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