ID A0A0D3F0T9_9ORYZ Unreviewed; 1950 AA.
AC A0A0D3F0T9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART02G04100.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART02G04100.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART02G04100.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART02G04100.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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 STRING; 65489.A0A0D3F0T9; -.
DR PaxDb; 65489-OBART02G04100-1; -.
DR EnsemblPlants; OBART02G04100.1; OBART02G04100.1; OBART02G04100.
DR Gramene; OBART02G04100.1; OBART02G04100.1; OBART02G04100.
DR eggNOG; KOG0260; Eukaryota.
DR eggNOG; KOG2992; Eukaryota.
DR Proteomes; UP000026960; Chromosome 2.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
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:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd02737; RNAP_IV_NRPD1_C; 1.
DR CDD; cd10506; RNAP_IV_RPD1_N; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.450.40; -; 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; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR040402; NRPD1_C.
DR InterPro; IPR040403; NRPD1_N.
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.
PE 3: Inferred from homology;
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}; Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960};
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 230..529
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1373..1761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1874..1950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1523..1542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1550..1584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1611..1635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1664..1705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1893..1932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1950 AA; 214586 MW; BF9037478CB9C992 CRC64;
MSVTWRRTAA GARGGGEGIL MEEDQSAIPV AEGAIKSIKL SLSTEDEIRT YSINDCPVTH
PSQLGNPFLG LPLETGKCES CGASENGKCE GHFGYIELPV PIYHPCHVTE LRQILNVVCL
KCLRVKKGKV KQTEGKDNTS ALSCYYCRDL PALSLKEIKT ADGAFRLELK MPPRKFMTEG
SWNFLDKYGF HHGGTSHCRT LLPEEALNIL KKIPEETKRK LAARGYIAQS GYVMKYLPVP
PNCLYIPEFT DGQSIMSYDI SISLLKKVLQ KIEQIKKSRA GSPNFESHEV ESCDLQLSIA
QYIHLRGTTR GPQDNTKRFA ISTDPSALST KQWLEKMRTL FISKGSGFSS RSVLTGDPYI
GVDVIGLPSE VAKRITFEEQ VTDINLNRLQ EIVDKGLCLT YRDGQATYAI TVGSKGHTTL
KVGQTISRRI VDGDVVFLNR PPSTHKHSLQ AFRVYVHEDH TVKINPLICA PFAADFDGDC
VHIYYPQSLA AKAEALELFS VEKQLTSSHS GKVNLQLVSD SLLALKHMSS RTMLSKEAAN
QLAMLVTCSL PDPAVIKSKP YWTISQIVQG ALPKALTSQG DKHVVRDSTI IKLDLDKESV
QTSFSDLVYS TLSVKGPGEA LQFLNVLQPL LMELILLDGF SVSLQDFNVP KVLLEEAQKN
IEKQSLILEQ SRFAENQVVE MRVDNNLKDI KQQISDFVVK RSHLGLLIDP KSDSSVSKVV
QQLGFVGLQL YREGKFYSRR LVEDCYYTFV NKHPAVREEH SPEAYGLVRS SYFHGLNPYE
ELVHAISTRE AIVRSSRGLT EPGTLFKNLM ALLRDVVICY DGTVRNVCSK SIIQLNYMED
DALDFPSAIG PGEPVGVLAA TAISNPAYKA VLDASQSNNT SWERMKEILQ TTSRYKNDMK
DRKVILFLND CSCAKKFCKE KAAIAVQGCL RRITLEDCAT DICIEDGNWA APAGFQHPVP
PPQCKILPVP IPIPAHGSVK FPPVPIPAPE HLKYNIHVVR YQKQIGLDGT SEAAPALVGH
IHLDRAHLER INISTEDILQ KCQEVSGKYG KKKGHLSNLD CSFTQKLVDG KLPKLPCLQF
FVSDNMIVSE SVERAVSVLA DSLCGVLLNT IIKGDPRIQE AKIVWVGSDA TSWVKNTQKA
SKGEPAVEII VEEEEALHIG DAWRTTMDAC IPVLNLIDIR RSIPYGIQQV RELLGISCAF
DQVVQRLSTT VRMVAKDVLK DHLVLVANSM TFTGNLNGFN NAGYKATFRS LKVQVPFTES
TLITPMKCFE KAAEKCHSDS LGCVVSSCSW GKHAASGTGS SFQILWNESQ LKSNKEYGDG
LYDYLALVRT DEEKARYTFF DDVDYLAEEN EADVCLSPEL DGTIGQPIFD DNLEEQDVQN
NSSWDNGTTT NASWEQNGSA GNDSDKWGGW NDAAAGADTG VTKPADQGNS CWDVPATVEK
SSSDWGGWGT EKAKEKEKIS EEPAQHDAWS VQGPKRATDG GASWKKQSST QNDGNSWKEN
KGRGSNGGSW EKDNAQKGSW GRGNDEAENN NDVQNKSWET VAADAHASTE KSWGNVTASP
SDNAWSAAPV SQGNGISQGN ERSDAKQSDS WDGWKSAGVD KAINKDKESL GNVPASPSFS
AWNAXPVSQG NERXDAKQSD SWDGWKSAGV DKAINKDKES LGNSAGVDAS TNKDKESWGN
VPASPSDSAW NAAPVSQGDD VWNSAEANES RNKDWKSDGW GARGGNWRGQ RNNPGRPPRK
PDGRGLPRRP DERGPPRRHF DLTAEEEKIL GEIEPTVLSI RKIFRESIDS IKLSPEDEKF
IKENVLEHHP EKQSKVSGEI DHIMVDKHQV FQDSRCLFVV SSDGTRSDFS YLKCMENFVR
KTYPEHGDSF CKKYFKRRRD QPPAADGGTA PGTPAGATQS TAVDTQEGTS QQTQPDIATA
PAATQQETLQ DTPAPPADDG LLGKGPSPSD
//