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
//