ID   A0A5Q2MMF6_9MAGN        Unreviewed;      1385 AA.
AC   A0A5Q2MMF6;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE            EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01324};
DE   AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01324};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE            Short=RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
GN   Name=rpoC2 {ECO:0000256|HAMAP-Rule:MF_01324,
GN   ECO:0000313|EMBL:QGG43788.1};
GN   ORFNames=LiagCp011 {ECO:0000313|EMBL:QGG43788.1};
OS   Lindera aggregata.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:QGG43788.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Lindera.
OX   NCBI_TaxID=545644 {ECO:0000313|EMBL:QGG43788.1};
RN   [1] {ECO:0000313|EMBL:QGG43788.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Jo S., Kim Y.-K., Cheon S.-H., Fan Q., Kim K.-J.;
RT   "Characterization of 20 complete plastomes from the tribe Laureae
RT   (Lauraceae) and distribution of small inversions.";
RL   PLoS ONE 14:0-e0224622(2019).
RN   [2] {ECO:0000313|EMBL:QXP99429.1}
RP   NUCLEOTIDE SEQUENCE.
RA   yuan x.L.;
RT   "The complete chloroplast genome of Lindera aggregate (Sims) Kosterm.";
RL   Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000256|HAMAP-Rule:MF_01324}.
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|HAMAP-Rule:MF_01324};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01324};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01324};
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.
CC       {ECO:0000256|HAMAP-Rule:MF_01324}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_01324}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01324}.
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DR   EMBL; MG581437; QGG43788.1; -; Genomic_DNA.
DR   EMBL; MZ027676; QXP99429.1; -; Genomic_DNA.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 1.
DR   HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR   InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
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; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR   TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000313|EMBL:QGG43788.1};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_01324};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01324};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01324}; Plastid {ECO:0000313|EMBL:QGG43788.1};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01324};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01324};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01324}.
FT   DOMAIN          95..157
FT                   /note="RNA_pol_Rpb1_4"
FT                   /evidence="ECO:0000259|Pfam:PF05000"
FT   DOMAIN          172..364
FT                   /note="RNA_pol_Rpb1_5"
FT                   /evidence="ECO:0000259|Pfam:PF04998"
FT   DOMAIN          1184..1271
FT                   /note="RNA_pol_Rpb1_5"
FT                   /evidence="ECO:0000259|Pfam:PF04998"
FT   BINDING         220
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT   BINDING         290
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT   BINDING         297
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1385 AA;  157388 MW;  3F1C4F49E29B0DF2 CRC64;
     MAEWADLFFY NKAIDGSAMK RLISRLIDHF GMAYTSHTLD QVKTLGFQQA TATSISLGID
     DLLTVPSKGW LVQDAEQQSF ILEKHHHYGN VHTVEKLRQS IEIWYATSEY LRQEMHPNFR
     MTDPSNSVHI MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
     SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRRTDC GTTRGISVSP RNGMTERIWV
     QTLIGRVLAY NIYMGPRCIA AQNKDIGVGL VTRFITFRTQ PIYIRTPFLC RSISWICRLC
     YGQSPTHGDL VELGEAVGII AGQSIGEPGT QLTLRTFHTG GVFTGGTAEH VRAPFKGKIK
     FNEDLVHPTR TRHGHPAFLC YIDLYVTIES HDILHNVNIP PKSFLLVQND QYVESEQVIA
     EIRAGTSTFN FNKVKEKVRK HIYSDSEGEM HWSTDVYHAP EYKYGNVHLL PKTSHLWILS
     GALCRSSIVP FSLHKDQDQM NVHSVERRSI SDLSVTNDQV RHKLFSSNPY GKKGGVLDYS
     GPDRIISNGH WNFIYPPILH ENSDLLAKRR RNRFIIPFQS DQEREKELMP RSGISIEIPI
     NGVLPRNSIL AYFDDPLYRR SSSGITKYGT IGVGSIVKKE DLIEYRRAKE FRPKYQMKVD
     RFFFIPEEVH ILPGSSPIMV RNNSIIGVDT RIALNTRSQV GGLVRVERKK KRIELKIFSG
     DIYFPGATDK ISRHCGILIP PGTGKKNSKE SKKWKNWIYV QRITPTKKKY FVSVRPVVTY
     EIADGINLAT LFPQDPLQER DNVQLRIVNY ILYGNGKPIR GIYHTSLQLV RTCLVLNWNQ
     DRDGSIEEVH ASFVEVRAND LIRDFIRIDL VKSSIFYIGK RNDMASSGLI ANNGSDRTNI
     NPFYFKARIQ SFTQHQGTIR TLLNRNKECP SFLILLSSDC SRIGLFNGSK SHKELIKLIK
     EDPAIPIRNS LGPLGVVPKI TNFYSFYYFY LITHNQILLK KYFLLDNFKH TFQGLKYYLM
     DENGRIYNPD SCSNIIFNPF DLNWCFLPHD YCEETSTIIS LGQFICENVC ISKCGPHIKS
     SQVLIVHVDS LVIRSAKPHL ATPGATVHGH CGEILYEGDT LVTFIYEKSR SGDITQGLPK
     VEQVLEARSI DSISMNLEKR VEGWNERITR ILGIPWGFLI GAELTIAQSR ISLVNKIQKV
     YRSQGVQIHN RHIEIIVRQI TSKVLVSEDG MSNVFSPGEL IGLLRAERTG RALEEAICYR
     AILLGITRAS LNTQSFISEA SFQETARVLA KAALRGRIDW LKGLKENVVL GGMMPVGTGF
     KGLVHRSRQH SNIPLEIKKK NLFEEEMRDL LFHHRELFGS CIPNNFPDTS ERSFTGFNDR
     FILFF
//