ID A0A061EX26_THECC Unreviewed; 1689 AA.
AC A0A061EX26;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 55.
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_024782 {ECO:0000313|EMBL:EOY09356.1};
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:EOY09356.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY09356.1, 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|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; CM001883; EOY09356.1; -; Genomic_DNA.
DR STRING; 3641.A0A061EX26; -.
DR EnsemblPlants; EOY09356; EOY09356; TCM_024782.
DR Gramene; EOY09356; EOY09356; TCM_024782.
DR eggNOG; KOG0262; Eukaryota.
DR InParanoid; A0A061EX26; -.
DR OMA; NREDYQQ; -.
DR Proteomes; UP000026915; Chromosome 5.
DR GO; GO:0005736; C:RNA polymerase I 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:0006360; P:transcription by RNA polymerase I; IEA:GOC.
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; 2.40.40.20; -; 1.
DR Gene3D; 3.30.70.2850; -; 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; 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}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
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 341..659
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 749..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1362
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1689 AA; 189181 MW; D5880006F8E991CF CRC64;
MAQITEGATD SVEAVRFNFM TTEEVRKHSF LKVTNANLLD LMDRPMPGGL YDAVLGPLED
RTPCKSCGLL KLHCPGHCGH IDLVSPIYNP LLFNFLHTLL QRICFFCYHF RAEKTEVERC
VSQLKLIGNG DIVGAKRLDS DSADASSYSD YNEGSQESGS IVHNSEAVKP KEWTSLQLME
AMSVLNNFLK LKYNKCKNCD AKNPNITKPV FGWLHMNGML GAQMRENVIR GCKMVDTFSD
EAGSGLEDAD DVSSSGNGVD IAEMDTSEIG FTGSEGNGAK ARKKKAQVPL EFMKQKNLFS
GPLLPSEVKK ITKLLWENEV ELCSIISDIQ QQGFGKKVGY SMFFLETILV PPIKFRAPTK
GGDSVMEHPQ TVLLSKVLQA NISLGNAYTN NLQSSKAVVR LWMDLQQSVN LLFDSKTAMS
QGRDVSSGIC QLLEKKEGMF RQKMMGKRVN FACRSVISPD PYLAVNEIGI PPYFALRLTY
PERVTPWNVV KLREAIINGS EFHPGATHYV DKLSTKRLPP SQKARISISR KLPSSRGAIA
QPGKNLDYEF EGKIVLRHLQ DGDVVLVNRQ PTLHKPSIMA HVVRVLKGEK TIRMHYANCS
TYNADFDGDE INVHFPQDEI SRAEAYNIVN ANNQYVRPSN GEPIRALIQD HIVSAVLLTK
RDTFLSRDEF NQLLYSSGVS SLAQNSFSGK PGQKVFVSTS EEGMLPIIPA ILKPKPLWTG
KQVISSVLSH ITRGRPPFTV GKTAKIPRDF FRNRRNKNKQ SSREENQPKN DGQKAKVAEK
NSKKEPDEEK ILIYRNDLVR GVIDKAQFAD YGLVHTVQEL YGSNTAGILL SVFSRLFTVF
LQMHGFTCGV DDLLIMEDKD IERKKQLEDC EKKVTEAHYE LFGVKVNSET ELQLEIERTI
RRDGETALTA LDRKMISVLN ENSSKGVLTE LLSEGLVKSM GENCISLMTT SGAKGSKVNF
QQISSFLGQQ ELEGKRVPRM VSGKTLPCFH PWDWAARAGG FISDRFLSGL RPQEYYFHCM
AGREGLVDTA VKTSRSGYLQ RCLIKNLECL KISYDHTVRD ADGSIVQFIY GEDGIDVHQT
SFIAKFEALA LNQDMMSEKL CSQLGEPDDS DKILPDGLRS KAEQFIREEI KKYQHQKIKP
KDFLNLLKLK FLSSLAQPGE PVGVLAAQSV GEPSTQMTLN TFHLAGRGEM NVTLGIPRLQ
EILMTASIDI RTPVMTCPLH KGKTKEDALC LANKMKKITV ADILESMEVS VAPFAVDNGD
ICSIYKLKMM LGKPDKYFEN SDITVKDCEH ILKVVFLREL EDAIQNHLVL LSKISGIKKF
MPDSQRNASN EMDEDVSEGR SRETKNDDDD DDDDADDEER AEDLGLDAQK QKQQTTDEMD
YEDDSEVEQN EGASLAALES EIDMSEDETG TIQINMIGSD NGKDEISQSS PNLENRSNPK
SREEKTGSEP KRKKMKAKFV RKESDRAIFN AIRGLCFEVH FKLKNEPHIL LAQIAEKTAK
KVYIQSFGKI DQCRVTDCSE NQVFYYGEDP KKRKSPSDKE KIQALHTTGV DFGAFWKMED
HIDVRYLYSN SIHAMLNTYG VEAARETIIR EISHVFTSYG IAVNIRHLTL IADFMTHSGR
YRPMSRLGGI AESISPFSKM SFETASKFIV EAAKHGLVDN LETPSSRICL GLPVKMGTGS
FDLMQKVEI
//
