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RPOC2_EUGLO
ID   RPOC2_EUGLO             Reviewed;         817 AA.
AC   P58132;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=rpoC2;
OS   Euglena longa (Euglenophycean alga) (Astasia longa).
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCAP 1204-17a;
RX   PubMed=11212895; DOI=10.1078/s1434-4610(04)70033-4;
RA   Gockel G., Hachtel W.;
RT   "Complete gene map of the plastid genome of the nonphotosynthetic euglenoid
RT   flagellate Astasia longa.";
RL   Protist 151:347-351(2000).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
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.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ294725; CAC24617.1; -; Genomic_DNA.
DR   RefSeq; NP_075006.1; NC_002652.1.
DR   AlphaFoldDB; P58132; -.
DR   PRIDE; P58132; -.
DR   GeneID; 802544; -.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell.
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:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; PTHR19376; 3.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW   Plastid; Transcription; Transferase; Zinc.
FT   CHAIN           1..817
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000067915"
FT   BINDING         219
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         291
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   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
SQ   SEQUENCE   817 AA;  94915 MW;  720F598DD33D7C89 CRC64;
     MYSKNIIYFN KAFDKIEIKN LINWFLINYG NIKTTKLLDK IKKFGLIHAT NAGISIGLND
     LIIPPSKKNL VEISNKNLNK INKKFKNGKI NLITYLIKEK RTWDNMNENL KIESIKNLKQ
     NDLLNSLYTM TLSGARGNIN QVKQLISMRG LISDSQGNLL NLPIKTNFKE GLNIVEYFIS
     CYGARKGIID TSLKTANAGY LTRRLIFASQ NTIIRKTNCF TKYKKKIKIK YETKQEFKLL
     KEELIGRINV KTIKEKDNNK IIISYGQDIC YTFKKILNHN INIYIRTPLN CILTTGICQM
     CYGWNLATGK IVELGETIGT IAAQSIGEPG TQLTMRTFHL GGIFTSKIKE SILSPFTGKI
     WYDLNKNGKK TYNKFNEKIF LTSKEKKITI YENNINKSIY YLPPNSYIFV RPGEKVFKAQ
     IIAETFDKQK KKENTKFNEV KKIKSNISGK KYINKKNKKF NNLYWILNAN FITFNKFYHK
     LTDKLNFKKK SYTISKNMQD KNKKSKKNLQ LKISIKNILN NMEKKKSKTN KKFIFINEIL
     NKNKTIILNK PKKEKIINNK WKIGKFILKD EITNKNRNLY PSQIIQEKKD TSVLKKVTPY
     RLNDKILDKN PYIMKKNALL YKAVTKKEKN KDIIQGLVEI EKLFEAKKSF IIDKTKNLHE
     ILKDLFVNYN KKYNNSTSTR KSIEIIQKYI LEEIQSIYKE QGINISNKHI EIIIKQMTSK
     VIIKNAGNSP FIVGEICNIN SIDNLNKNYE HKIIYEPILL GITKSSLYTQ SFISQITFQE
     SIKSLIKAAI ENKIDWLYGL KENLILGNLI PIGTGFK
 
 
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