ID S3CZ06_GLAL2 Unreviewed; 1727 AA.
AC S3CZ06;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-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=GLAREA_03767 {ECO:0000313|EMBL:EPE30800.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE30800.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE30800.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(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; KE145363; EPE30800.1; -; Genomic_DNA.
DR RefSeq; XP_008082211.1; XM_008084020.1.
DR STRING; 1116229.S3CZ06; -.
DR GeneID; 19462822; -.
DR KEGG; glz:GLAREA_03767; -.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_000487_1_1_1; -.
DR OMA; MVQYDRT; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000016922; 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; 11.
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; 5.
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:UP000016922};
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 240..546
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1509..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1727 AA; 189904 MW; 5ABA938B61B0ABA3 CRC64;
MANLNFTHSD APLKTIQEIQ FGLLSPEEIK NMSVVHILYP ETMDESRMKP RDQGLNDPRL
GSIDRQFKCG TCDQQMSECP GHFGHIELAK PVFHPGFIKK IKKILEMVCH NCGKILLDRS
NPAYKAAVSI RDPKRRFDTI WRLCKPKMIC DSDVSNEEGN SEGKEQAVSI HGGCGNLQPE
VRQQSLTLTG TWKVPKDEDG ETAQPEKRNI TPEMALAVFK SISSSEIRDL GLSNDYARPE
WMIITVLPVP PPPVRPSVSM DGTGQGMRGE DDLTFKLGDI IRANGNVRQA QQEGSPAHIL
SDFEALLQYH VATYMDNDIA GTPQALQKSG RPVKSIRARL KGKEGRLRGN LMGKRVDFSA
RTVITGDPNL SLDEVGVPRS IARTLTYPET VTPYNINHLS KLVRNGPNDH PGAKYVMRAD
GTRIDLRHNK NSAGVNLEYG WKVERHIVDG DFIIFNRQPS LHKESMMGHR VRVMPYSTFR
LNLSVTSPYN ADFDGDEMNL HVPQTEETRA EVMNLCMVPL NIVSPQRNGP LMGIVQDTLA
GVYKMCRRDV FITKEHLMNI LLWVPEWDGV IPQPAILKPR PRWTGKQIVS MIIPKIVNLH
TANDAREDAP LKDDGLLVHE GELMFGLLTK KNVGASSGGI IHIIFNEQGP DAAMAFFNGC
QRVVNYWLLH NGFSIGIGDT IPDKSTIEKI EGAIQVQKDE VAELTAKATA NELESLPGMN
VRETFESLVS KALNTARDKA GTKTEDSLKD SNNAVQMARS GSKGSTINIS QMTALVGQQS
VEGKRIPFGF KYRTLPHFTK DDYSPESRGF VENSYLRGLT PTEFFFHAMA GREGLIDTAV
KTAETGYIQR RLVKALEDVM AKYDGTVRNS LGDIVQFVYG EDGLDGTIIE KQRVDHINLS
DKAFEDRFRL DVMDDRNPAI SSEVLSDAAD VSGDIEVQKL LDLEWEQLVA DRDMLRDVNF
KKKDDEQMQL PLNVIRIIDS AKRLFKIDIT KRSDLTPQVV IPLVQGLLDR LVVVRGKDEL
SEEAQLNATL LIKAQLRSRL AFKRIACHMR LNRLAFDHVL GEIETRFIKS LVNPGEMVGV
LAAQSIGEPA TQMTLNTFHF AGVSSKNVTL GVPRLKEILN IASNIKTPSM VVYQEGEDAS
QDSAKLLRSA VEHTNLRSVM QATEIYHDPE IQSTEIADDL DMVESFFIIP EEHHDSLDNQ
SRWLLRLILD RQKMLDKGLR VEDVAIKIKE NYPKDLAVIF SDNNAEKQVI RIRMIKAGDG
KYDDDDIEED IMLKRLEAHI LDTLTLRGVP GVDRAFLNKE TKLITTPDGG LLASKSDDRC
TEWYLDTSGT SLAQVLTVPG VDTTRTYTNH FIQVLEVFGI EAARSALMRE LTQVLAFDGS
YVNHRHLALL VDVMTSRGLL MAITRHGINR ADTGALMRCS FEETVEILLE AAAIGELDDC
RGISENVMLG QLAPMGTGEL EVLLDPVMLD TVISDNGRMN LVPGLQAKGA DGAATPYDNG
SPMNEAGYMG SSPDYTGGGF SPVQSANPDE NRGFATEYGG YGSGIGTPNP RSPGGGWSPV
SPNTFGTPTS PGYSPVSPGY SPTSPGMTSP GFSPSSPAFT PTSPAYSPTS PSFVSPTSPS
YSPTSPNYSP TSPAFHGQSP SSPNYSPTSP SYSPTSPSYS PTSPNFTANK TSPGSGLSPT
SPVYSPTSPS FSPTSPAYAA AQANATSPKY SPTSPSYSPT SPQFSPT
//
