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Database: UniProt
Entry: S3CKS6_GLAL2
LinkDB: S3CKS6_GLAL2
Original site: S3CKS6_GLAL2 
ID   S3CKS6_GLAL2            Unreviewed;      1693 AA.
AC   S3CKS6;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
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_01696 {ECO:0000313|EMBL:EPE25784.1};
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:EPE25784.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE25784.1, 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   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000256|RuleBase:RU004279}.
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DR   EMBL; KE145371; EPE25784.1; -; Genomic_DNA.
DR   RefSeq; XP_008087103.1; XM_008088912.1.
DR   STRING; 1116229.S3CKS6; -.
DR   GeneID; 19460754; -.
DR   KEGG; glz:GLAREA_01696; -.
DR   eggNOG; KOG0262; Eukaryota.
DR   HOGENOM; CLU_000487_2_3_1; -.
DR   OMA; NREDYQQ; -.
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-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd02735; RNAP_I_Rpa1_C; 1.
DR   CDD; cd01435; RNAP_I_RPA1_N; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 1.
DR   Gene3D; 1.10.357.120; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.70.2850; -; 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; IPR047107; DNA-dir_RNA_pol1_lsu_C.
DR   InterPro; IPR015699; DNA-dir_RNA_pol1_lsu_N.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR000722; RNA_pol_asu.
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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF11; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA1; 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   SMART; SM00663; RPOLA_N; 1.
DR   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|RuleBase:RU004279};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          354..681
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          263..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1332..1387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1399..1464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1429..1464
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1693 AA;  187284 MW;  4D72CB6C79BE94BC CRC64;
     MNISQPVSSA IDSVDFTFLS ASEILSLSVA RIENPETFDT LLHPVPQGLC STCKLKDKAC
     PGHVGHIELP VPVYHPTFMT QMLRLLRAKC RYCHYLRLSR KEVNRYLCKL RLIQYGLLNA
     AEEVDNIEVS NTEDADGSGG EDGQASSVEK LIRLRNAHVK RNIKVAKQNQ WDWQREKNEA
     VAEARRVTIK EFLKTITTGK TCSNCKGISP TYRKDRFVKI FRKDLSPKEK AKMSLANIQA
     KNAVTTLRER EKRKADGDFD EGIADIDLSS NESNEDEEGD GEDLDVDGDV VMGDTATKTA
     RSSKSKVAAT PQIYCNPMEV KAELILLFEN EQEILSLVYN SRSTVKKAAV VSPDMFFMQT
     LLVPPNKFRP EAKTGAGEIT ENPQNTLYKS ILRGCLLVSQ IYDEVNGLTE ETPYRIRDFG
     DLQESWAGLQ DAVNSLIDRD RNPIQGAAGK KNEDGIKQKL EKKEGLFRKN MMGKRVNFAA
     RSVISPDPNI ETNEIGVPPV FAKKLTYPEP VTSHNFKELQ QAVINGPDIW PGAQAIENEH
     GQVISLTIKT PDERLALANQ LLAPSNNRAN GSRNKKVHRH LTNGDVVLMN RQPTLHKPSM
     MGHRARVLTG EKTIRMHYAN CNTYNADFDG DEMNMHFPQN EVARAEVLQI ADTDHQYLAG
     TFGKPLRGLI QDHISVSVWM CSRDTFFDRA TYQQLIYNSL RPESGHIVGD RIETVTPAII
     KPKPLWTGKQ VITTILRNIK PVDCAPLGLN SKPSVPGDRW GSDSNEDRVL FKGGEFITGI
     LDKAQIGPSG GGFIHAIHEV YGPTAAGKTL SILGRLLTKF LHMRAFTCGM DDLRLTPRGE
     QARRDTLKEA HRLGLEVASK YVSLQDQKPT DTDAELMERM EDVLRDDSKQ GGLDVMMNAR
     SGNLSSQITK ACLPDGLVKQ FPKNQMQNMT VSGAKGSAVN ANLISCNLGQ QVLEGRRVPV
     MVSGKSLPCF RPYETNIRAG GYIVNRFLSG IRPQEYYFHA MAGREGLIDT AVKTSRSGYL
     QRCLIKGMEG LKVEYDTSVR DSDGSMVQFL YGEDGLDVTK QVHLQDFKFL LENITSELSQ
     LNYGDPNYEQ IFSEKEIILK KMKKALKYSK ANDPNGPDPV LSSFNPGKYG YATSEKFYDA
     LTNYLKANPD GMVKDKEHPD GVGVRKALEP VLMAKYLKSV VDPGEAVGIV AGQSVGEPST
     QMTLNTFHLA GHSTKNVTLG IPRLREIVMT ASNHISTPSM TLRVNDELSA EDGEKFAKGI
     SVLSLGEVLD EATVKERVGR GVAFSEARIY EVQVKLFPSK EYIDTYAITV ADVLHTLEKK
     FAPKLQALTR RALGRKKEEK SSKSTKGGVP EIGKSVGAIE DPAAATRRGS EDPQAEDEDD
     DIEEDDAKQV NANALVSYAE NDEEDDQVQA QMQKDSEQDD ADVPDMEDEG IGGSPREPDS
     DGEGQQKVDR QEQRATEASA EREARVMKNC SDVVRFRFDE EAGEWCDITL EYAADVPKIL
     MMTVVEDALR QCLIQQIPGL GACNYIPNQD SSKYGNKIHL PVVQTVGVNL KAMQTYPHII
     NPNTISTNDI AAMLANYGVE ACRATIIQEL AGVFGGHAIS VDNRHLNLIA DFMTRGGGFS
     PFNRNGLRGS VSPFMKMSFE TTVGFLADAV ADGDFDDLSN PSSRIVVGRM SKVGTGAFDV
     LTKVPTVRSD EES
//
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