -; Genomic_DNA.
DR STRING; 933388.S8AIQ1; -.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_000487_3_0_1; -.
DR OrthoDB; 169836at2759; -.
DR PhylomeDB; S8AIQ1; -.
DR Proteomes; UP000019376; 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 Pfam; PF05001; RNA_pol_Rpb1_R; 8.
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; 3.
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:UP000019376};
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 243..548
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1503..1734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1559..1662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1734 AA; 191651 MW; 9953DAD9A9ECD56C CRC64;
MSNVHFPYSK APLRTIKEIQ FGLFSPEEVK RMSVVHIEYP ETLDETRMRP RTKGVNDSRL
GTIDRQYNCE TCEEGPKECP GHFGHIELAS PVFHIGFVTK IKKLLETVCH NCGKIKVGAD
NAKFLEAIRI RDPKRRFDAI WRASKDINIC ETDPSPDEEE EALKDGKKRY FHGGCGNAQP
TVRKEGISLV GTWKPSKSMM EDDATAQPEK KVITPAMALN IFRNISHEDV RIMGLSNDYA
RPEWMILTVL PVPPPTVRPS VVMGSSSGSR GEDDLTYKLA EIVRANQSVQ RCEQEGAPEH
VTREFESLLQ YHIATYMDND IAGQPKAMQK GNRPVKALRS RLKGKEGRLR QNLMGKRVDF
SARTVITGDP NLSLDEVGVP YSTAKILTYP EVVTPYNIEK LQKLVSNGPL IHPGARYIVR
DTGERIDLRH AKRAGTQQLL YGWKVERHLD NGDVILFNRQ PSLHKESMMG HRVRVMPFST
FRLNLSVTTP YNADFDGDEM NLHVPQSEES RAELAELALV PKNIVSPQRN GPLMGIVQDT
LCGIYKICRR DIFLAKEHVM NIMLWVPNWD GVIPPPAIMK PRPRWTGKQI ISMAFPTGLN
LVRVDKDSAP ASEKFSPLND GGLLIQGGQL MYGMLSKKTV GASGGGVIHT IFNEYGADTC
VGFFNGAQTI VNYWLLHHGF SIGIGDTIPD RKTIEKIEEA VRERKQEVQE ITASATDNTL
EALPGMNVRE TFESKVSRAL NNARDEAGSA TERGLKDLNN AIQMARSGSK GSTINISQMT
AVVGQQSVEG KRIPFGFAYR TLPHFTKDDY SPESRGFVEN SYLRGLTATE FFFHAMAGRE
GLIDTAVKTA ETGYIQRKLV KALEEVMVKY DGTVRNSLGD IIQFIYGEDG LDGVHIENQP
VDIIRCSDEK MRQRFRVDVM DPEMSLGPEV LEQANEIAGD IEVQRYFDEE WEALLESRAF
LRTVAKEDEE MMQLPINVRR ILEMARSTFR IREGTISDLH PAEVIPQVQA LLDRLVVVRG
DDPISQEADY NSTLLFKAQL RSRLAFKRLV TEYSLNKLAF QHVLGAIENR FARAAANPGE
MVGVLAAQSI GEPATQMTLN TFHFAGVSSK NVTLGVPRLK EILNVATNIK TPSMTVYQEG
DNTYRKEGAK QLRSLVEHTS LRSVTEATEI YYDPDIQSTV IENDRDMVES YFIIPEEVEG
DLANQSKWLL RIILSRPKLL DKGLTVQDVA NRIKKAYKDD IAVIFSDNNA DEQVIRIRQV
QHHKEEEDDD DVEYDVTLKK LEQHLLDTLT LRGVPGVERA FINERGKVRV TEDGALLMSK
TDPLCKDWVL ETSGSSLAPV LAIPGVDATR TYSNQFIEIF EVFGIEAART AVLRELTQVL
AFDGSYVNHR HLALLVDVMT QRGYLTPVTR HGINRADNGA LMRCSFEETV EILLEAAAFG
ELDDCRGVSE NLILGQMAPA GTGEFDVYLD QNLLNTVVSN NARFALMGGV GAKDAIISDG
AATQYDSGSP MPSSPYLDDS DPESRFSPIA QGGAESPRGF PKYQPADGFG GLSPLGRSPG
QAYSPTSPFN TSAASPMWSP SSTAYSPTSP GISSPGFTSP RMSPTSPSSP QFVITSPAYS
PSSPAGASPS YSPTSPTYSP SSPNFSPASP AFSLTSPEYS PTSPALGGGR HFSPTSPASP
TSPKWSPTSP SWSSAQPEAY SPTSPKFSGS PTSPAAAYSP SSPEFHSPTS PRQK
//
