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Database: UniProt
Entry: D8SYZ7_SELML
LinkDB: D8SYZ7_SELML
Original site: D8SYZ7_SELML 
ID   D8SYZ7_SELML            Unreviewed;      1797 AA.
AC   D8SYZ7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   ORFNames=SELMODRAFT_128226 {ECO:0000313|EMBL:EFJ10314.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ10314.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(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   -!- 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; GL377654; EFJ10314.1; -; Genomic_DNA.
DR   RefSeq; XP_002988518.1; XM_002988472.1.
DR   STRING; 88036.D8SYZ7; -.
DR   EnsemblPlants; EFJ10314; EFJ10314; SELMODRAFT_128226.
DR   Gramene; EFJ10314; EFJ10314; SELMODRAFT_128226.
DR   KEGG; smo:SELMODRAFT_128226; -.
DR   eggNOG; KOG0260; Eukaryota.
DR   HOGENOM; CLU_000487_3_0_1; -.
DR   InParanoid; D8SYZ7; -.
DR   OMA; MVQYDRT; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; IBA:GO_Central.
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; 27.
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; 19.
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:UP000001514};
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          253..559
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          161..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1557..1797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1797 AA;  200676 MW;  61F57E22E861B192 CRC64;
     MDLRFPYSPA ELARVKRVQF GLMSPDEIRQ MSVCKIESSE TYDRGKPKSG GLSDPRLGTI
     DRQTKCETCG GSMAECPGHF GHLELAKPMF HIGFLKTVLA LLRCVCYNCS HILALEVCRE
     TLLLCFIFGL FKLAKKAKNP KQRLKKVLEC CKNKQKCEGN NNDMDGEQDD QEGEQKGHGG
     CGAQQPKITI DGMKIIAEFK VPKKKGDDQD QYLPEPVERK QQLTAERVLG ILKRISDEEC
     RILGLDPQFA RPDWMILQVL PIPPPPVRPS VMMDSSARSE DDLTHQLAMI IRHNNNLKRQ
     EQNGAPTHII NEFTQLLQFH IATYFDNDLP GQPRATQRSG RPIKSICQRL KAKEGRIRGN
     LMGKRVDFSA RTVITPDPNI NIDELGVPWS IALNLTYPET VTPYNLERLK ELVEYGPHPP
     PGKTGAKYII REDGQRLDLR YLKKSSDRHL ELGYKVERHL CDGDFVLFNR QPSLHKMSIM
     GHRIRIMPYS TFRLNLSVTS PYNADFDGDE MNMHVPQSFE TRAEVSELMI VPKCIVSPQS
     NRPVIGIVQD TLLGCRKVTK RDTFIEKDVF MNILMWWEDF DGKVPTPAIV KPRPIWTGKQ
     IFSLIIPKQI NMVRTAAWHN DSETGDNSPG DTMVRIEKGE LLTGTLCKKT LGTSSGSLIH
     VIWEEVGPDA ARKFLGHTQW LVNYWLLQHG FSIGIGDTIA DSATMEKIND TIFKAKNEVK
     DLIKIAQEKQ LESQPGRTMM ESFENRVNQV LNRARDEAGS SAQKSLSESN NVKAMVTAGS
     KGSFINISQM IACVGQQNVE GKRIPFGFID RTLPHFTKDD YGPESRGFVE NSYLRGLTPQ
     EFYFHAMGGR EGLIDTAVKT SETGYIQRRL VKAMEDVMVK YDGTVRNSLG DVIQFLYGED
     GMDAVWIESQ HLDSIKMKKK NFDMTYKFEV DNENWNPDYM ASDCAEDIKT IQEIRNVFDA
     EVQKLEADRK QLGLEIATSG EPHWPLPVNL KRLIWNAQKI FKIEMKKPSD MHPMEIVEAV
     DKLQEKLLVV PGDDPISIEA QKNATLFFNC LLRSTFASKR VLKEYRLTKE AFEWVIGEIE
     TRFLQSLVAP GEMIGCVAAQ SIGEPATQMT LNTFHYAGVS AKNVTLGVPR LREIINVAKK
     IKTPSLYVHL KPEVSKEKER AKNVQCALEY TTLRSVTQAT EIWYDPDPMS TIIEEDVEFV
     KSYYEMPDED VTPDKISPWL LRIELNREMM VDKKLSMADI AEKINLEFVD DLTCIFNDDN
     AEKLILRVRI MNDDVSKGGE VDQSDDDVFL KKIESNMLTE MALRGIPDIH KVFIREHKRQ
     RFDEHEGFKT ETEWMLDTEG VNMLAVMCNE DVDATRTVSN HLIEVIEVLG IEAVRQALLK
     ELREVISFDG SYVNYRHLAI LCDVMTYRGH LMAITRHGIN RNDTGPMMRC SFEETVDILL
     DAAVFAEADH LRGVTENIML GQLAPIGTGD FGLLLNDKML EHAIELQLPS YMETADFGLG
     GVTGTPHHEG MMSPSYLLSP NLRASPITDA QFSPYVGGIT FSPGAYSPLS PAYSPAGYSP
     ASPNYSPSSP TYSPSSPAYS PASPAYSPSS PGYSPASPAY SPTSPSYSPT SPSYSPTSPS
     YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT
     SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPAY
     SPTSPSYSPT SPSYSPTSPS YSPTSPAYSP TSPAYSPSSH TYSPSSLKYS SASPSYR
//
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