ID W9Y3I6_9EURO Unreviewed; 1761 AA.
AC W9Y3I6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=A1O3_04306 {ECO:0000313|EMBL:EXJ87347.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ87347.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ87347.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ87347.1,
RC ECO:0000313|Proteomes:UP000019478};
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 Capronia epimyces CBS 606.96.";
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:EXJ87347.1}.
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DR EMBL; AMGY01000003; EXJ87347.1; -; Genomic_DNA.
DR RefSeq; XP_007732626.1; XM_007734436.1.
DR STRING; 1182542.W9Y3I6; -.
DR GeneID; 19168426; -.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_000487_3_0_1; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000019478; 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; 13.
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; 4.
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:UP000019478};
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 1527..1761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1560..1659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1672..1707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1761 AA; 193846 MW; 8B6A25743468BB4C CRC64;
MSNLNFPYSS APLRTVEEIQ FGLFSAKETE RLAVIEIEYP ETMDEQRLRP REKGPNDPHL
GTIDRNFRCS TCEENMAECP GHFGVIKLAT PVYHYGFMSK VKKILETVCH NCGKIKALDS
EEFRRAISLR DRKRRFDAVW RLSKPRNICE ADPPEDPDQP LKGPPQPKHG GCGNAQPDIR
RTGLQLWATW KAGKGDDDED TAPDKKRIFP QDALNTFRTL TDETLEMMGL SLDYARPEWM
ILSALPVPPP PVRPSISVDG SGQGSRGEDD LTFKLGDIIR ANQAVLRTEV DGTPDHIKVD
LCDLLQYHIA TYMDNEIAGL ERAQHKSGRP IKSIRARLKG KEGRLRQNLM GKRVDFSART
VITGDPNLSL DEVGVPRSIA RNLTYPETVT PFNLDKLKRL VANGPTEHPG ARYVIRDTGE
RIDLRHHKRA GEMTLQYGWK VERHIQDGDV ILFNRQPSLH KESMMAHRVR VMPYSTFRLN
LSVTTPYNAD FDGDEMNLHV PQSEESRAEL ANLCMVPLNI VSPQRNGPLM GIVQDTLCGI
YKVCRRDVFL TREQVMNIML WVPDWDGVIP QPAIIKPRPR WTGKQMISMI LPNALNLERL
DAKGEDPYVP ANDTGLMVLE GNLMFGLFSK KFVGTSAGGI IHTIFNEFGH DAAMAFFNGA
QHVVNYWLLH NGFSIGIGDT VPDPETVQKI QEVVDAKKAE VEELTIRAYK EDLEPSPGMN
VRQTFESKVM NALNQARDQA GAVTENSLKD LNNGITMARA GSKGSTINIA QMTAIVGQQA
VEGKRIPFGF KYRTLPHFAK DDYSAPSRGF VENSYLRGLT PSEFFFHAMA GREGLIDTAV
KTAETGYIQR RLVKALEEVT VKYDSTVRDS RGNIVQFIYG EDGLDGAHIE NQKVDIITMS
DKAFHNRYAV DIMSGDVSGW RGKLLQAREI QGDTELQELF DEELEALRES REFLRKMGKG
TEDSMQLPLN IARIIDQAQK NFKIRRGDKT DLDPRHALTS VKQLLDRLVV VRGDDPISQE
AQSNATLLLK AQLRSRLAYK RLVLEHGLNR LAFDNVIGAV ESRFIAAQAN PGEMVGVLAA
QSIGEPATQM TLNTFHFTGV SAKNVTLGVP RLKEILNVSQ TIRTPSMTVY QLPENAGDKE
AAKLLRSRVQ HTNLRSVAET CELWYDPDIQ STIIPEDLDM VESYFIIPED NEADLSLHSK
WLLRVILSRA KLLDKGLNIQ EVAAKIKSTY GKDLSVIFSD INADEQVIRV RLVQGYGKDE
DEDRKEDDEI LRRFMNEMLD HLTFHGVPGV SRAFIDHKSR AIIDDDNSVY MAKSDPRCNE
YVLETSGSAF AKVLAIEGVD TARTYTNRFT EIFEVLGIEA TRAAILRELT QVLSFDGSYV
NARHLGILCD VMTARGYVMA VTRHGINKSD TGALMRCSFE QTVEILLEAA AAGELDDCRG
VSENLILGQV APVGTGAMEI LLDENMLSQV VTDNANLGLG GAIGVKGSQQ LIEGAATPYD
TGSPMHDSGY LGSPDYGASF SPIAASGSET PGGFTEYQPG FGGAGGFSPY GPRSPGGYSP
ASPLGTSPSS PGFSPTAGYS PTSPMFGRTS PGFGPTSPSF SPASPAFTPT SPAYSPTSPG
YQASPTSPSY SPTSPNYSPT SPAYGSPTSP SYSPTSPAFS PTSPTSPTSP VYSPTSPMYS
PTSPMYGTTG NKQSPTSPSY SPTSPTYSPT SPTSPTSPSY SPTSPMYNAS PRSPQARSAS
VTSPQYSPNS PQYSPTSPKE D
//
