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Database: UniProt
Entry: A0A061FR78_THECC
LinkDB: A0A061FR78_THECC
Original site: A0A061FR78_THECC 
ID   A0A061FR78_THECC        Unreviewed;      1788 AA.
AC   A0A061FR78;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   ORFNames=TCM_045152 {ECO:0000313|EMBL:EOY19810.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY19810.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY19810.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(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|RuleBase:RU004279};
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000256|RuleBase:RU004279}.
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DR   EMBL; CM001888; EOY19809.1; -; Genomic_DNA.
DR   EMBL; CM001888; EOY19810.1; -; Genomic_DNA.
DR   STRING; 3641.A0A061FR78; -.
DR   EnsemblPlants; EOY19809; EOY19809; TCM_045152.
DR   EnsemblPlants; EOY19810; EOY19810; TCM_045152.
DR   Gramene; EOY19809; EOY19809; TCM_045152.
DR   Gramene; EOY19810; EOY19810; TCM_045152.
DR   eggNOG; KOG0260; Eukaryota.
DR   eggNOG; KOG2992; Eukaryota.
DR   HOGENOM; CLU_002449_2_0_1; -.
DR   InParanoid; A0A061FR78; -.
DR   OMA; WGSQQKS; -.
DR   Proteomes; UP000026915; Chromosome 10.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:GOC.
DR   CDD; cd02737; RNAP_IV_NRPD1_C; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.10.450.40; -; 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; 1.
DR   Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR040402; NRPD1_C.
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; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF51; DNA-DIRECTED RNA POLYMERASE V SUBUNIT 1; 1.
DR   Pfam; PF11523; DUF3223; 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; 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.
DR   PROSITE; PS50896; LISH; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|RuleBase:RU004279}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004279};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
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          205..504
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1458..1477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1492..1631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1504..1521
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1542..1611
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1612..1626
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1788 AA;  198799 MW;  182D0CA71CE284FD CRC64;
     MEENSSASTV DGEIVGIGFC LATPREIFTA SISGFPINHV SQLSNSYLGL PLEFGKCNAC
     GTSEPGKCEG HFGYIELPIP IYHPSHISEL KRLLSLLCLK CLRMKNKFQI KSGSISDRLL
     ASCCENAPQV SIKEVKTTDG ACSLELKQPS RQARTSWEFL EKYGFRYGDH HNTRTLLPCE
     VMEILKRIPA ETRRKLSGKG FFPQEGYILR YLPVPPNCLS VPDISDGVSI MSSDLSTAML
     KKVLKQVEII KSSRSGTPNF ESHEVEANDL QSAVEQYLQV RGTVKASRNI DARYGISKDA
     SDSSTKAWLE KMRTLFIRKG SGFSSRGVIT GDPYKKVNEI GIPSEIAQRI TFEERVNMHN
     MRYLQNLVDN KLCLTYRDGS STYSLREGSK GHTFLRPGQV VHRRIMDGDI VFINRPPTTH
     KHSLQALSVY VHDDHTVKIN PLICGPLSAD FDGDCIHLFY PQSLAAKAEV FELFSVEKQL
     LSSHNGNLNL QLATDSLLSL RVMLKTLLFK KADAQQLSMF LSSALPQPAF LKGNSFGPCW
     TALQILQTAF PACLDCSGDR YLISKSDILT VDFSRDLMQS VINEVVTSIF FEKGPKEVLN
     FFDSLQPLLM ENVFAEGFSV SLEDFSVSRE VIQNIQKDIQ DISPLLYQLR STYNELVGLQ
     MENHIRVAKA PVANFILNSS ALGDLIDSKS DSTVNKVVQQ IGFLGLQLSN KGKFYSKTLV
     EDVAYQFQSI YPSDGVDYPS AEFGLIKSCF FHGLDPYEGM VHSISTREVI VRSSRGLSEP
     GTLFKNLMAI LRDVVICYDG TVRNISSNSI IQFQYGLNAR TKPQFPAGEP VGVLAATAMS
     NPAYKAVLDS TPSSNSSWEL MKEILLCKVS LKNDLVDRRV ILYLKDCDCG RKYCQENAAY
     LVKNHLRKVK LKDTAVELIF EYKQQQTVSE SEAGLVGHIL LNKAVLKELN ISMQEVHMKC
     QETIISFRKK KKTADTFKRT DLFFSECCSI QQSCGGKWLD MSCLMFFCRN TKDDHLDCTL
     QDLVDIIYPV LLETVIKGDP RICSANIIWV SPDTTTWIRS PSKTQKGELA LDVVLEKSAV
     KQNGDAWRTV IDCCLPVINL IDTQRSIPYA IKQVQELLGI SCAFEQAVQR LSTSVSMVAR
     GVLKEHLILL ANSMTCAGNL IGFNSGGYKA LSRSLNIQVP FSEATLFTPR KCFERAAEKC
     HVDSLSSIVA SCSWGKHVAV GTGSRFDVLW DRKEVGFDQK SGIDVYNFLH MLSSASGPSS
     TTTCLGEEVD DLMDVDNMAE WSLSPEHSNG LDKPVFEDAA DFENDLDFQP AESSWEKGVS
     LDKVSSWNVS SAWNKKAEDG DKFAAALTST TKQSDWCDWG TSKSKTQDAA AAATSTTKKT
     EWCDWGTSKS KTQEVAATVT GTAEQNEWCD WRTSKSKIQV VAAAVTSTTK QSEWGDWGTS
     KSKTQDVAAA VTGTMETEWG DWGKGKSKTQ DVSPKVDGTC VNEQTKLSDW GLKKNDTQDV
     SMEEKTFKSN GADTGTSWGT MGKESEKPDA NDALPWSGWG TQDVIPTKTL DDSSKSSGWE
     QQKSPECSQG WGSLDESNQP ASSNGWDTPN GLGSTQSEKQ HQWGQSRGSR RWASDASKKN
     HPVKSARVMN DDSSMAAMYT ATRQRLDMFT SEEQDILSDV EPLMQSIRKI MHQSGYNDGD
     PLSALDQSFI LENVFTHHPD KAIKMGAGVD YVMVSKHSNF PDSRCFYVVS TDGRKQDFSY
     RKCLDNFIKG KYPDMADVFI AKYFRKPRFG GFRERSVAPE NTEGENRK
//
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