RPOC2_PLAF7
ID RPOC2_PLAF7 Reviewed; 959 AA.
AC Q25802; A0A5K1K9C5;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'';
DE EC=2.7.7.6 {ECO:0000250|UniProtKB:P0A8T7};
DE AltName: Full=PEP;
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'';
DE Short=RNA polymerase subunit beta'';
GN Name=rpoC2 {ECO:0000303|PubMed:27458998}; Synonyms=rpoD;
GN ORFNames=PF3D7_API04200 {ECO:0000305};
OS Plasmodium falciparum (isolate 3D7).
OG Plastid; Apicoplast.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BW/C10;
RX PubMed=8757284; DOI=10.1006/jmbi.1996.0449;
RA Wilson R.J.M., Denny P.W., Preiser P.R., Rangachari K., Roberts K., Roy A.,
RA Whyte A., Strath M., Moore D.J., Moore P.W., Williamson D.H.;
RT "Complete gene map of the plastid-like DNA of the malaria parasite
RT Plasmodium falciparum.";
RL J. Mol. Biol. 261:155-172(1996).
RN [2] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RG Pathogen Informatics;
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION.
RX PubMed=27458998; DOI=10.1016/j.protis.2016.06.003;
RA Nisbet R.E.R., Kurniawan D.P., Bowers H.D., Howe C.J.;
RT "Transcripts in the Plasmodium Apicoplast Undergo Cleavage at tRNAs and
RT Editing, and Include Antisense Sequences.";
RL Protist 167:377-388(2016).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000250|UniProtKB:P0A8T7}.
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:0000250|UniProtKB:P0A8T7};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0A8T7};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A8T7};
CC -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core is
CC composed of four subunits: alpha, beta, beta', and beta''. When a
CC (nuclear-encoded) sigma factor is associated with the core the
CC holoenzyme is formed, which can initiate transcription (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, apicoplast
CC {ECO:0000305|PubMed:27458998}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=VWP78959.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X95275; CAA64574.1; -; Genomic_DNA.
DR EMBL; LR605956; VWP78959.1; ALT_SEQ; Genomic_DNA.
DR PIR; S72284; S72284.
DR AlphaFoldDB; Q25802; -.
DR STRING; 36329.Q25802; -.
DR PRIDE; Q25802; -.
DR InParanoid; Q25802; -.
DR Proteomes; UP000001450; Apicoplast A.
DR Proteomes; UP000001450; Chromosome: api.
DR GO; GO:0020011; C:apicoplast; IEA:UniProtKB-SubCell.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.132.30; -; 1.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR PANTHER; PTHR19376:SF11; PTHR19376:SF11; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
PE 3: Inferred from homology;
KW Apicoplast; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Plastid; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..959
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000344060"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT CONFLICT 524
FT /note="K -> KK (in Ref. 1; CAA64574)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 959 AA; 117860 MW; 0E3810F870431D28 CRC64;
MYFYFFNKYN LKILEKKLLI IFKYNISFKI LHELLYLGYE YSFLYNYSLN IKDFSNFIYL
LILYKNKINN IYNNKYYEIK NNYINVFLNN YYYLKVINKI QGILNNNLYN KINPIYSNLF
LFFNNKIKIK YSQLQQLIGY KGYISNIKGM IYEKPVINNY INELNIYEYI LSCYGSKKGI
IDTALKTADS GYLTKRLINI TSNFIIKELN CKSPFILKYI LNMDIYGNII LPLNILRFKI
LQNNILNLNN GTFIYTKNTY ITKYILNKLL NLYNRRNIYL NIKSVYLCNI YNNICNTCLN
YKQLYKYNLG QHIGVISSEA ISEPSTQMVL RTFHASSILK DKFNFNKYLI YKIYLYKLNI
NKIFKLIINF KKYINIKFNL IFLMNKILYN YNNILFEYKY ILQNQYIKCN FIYNSISKNF
KYNLNNIIIK YLNNVIKYYN YSNIQLLIKN IHNKWILYNI YTYYLYYYHI KFYNLYNKGI
ILNNNNNKYN VIYFLINYFN LFSNYYYKIY NNNYNFINSN YYFKMNFILK NFNNIQILNK
LFYVNNIFIY YKYEKKLFIY LNIINNIIIK KYLNFYKYTY NKLFFIKKYN NFLYLYEIFK
YNWYKYLLLN NKYNLYIIYN NYIKYLYKYN ININLYFIKN LFYNNNNFIH NHIIYKNNYY
IYNNNMNLYQ YNKNILINNN LLYNKLFYNY INNNIYNLYL NDITIGLQSI NIIFENKNIK
DNIFFISNNI YVIFYIKYYN YLNNIIYIYN ICNKYNINHY KYKLNFYSYI FEDISSILYS
GYSLHTEFYS INKNLKYYFR FLLKSINIYQ ATKSSYIYVY NILIESILKQ YSYQNIYLPS
IYFELIIKKM LSCIKIISNN FKIFKYNDII SLQLINIINY SLNLNKHYIY KYEPIILGIT
KSILANSGFL TNISFQNTFK IISLNILNNK IDWLIDIKSK IILTDLLPVG NGWYRYLVN
