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Database: UniProt
Entry: A0A2G2XG60_CAPBA
LinkDB: A0A2G2XG60_CAPBA
Original site: A0A2G2XG60_CAPBA 
ID   A0A2G2XG60_CAPBA        Unreviewed;      1816 AA.
AC   A0A2G2XG60;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   ORFNames=CQW23_04935 {ECO:0000313|EMBL:PHT56449.1};
OS   Capsicum baccatum (Peruvian pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=33114 {ECO:0000313|EMBL:PHT56449.1, ECO:0000313|Proteomes:UP000224567};
RN   [1] {ECO:0000313|EMBL:PHT56449.1, ECO:0000313|Proteomes:UP000224567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. PBC81 {ECO:0000313|Proteomes:UP000224567};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PHT56449.1};
RX   PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA   Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA   Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA   Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA   Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA   Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA   Bennetzen J.L., Choi D.;
RT   "New reference genome sequences of hot pepper reveal the massive evolution
RT   of plant disease-resistance genes by retroduplication.";
RL   Genome Biol. 18:R210.1-R210.11(2017).
RN   [2] {ECO:0000313|Proteomes:UP000224567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. PBC81 {ECO:0000313|Proteomes:UP000224567};
RA   Kim S., Park J., Yeom S.-I., Kim Y.-M., Seo E., Kim K.-T., Kim M.-S.,
RA   Lee J.M., Cheong K., Shin H.-S., Kim S.-B., Han K., Lee J., Park M.,
RA   Lee H.-A., Lee H.-Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E.,
RA   Jeon J., Kim H., Choi G., Song H., Lee J., Lee S.-C., Kwon J.-K.,
RA   Lee H.-Y., Koo N., Hong Y., Kim R.W., Kang W.-H., Huh J.H., Kang B.-C.,
RA   Yang T.-J., Lee Y.-H., Bennetzen J.L., Choi D.;
RT   "Multiple reference genome sequences of hot pepper reveal the massive
RT   evolution of plant disease resistance genes by retroduplication.";
RL   J. Anim. Genet. bioRxivorg:115410-115410(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PHT56449.1}.
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DR   EMBL; MLFT02000002; PHT56449.1; -; Genomic_DNA.
DR   STRING; 33114.A0A2G2XG60; -.
DR   Proteomes; UP000224567; Chromosome 2.
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; 17.
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; 15.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000224567};
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          212..518
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1508..1816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          664..691
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1508..1721
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1734..1803
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1816 AA;  201860 MW;  3094C9FA32CF2D45 CRC64;
     MSVVHIEHGE TTERGKPKPG GLSDPRLGTI DRKMKCETCM ANMAECPGHF GHLELAKPMF
     HIGFMKPVLS ILRCVCFNCS KILADEEDPK FKQAMRIRNP KNRLRKMLDA CKNKTKCEGG
     DEIDVQSQDT EEPVRKSRGG CGAQQPKISI DGMKMVAEYK MQKKKSDDPE QMPEPVERKQ
     QLSAERVLSI LKRVSDEDCV LLGLNPEYAR PDWMILQALP IPPPPVRPSV MMDTSSRSED
     DLTHQLAMII RHNENLKRQE RNGAPAHIIS EFAQLLQFHI ATYFDNDLPG QPRATQRSGR
     PIKSICSRLK SKEGRIRGNL MGKRVDFSAR TVITPDPTIN IDQLGVPWSI ALNLTYPETV
     TPYNIERLKE LVEYGPHPPP GKTGAKYIIR DDGQRLDLRY LKKSSDQHLE LGYKVERHLN
     DGDFVLFNRQ PSLHKMSIMG HRIKIMPYST FRLNLSVTSP YNADFDGDEM NMHVPQSFET
     RAEVLELMMV PKCIVSPQAN RPVMGIVQDT LLGCRKVTKR DTFIEKDVFM NILMWWEDFD
     GKVPAPAILK PRPLWTGKQV FNLIIPKQIN LLRYSAWHND SEKGYITPGD TQVRIEKGEL
     LSGTLCKKTL GTSTGSLIHV IWEEVGPDAA RKFLGHTQWL VNYWLLQQAF SIGIGDTIAD
     AATMEKINET ISNAKSKVKE LIKAAQEKQL EAEPGRTMME SFENRVNQVL NKARDDAGSS
     AEKSLSESNN LKAMVTAGSK GSFINISQMT ACVGQQNVEG KRIPFGFIDR TLPHFTKDDY
     GPESRGFVEN SYLRGLTPQE FFFHAMGGRE GLIDTAVKTS ETGYIQRRLV KAMEDIMVKY
     DGTVRNSLGD VIQFLYGEDG MDSVWIETQK LDSLKAKKST FEDMYAYEID DPNWNPSYML
     LEAVEDLKGI REIRSVFDAE VQKLEADRHQ LGTEIAVTGD NSWPLPVNIQ RLVLNAQKTF
     KIDFRRPSDM HPMEIVEAVD KLQERLKVVP GDDYLSMEAQ KNATLFFNIL LRSALASKRV
     LKEYRLSREA FEWVVGEIES RFLQSLVAPG EMIGCVAAQS IGEPATQMTL NTFHYAGVSA
     KNVTLGVPRL REIINVAKKI KTPSLSVYLK PEVGKTKERA KTVQCALEYT TLRSVTQATE
     VWYDPDPMST LIEEDVEFVK SYYEMPDEEI DPDKISPWLL RIELNREMMV DKKLSMADIA
     EKINLEFDDD LTCIFNDDNA EKLILRIRIM NDEAPKGELD ESAEDDVFLK KIESNMLTEM
     ALRGIPDINK VFIKNSKVQK FDDNEGFKAE NEWMLDTEGV NLLAVMTHED VDASRTTSNH
     LIEVIEVLGI EAVRRALLDE LRVVISFDGS YVNYRHLAIL CDTMTYRGHL MAITRHGINR
     NDTGPMMRCS FEETVDILLD AAVFAESDYL KGVTENIMLG QLAPIGTGGC ALYLNEEMLK
     QAIEIPLPSY MEGGLEFGMT PGRSPISGTP YHDGMMSPNY LLSPNMRMSP MTDAQFSPYV
     GGMAFSPTSS PGYSPSSPGY SPSSPGYSPT SPGYSPTSPG YSPTSPGYSP TSPTYSPSSP
     GYSPSSPAYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPA YSPTSPAYSP
     TSPAYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPTY SPTSPSYSPT SPAYSPTSPG
     YSPTSPSYSP TSPSYSPTSP SYNPSARYSP SLAYSPTSPK LSPSSPYSPS SPSYSPTSPS
     YSPTSPSYSP SSPTYSPSSP FNNSGTSPDY SPSSPQYSPS AGYSPSAPGY SPSSTSQYTP
     RISDRDNKSV KDDKTG
//
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