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Database: UniProt
Entry: S9W8A4_SCHCR
LinkDB: S9W8A4_SCHCR
Original site: S9W8A4_SCHCR 
ID   S9W8A4_SCHCR            Unreviewed;      1672 AA.
AC   S9W8A4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   ORFNames=SPOG_02772 {ECO:0000313|EMBL:EPY54005.1};
OS   Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS   NBRC 106824 / NRRL Y48691) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY54005.1, ECO:0000313|Proteomes:UP000015464};
RN   [1] {ECO:0000313|EMBL:EPY54005.1, ECO:0000313|Proteomes:UP000015464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC   {ECO:0000313|Proteomes:UP000015464};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
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; KE546988; EPY54005.1; -; Genomic_DNA.
DR   RefSeq; XP_013020888.1; XM_013165434.1.
DR   STRING; 653667.S9W8A4; -.
DR   EnsemblFungi; EPY54005; EPY54005; SPOG_02772.
DR   GeneID; 25037094; -.
DR   eggNOG; KOG0262; Eukaryota.
DR   HOGENOM; CLU_000487_2_4_1; -.
DR   OMA; NREDYQQ; -.
DR   OrthoDB; 169836at2759; -.
DR   Proteomes; UP000015464; Unassembled WGS sequence.
DR   GO; GO:0005736; C:RNA polymerase I complex; IEA:EnsemblFungi.
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; 6.10.250.2940; -; 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:UP000015464};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          345..684
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          148..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1328..1399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..288
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1331..1350
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1373..1399
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1672 AA;  185863 MW;  780C671C8303B4FF CRC64;
     MNIARPISSE VKNVTFGIYD VEQIEKISVK QIVNPVLFDN LNHPTSGGLY DLALGPYLKN
     SLCATCHLDE RYCPGHFGHI VLPTPAYHPL FFSQMYNLLR STCLYCHHFK LSKVKVHLYG
     CMLKLLDHGL LNESQLVENV SLTEAAVTKP KSASGTEGGS DSEDSGLGND DIAKDASTLM
     RLRDEYVNNA IAQAKGNVHV DSHTTTILLH ERKKVCDNCQ SFSPNFRKEG FAKIFELPLS
     GKNLQYMEHT GKVRSDVLRD TSKKDSEDEG YEGESDSNDD EGEGIDLMEE DPNPMKKKSK
     VSASHGAKYM TSTEVRNHLR RLFSKESSVL TRLYSHKRGS PATSDMFFLQ NIAVPPTRFR
     PASKMGDEVH ENIQNELLTK ILQSSIQIAA LSKDTNVPKN AEGKEAYERG SRAFELLIAA
     FVQLQHDVNS LIDSNRNPTQ MGQSRVVPPG IKQILEKKEG LFRKHMMGKR VNYAARSVIS
     PDPNIETNEI GVPPVFATKL TYPEPVTLFN FNEMRNAVIN GPHKWPGATH IQNEDGTLIS
     LMPLTTEQRT ALANQLLTPQ SNLISSPYSY SRLVNTNKKV YRHVRNGDML ILNRQPTLHK
     PSMMAHKARI LPGEKTIRMH YANCNSYNAD FDGDEMNMHF PQSANARAEA QFIANTDSQY
     LVPTSGDPLR GLIQDHVVMG VWLTCKDTFY TRDEYQQLLY QALKPDETGL FGKIKTIPPA
     ILTPKIFWTG KQVISTILLN LKPSDRPGLN LRGKAKVAGK YWSPNSEEGS VLFEDGELLC
     GVLDKSSFGA SSFGIVHSVH ELYGADIAGR LLSILSRLFT AYAQMRGFTC RMDDLQLGEN
     GDSWRSELLN GGKGFGREAA SEYVGLPSDA NLSVLNANLE EVYRDDEKLQ GLDAAMKGKM
     NGLTSSIINK CIPDGLLTKF PENHMQAMTV SGAKGSNVNV SQISCLLGQQ ELEGRRVPIM
     VSGKSLPSFL PYETSAKAGG FIASRFLTGI APQEYFFHCM AGREGLIDTA VKTSRSGYLQ
     RCLMKHLEGL NVEYDHTVRD ADGSIVQFFY GEDSLDVTKQ KHLTQFEFSA RNYKSLIQKY
     KVKSVLSAVD SEKASSYAKK ALKKPHKYDP VLDKYPPSRY LGSVSEKFQR AVDDYTQKNP
     DKLIASKKES KQDESLLNEA KFKALMQLRY QQSLVDPGEG VGVLASQSIG EPSTQMTLNT
     FHFAGFGAKN VTLGIPRLRE IIMTASANIQ TPQMILRLND NISEQRASAF CKEANKLVLS
     EVAKQVRVVE RISGQGSDEQ SKSYSIHLDL YPRKEYEEEY GAQQEEIERT VSSTFLRVLN
     RNIKGYLSKS RQRKSAGDES SPEVGEALRP LEDIADAPVE GAAQESLEDE DNDATNEKMA
     ARSKQHASYD GPDEGDKDAL RDLKKSQKMD EELDEDDGFK SDESVTEYKE RIQAEKLKAS
     SINEKRALNL QTAQTVLPNC KNIDFDYQNG EWAVVELVFP INTEKLLMVS LVEAACAQTV
     VHEISGITRC YPKPPESAMD TVPKVITEGV NLKAMWEFFN EISMNDISTN DIAAILRIYG
     VEAARNAIIN EVSAVFGVYG IGVDSRHLSL IADYMTFEGG YKAFNRMGIE YNTSPFAKMS
     FETTCHFLTE AALSGDVDTL SNPSARLVMG QVGRFGTGSF DLLTPLVDSA AN
//
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