RPOC2_SORBI
ID RPOC2_SORBI Reviewed; 1520 AA.
AC Q01923; A1E9R6;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE Short=RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623;
RX PubMed=17534593; DOI=10.1007/s00122-007-0567-4;
RA Saski C., Lee S.-B., Fjellheim S., Guda C., Jansen R.K., Luo H.,
RA Tomkins J., Rognli O.A., Daniell H., Clarke J.L.;
RT "Complete chloroplast genome sequences of Hordeum vulgare, Sorghum bicolor
RT and Agrostis stolonifera, and comparative analyses with other grass
RT genomes.";
RL Theor. Appl. Genet. 115:571-590(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 409-843.
RC TISSUE=Leaf;
RX PubMed=8437572; DOI=10.1007/bf00277120;
RA Chen Z., Muthukrishnan S., Liang G.H., Schertz K.F., Hart G.E.;
RT "A chloroplast DNA deletion located in RNA polymerase gene rpoC2 in CMS
RT lines of sorghum.";
RL Mol. Gen. Genet. 236:251-259(1993).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01324}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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DR EMBL; EF115542; ABK79488.1; -; Genomic_DNA.
DR EMBL; Z14983; CAA78707.1; -; Genomic_DNA.
DR EMBL; Z14984; CAA78708.1; -; Genomic_DNA.
DR PIR; S30925; S30925.
DR PIR; S30926; S30926.
DR RefSeq; XP_002457875.1; XM_002457830.1.
DR RefSeq; YP_899399.1; NC_008602.1.
DR AlphaFoldDB; Q01923; -.
DR STRING; 4558.Sb03g017630.1; -.
DR EnsemblPlants; EES02995; EES02995; SORBI_3003G169400.
DR GeneID; 4549110; -.
DR GeneID; 8074931; -.
DR Gramene; EES02995; EES02995; SORBI_3003G169400.
DR KEGG; sbi:4549110; -.
DR KEGG; sbi:8074931; -.
DR eggNOG; ENOG502QPYA; Eukaryota.
DR HOGENOM; CLU_000524_1_0_1; -.
DR InParanoid; Q01923; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 731145at2759; -.
DR Proteomes; UP000000768; Chloroplast.
DR ExpressionAtlas; Q01923; baseline.
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; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Plastid; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..1520
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067949"
FT REGION 645..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..775
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT CONFLICT 676..731
FT /note="Missing (in Ref. 2; CAA78708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1520 AA; 175010 MW; EE0CD22633381E07 CRC64;
MAERANLVFH NKEIDGTAMK RLISRLIDHF GMGYTSHILD QIKTLGFHQA TTTSISLGIE
DLLTIPSKGW LVQDAEQQSF LLEKHYYYGA VHAVEKLRQS VEIWYATSEY LKQEMNSNFR
ITDPSNPVYL MSFSGARGNA SQVHQLVGMR GLMADPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTADAG YLTRRLVEVV QHIIVRRRDC GTIQGISVSP QNGMTEKLFV
QTLIGRVLAD DIYIGSRCIA SRNQDIGIGL VNRFITAFRA QPFRAQPIYI RTPFTCRSTS
WICQLCYGRS PTHGDLVELG EAVGIIAGQS IGEPGTQLTL RTFHTGGVFT GGTADLIRSP
SNGKIQFNED LVHPTRTRHG QPAFLCYIDL HVTIQSQDIL HSVNIPLKSL ILVQNDQYVE
SEQVIAEIRA GTSTLHFKEK VQKHIYSESD GEMHWSTDVY HAPEYQYGNL RRLPKTSHLW
ILSVSMCRSS IASFSLHKDQ DQMNTYSFSV DGRYIFDFSM ANDQVSHRLL DTFGKKDREI
LDYLTPDRIV SNGHWNCFYP SILQDNSDLL AKKRRNRFAV PLQYHQEQEK ERISCLGISM
EIPFMGVLRR NTIFAYFDDP RYRKDKRGSG IVKFRYRTLE EEYRTREEEY RTREEDSEDE
YESPENKYRT REGEGEYEIL EDEYRTLEDE YETLEDEYGI LEDEYRTLEK DSEEEYGSLE
NKYRTREGEG EYEILEEDSE EEYGSSEDGS EKEYGTLEED SEEDSEEDSE DEYGSPEEDS
ILKKEGFIEH RGTKEFSLKY QKEVDRFFFI LQELHILPRS SSLKVLDNSI IGVDTQLTKN
TRSRLGGLVR VKRKKSHTEL KIFSGDIHFP EEADKILGGS LIPPEREKKD SKESKKRKNW
VYVQRKKILK SKEKYFVSVR PAVSYEMDEG RNLATLFPQD LLQEEDNLQL RLVNFISHEN
SKLTQRIYHT NSQFVRTCLV VNWEQEVKEG ARASLVEVRT NDLIRDFLRI ELVKSTISYT
RRRYDRTSVG LIPNNRLDRN NTNSFYSKAK IQSLSQHQEV IGTLLNRNKE YPSLMILLAS
NCSRIGLFKN SKYPNAVKES NPRIPIRDVF GLLGVIVPSI SNFSSSYYLL THNQILLKKY
LFLDNLKQTF QVLQGLKYSL IDENQRISNF GSNIMLEPFH LNWHFLHHDS WEETLAIIHL
GQFICENLCL FKSHIKKSGQ IFIVNMDSFV LRAAKPYLAT IGATVHGHYG KILYKGDRLV
TFIYEKSRSS DITQGLPKVE QIFEARSIDS LSPNLERRIE DWNERIPRIL GVPWGFLIGA
ELTIAQSRIS LVNKIQKVYR SQGVQIHNRH IEIIIRQVTS KVRVSEDGMS NVFLPGELIG
LLRAERAGRA LDESIYYRAI LLGITRASLN TQSFISEASF QETARVLAKA ALRGRIDWLK
GLKENVVLGG IIPVGTGFQK FVHRSPQDKN LYFEIKKKNL FASEMRDILF LHTELVSSDS
DVTNNFYETS ETPFTPIYTI
