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Database: UniProt
Entry: H9LIB3_GOSHI
LinkDB: H9LIB3_GOSHI
Original site: H9LIB3_GOSHI 
ID   H9LIB3_GOSHI            Unreviewed;      1393 AA.
AC   H9LIB3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
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:AEB90586.1, ECO:0000313|RefSeq:YP_538925.1};
GN   ORFNames=GohiCp011 {ECO:0000313|RefSeq:YP_538925.1}, GopuCp011
GN   {ECO:0000313|EMBL:AEB90586.1};
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AEB90586.1,
OG   ECO:0000313|RefSeq:YP_538925.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635 {ECO:0000313|EMBL:AEB90586.1};
RN   [1] {ECO:0000313|RefSeq:YP_538925.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16553962; DOI=10.1186/1471-2164-7-61;
RA   Lee S.B., Kaittanis C., Jansen R.K., Hostetler J.B., Tallon L.J.,
RA   Town C.D., Daniell H.;
RT   "The complete chloroplast genome sequence of Gossypium hirsutum:
RT   organization and phylogenetic relationships to other angiosperms.";
RL   BMC Genomics 7:61-61(2006).
RN   [2] {ECO:0000313|RefSeq:YP_538925.1}
RP   NUCLEOTIDE SEQUENCE.
RG   NCBI Genome Project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AEB90586.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22876273; DOI=10.1371/journal.pone.0037128;
RA   Xu Q., Xiong G., Li P., He F., Huang Y., Wang K., Li Z., Hua J.;
RT   "Analysis of complete nucleotide sequences of 12 gossypium chloroplast
RT   genomes: origin and evolution of allotetraploids.";
RL   PLoS ONE 7:E37128-E37128(2012).
RN   [4] {ECO:0000313|Proteomes:UP000189702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX   PubMed=25893780; DOI=10.1038/nbt.3208;
RA   Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA   Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA   Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA   Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA   Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT   "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT   provides insights into genome evolution.";
RL   Nat. Biotechnol. 33:524-530(2015).
RN   [5] {ECO:0000313|RefSeq:YP_538925.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (MAR-2017) to UniProtKB.
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|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; HQ901197; AEB90586.1; -; Genomic_DNA.
DR   RefSeq; YP_538925.1; NC_007944.1.
DR   SMR; H9LIB3; -.
DR   STRING; 3635.H9LIB3; -.
DR   PaxDb; 3635-H9LIB3; -.
DR   GeneID; 3989195; -.
DR   KEGG; ghi:3989195; -.
DR   OrthoDB; 806648at2759; -.
DR   Proteomes; UP000189702; Chloroplast Pltd.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   CDD; cd02655; RNAP_beta'_C; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 1.
DR   Gene3D; 1.10.1790.20; -; 1.
DR   Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR   HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR   InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
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   NCBIfam; TIGR02388; rpoC2_cyan; 1.
DR   PANTHER; PTHR48355; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR   PANTHER; PTHR48355:SF1; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000313|EMBL:AEB90586.1, ECO:0000313|RefSeq:YP_538925.1};
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};
KW   Plastid {ECO:0000313|EMBL:AEB90586.1, ECO:0000313|RefSeq:YP_538925.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189702};
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          93..157
FT                   /note="RNA polymerase Rpb1"
FT                   /evidence="ECO:0000259|Pfam:PF05000"
FT   DOMAIN          172..365
FT                   /note="RNA polymerase Rpb1"
FT                   /evidence="ECO:0000259|Pfam:PF04998"
FT   DOMAIN          1196..1281
FT                   /note="RNA polymerase Rpb1"
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         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1393 AA;  158638 MW;  5AFD403BADE21F47 CRC64;
     MAERANLVFH NKVIDGTAIK RLISRLIDHF GMAYTSHILD QVKALGFQQA TATSISLGID
     DLLTIPSKGW LVQDAEQQSL ILEKHHHFGN VHAVEKLRQS IEIWYATSEY LRQEMNPNFR
     MTDPFNPVHI MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
     SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRRTDC GTTRGISVSP QKRTLPERIF
     IQTLIGRVLA DDIYMGPRCI AIRNQDIGLG LVDRFRAFRT QPISIRTPFT CRSTSWICRL
     CYGRSPTHGD LVELGEAVGI IAGQSIGEPG TQLTLRTFHT GGVFTGGTAE HVRAPFNGKI
     KFNEDLVHPT RTRHGHPAFL CYRDLYVIIE SEDIIHKVAI PPKSFLLVQN DQYVESEQVI
     AEIRAGTYTL NLKERVRKHI YSDSEGEMHW STDVYHSPEF TYSNVHLLPK TSHLWILSGG
     SYKFSVVPFS LHKDQDQISI HYLSAERRYI SRFSVNNDQV RHNLFSSDFS DKKEERIYDY
     SELNRIIGTG HCDFIYSAIL HENADLLAKR RRNRFIIPFQ LIQDQEKELM LHSHSGISME
     IPINGIFRRK SILAFFDDPR YRRKSSGITK YGTLGAHSIV KREDVIEYRG VKKVKPKYQM
     KVDRFFFIPE EVHILSESSS IMVRNNSIIG VDTPITLNTR SQVGGLVRVE RKKKRIELKI
     FSGNIYFPGE RDKISRHSGI LIPPGTGKTN SKESKKLKNW IYVQRITPTK KKYFVLVRPV
     TPYEIPDGLN LATLFPQDPF QEKDNMQLRA VNYILYGNGK PTRRISDTSI QLVRTCLVLS
     WDQDNKSSFA EEVCASFVEV RTNGLIRDFL RIDLVKSHIF YIRKRNDPSG SELISDNRSD
     RTNKNPFYSI YSNARIQQSF SQNHGTIHTL LNRNKESQSL IILSASNCFR MGPFNDVKYH
     NVIKQSIKKD PLIPIKNLLG PLGTAPKIAN FYSSFYPLIT HNQTSVAKYF ELDNLKQAFQ
     VLNYYLIAEN GRIYNFDPCR NIFLNAVNLN WYFPHHHYHH NYCEETSTII SLGQFICENV
     CIAKSGPRLK SGQVFIVQAD SIVIRSAKPY LATPGATVHG HYGETLYEGD TLVTFIYEKS
     RSGDITQGLP KVEQVLEVRS IDSISMNLEK RIEGWNECIT RILGIPWGFV IGAELTIVQS
     RLSLVNKIQK VYRSQGVQIH NRHIEIIVRQ ITSKVLVSED GMSNVFLPGE LIGLLRAERT
     GRALEEAICY RAVLLGITRA SLNTQSFISE ASFQETARVL AKAALRGRID WLKGLKENVV
     LGGMIPAGTG FKGLVHRSRQ HNNILLETKK KNFFGGEMRD IFFHHRELFD SCISNNLHDT
     SGRSFIGIEF NDS
//
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