ID   RPOB_NEOCA              Reviewed;        1050 AA.
AC   Q9NJN5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta;
DE            EC=2.7.7.6;
DE   AltName: Full=PEP;
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta;
DE            Short=RNA polymerase subunit beta;
GN   Name=rpoB;
OS   Neospora caninum (Coccidian parasite).
OG   Plastid; Apicoplast.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX   NCBI_TaxID=29176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUGGESTION OF ALTERED GENETIC CODE.
RC   STRAIN=Nc1;
RX   PubMed=10608442; DOI=10.1016/s0020-7519(99)00119-8;
RA   Lang-Unnasch N., Aiello D.P.;
RT   "Sequence evidence for an altered genetic code in the Neospora caninum
RT   plastid.";
RL   Int. J. Parasitol. 29:1557-1562(1999).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000250}.
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;
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 (Potential).
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, apicoplast.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000305}.
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DR   EMBL; AF138960; AAF14261.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9NJN5; -.
DR   SMR; Q9NJN5; -.
DR   VEuPathDB; ToxoDB:NCLIV_028180; -.
DR   VEuPathDB; ToxoDB:NCLIV_034580; -.
DR   GO; GO:0020011; C:apicoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; 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:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.30.150.10; -; 1.
DR   Gene3D; 2.40.270.10; -; 2.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR   InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR   InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR   InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR   InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR   InterPro; IPR007645; RNA_pol_Rpb2_3.
DR   InterPro; IPR007641; RNA_pol_Rpb2_7.
DR   InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
PE   3: Inferred from homology;
KW   Apicoplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW   Transcription; Transferase.
FT   CHAIN           1..1050
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000300455"
SQ   SEQUENCE   1050 AA;  123935 MW;  65CDC2DDEF899E85 CRC64;
     MAFKIKTFLS IKSHKIFYTD FYFFLKKKLI ILIKNIFPEY FNFNNKYKNW NLICLPDFLY
     FKVNNTHFLD NVQYINSLIK IFLPLKFQNL KTNQIFFKNL LIFELPKYNS HNYCYLNGLK
     KIFISKYFTS NGIFFHKYLK RKYDIYYAKI LLTNSNFFNI VLDLKLKQIY LSIKNLKFNF
     ILFLYYLGIN NKDILKYSRY KKSKILKLLI FTALQTNLIN NKKFILKNLN YLKSIFKVTN
     LNKNYKHFII NKNKLNYNYG NFNKNNFLTI DFIFILDLLL DLQSKKLCFK NIDHLDNKHI
     NTIGNYFQHN FKFYLKKFIS IIPNLIKLKK FSLLKVYNFK ELLILNPLIQ YLEQINSFSE
     LTHKYKLNNY NSSLKGILNL REICLNQIGK LCLIDTTEGI NCGLIVNFAK HIRIYKKGII
     QIYVSPVFKN KTKEFINFKT SLDQELYLIQ FNNINLRKNK LFNENIKVVY NKNNFRIKFI
     SNKKSFLLKF ADLFSFTENL IPFIKYNDPA RCLMGAKMQS QSVPLLNKKK SFVVTGYEKE
     IITKSDITIK ALQEGIVLNA SSLKIHIKDL FNREIVYYLS KYKKSNQNTL IHQKPLVWNG
     ERVFTNQLLT QHQDIIDSEF AIGNNLLIYY GNFCGYDFED AVIGSKRVLY QQLFSSLHMD
     IYEFNFGYNN ENDIEFSTLE IPKQSYYIKK SLDSLGIVKE GEKILTGNIL LTKIKVTKPN
     YTYKSIFKLI YSIFGKTIRN IKDNSLYIQT GKNGRVSKIE LFLINTNSHY KTYNNSYLKC
     RIFICKQRFL TVGDKLCGRY GNKGILSYIA ENADLPFLQN SFYPDIIVGA LGIPSRMNLG
     QLFEALVGKI GFSYNIRILP SFTSSSNAYF NYLKILIYNF LMFNNLKKGF NWLYNFNLPG
     KFLIRDGRTG IKLKSSVLCG VSRYSKLIHM IKDKLHFRTT GPYTEILQQP LKGKKNLGGQ
     RFGEMEIWAL EAFGASYNLK EILNYKSDDC FARNNLKDYL LFRNSELQNS TITESFRVIL
     KEFNGLILNL ELFLITDDLE ENYLNLTINY