ID W9W0G9_9EURO Unreviewed; 1760 AA.
AC W9W0G9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-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=A1O7_02010 {ECO:0000313|EMBL:EXJ61582.1};
OS Cladophialophora yegresii CBS 114405.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182544 {ECO:0000313|EMBL:EXJ61582.1, ECO:0000313|Proteomes:UP000019473};
RN [1] {ECO:0000313|EMBL:EXJ61582.1, ECO:0000313|Proteomes:UP000019473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114405 {ECO:0000313|EMBL:EXJ61582.1,
RC ECO:0000313|Proteomes:UP000019473};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora yegresii CBS 114405.";
RL Submitted (MAR-2013) 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:EXJ61582.1}.
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DR EMBL; AMGW01000002; EXJ61582.1; -; Genomic_DNA.
DR RefSeq; XP_007754236.1; XM_007756046.1.
DR STRING; 1182544.W9W0G9; -.
DR GeneID; 19176621; -.
DR VEuPathDB; FungiDB:A1O7_02010; -.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_000487_3_0_1; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000019473; 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; 15.
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; 6.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000019473};
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 238..544
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 147..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1538..1760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 687..714
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1559..1658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1671..1706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1719..1760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1760 AA; 193457 MW; 4F0A0BE7683FD947 CRC64;
MTSLNFPHST APLRTVEEIQ FGLFSAKETE RLAVIDIEYP ETMDEQRLRP REKGPNDPHL
GTIDRNFKCS TCEENMNECP GHFGVIKLAT PVFHYGFMNK VKKILETVCH NCGKIKALDN
ADFQQAIATR DPKRRFEAVW RLSKPRNICE ADPPEDPDQP LKGPAPPKHG GCGNAQPDIR
RTGLHLYATW KPRKGDDDED TTPDKKRIFP QDVLNTFRTL TDETLQMMGI NLDYARPEWM
ILTALPVPPP PVRPSISVDG SGQGQRGEDD LTFKLGDIIR ANQAVLRTEV DGTPDHIKVD
LCDLLQYHIA TYMDNEIAGL DKAQHKSGRP IKSIRARLKG KEGRLRQNLM GKRVDFSART
VITGDPNLSL DEVGVPRSIA RTLTFPERVT QKNIDKLKRL VANGPNEHPG ARYVIRDSGE
RIDLRHHKNA SEMNLQHGWI VERHIQDGDV ILFNRQPSLH KESMMGHRVR VMPYSTFRLN
LSVTAPYNAD FDGDEMNLHV PQSQESRAEL ANLCMVPLNI VSPQRNAPLM GIIQDTLCGI
YKICRRDIFL TREQVMNIML WVPDWDGVIP QPAIIKPTPR WTGKQMISMV LPPALNLERL
DAKGEDPYVP TNDTGLIVLE GNLMFGVLSK KFVGTGAGGI IHTIYNEFGW ETALSFFNGA
QTVVNYWLLH NGFSIGIGDT VPDPDTVQKI QHAVDTKKAE VEDLQKKAEA EDLEPSPGMN
VRQTFESKAM NSLNQARDQA GAATEDSLKD LNNAITMARA GSKGSTINIA QMTAIVGQQA
VEGKRIPFGF KYRSLPHFTK DDYSAPSRGF VENSYLRGLT PTEFFFHAMA GREGLIDTAV
KTAETGYIQR RLVKALEEVT VKYDSTVRDS RGNIVQFIYG EDGLDGAHIE NQKVDIITMS
TKAFNDRYFV DIMSGDVSMW KGRLLQAREI QGDVELQEMF DLEFANLKEC QRLLRNMGKG
TEDSMQLPLN IGRIIDQAQK NFKIRRGDKT DLDPRYALTA VNQLLERLVI VRGDDPISKE
AQDNATLLLK AQLRSRLAYK RLVLEHGVNR LAFDNIIGAV ESRFTAANAA PGEMVGVLAA
QSIGEPATQM TLNTFHFTGV SAKNVTLGVP RLKEILNVSQ NIRTPSMSVY QLPENTGDKD
AAKLLRSQIQ HTNLRSVAET CELWYDPDIQ NTIIPEDVDM VDAYFILPED GEADLSLHSK
WMLRVILSRA KLLDKGLDIT QVAGKIKSTY GKDLAVIYSD RNADEQVVRI RLVQNYGKDE
EDDRKEDDEI LRRFLNEMLD HLTFHGVPGV ERAFIDQKSR SIIKPDGSVF MAKSDPECNE
YVLETTGSAF AKVLAVEGVD ATRTYTNRFT EVFEVLGIEA TRAAILRELT QVLSFDGSYV
NARHLGILCD VMTSRGYVMA VTRHGINKSD TGALMRSSFE QTVEILLEAA AAGELDDCKG
VSENIILGQH APVGTGTMEI LLDQAMLATL PASSGYGLGG PIGIKTSQQL LEGAATPYDS
GSPMQDNGYL GSPDYGASFS PIAAPGSETP GGFTDYQPGF GGAGGFSPYG PRSPGGYSPA
SPFGQTSPTS PGFSPTAGYS PTSPMFGATS PGFGPTSPSF SPASPAFTPT SPAYSPTSPG
YQSPTSPSYS PTSPNYSPTS PAYGSPTSPS YSPTSPAFSP TSPTSPTSPV YSPTSPMYSP
TSPMYGGGGN KQSPTSPSYS PTSPTYSPTS PSSPTSPSYS PTSPVYNASP RSPQARNQSP
TSPQYSPNSP QYSPTSPKED
//
