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Database: UniProt
Entry: A0A369QDC3_9SPHN
LinkDB: A0A369QDC3_9SPHN
Original site: A0A369QDC3_9SPHN 
ID   A0A369QDC3_9SPHN        Unreviewed;      1474 AA.
AC   A0A369QDC3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE            Short=RNAP subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE            EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01322};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
GN   Name=rpoC {ECO:0000256|HAMAP-Rule:MF_01322,
GN   ECO:0000313|EMBL:RDC60919.1};
GN   ORFNames=HME9302_02136 {ECO:0000313|EMBL:RDC60919.1};
OS   Alteripontixanthobacter maritimus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Alteripontixanthobacter.
OX   NCBI_TaxID=2161824 {ECO:0000313|EMBL:RDC60919.1, ECO:0000313|Proteomes:UP000253727};
RN   [1] {ECO:0000313|EMBL:RDC60919.1, ECO:0000313|Proteomes:UP000253727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HME9302 {ECO:0000313|EMBL:RDC60919.1,
RC   ECO:0000313|Proteomes:UP000253727};
RA   Kang H., Kim H., Joh K.;
RT   "Altererythrobacter sp. HME9302 genome sequencing and assembly.";
RL   Submitted (APR-2018) 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_01322, ECO:0000256|RuleBase:RU004279}.
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_01322, ECO:0000256|RuleBase:RU004279};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01322};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01322};
CC   -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC       and 1 omega subunit. When a sigma factor is associated with the core
CC       the holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000256|HAMAP-Rule:MF_01322}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDC60919.1}.
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DR   EMBL; QBKA01000002; RDC60919.1; -; Genomic_DNA.
DR   Proteomes; UP000253727; Unassembled WGS sequence.
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:0000287; F:magnesium ion binding; 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   CDD; cd01609; RNAP_beta'_N; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 1.
DR   Gene3D; 1.10.1790.20; -; 1.
DR   Gene3D; 1.10.40.90; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 2.40.50.100; -; 3.
DR   Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR   Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR   HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   NCBIfam; TIGR02386; rpoC_TIGR; 1.
DR   PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   SMART; SM00663; RPOLA_N; 1.
DR   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_01322};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01322};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01322};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01322}; Reference proteome {ECO:0000313|Proteomes:UP000253727};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01322};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01322};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01322}.
FT   DOMAIN          236..515
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1407..1474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         461
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         463
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         465
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         809
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         883
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         890
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         893
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1474 AA;  162643 MW;  EC65C357809E1D2F CRC64;
     MNELSKFTNQ LAKPETFDQI QIGLASPERI RSWSFGEIKK PETINYRTFK PERDGLFCAR
     IFGPVKDYEC LCGKYKRMKY KGVVCEKCGV EVTVTKVRRE RMGHIELAAP VAHIWFLKSL
     PSRIGLLLDM QLKQLERVLY FESYIVTEPG LTPMEKFQLL TEDELLEAQD EYGEDAFTAG
     IGAEAVKIML MDLDLEQERD DLMEELATTK SKLKPAKIIK RLKVVESFIG SGNRPEWMIL
     EVVPVIPPEL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLIELRAPD IIVRNEKRML
     QEAVDALFDN GRRGRVITGA NKRPLKSLSD MLKGKQGRFR QNLLGKRVDY SGRSVIVTGP
     ELKLHQCGLP KKMALELFKP FIYARLDAKG LSMTLKQAKK WVEKERKEVW DILDEVIREH
     PVMLNRAPTL HRLGIQAFEP VLIEGKAIQL HPLVCSAFNA DFDGDQMAVH VPLSLEAQLE
     ARVLMMSTNN ILSPANGKPI IVPSQDMILG LYYLSMDREG EPGEGMMLAD MAEIHQALHV
     GAVTLHSKIV TRVPQTNDKG KIVMERVETT PGRMLIGECL PKSHKVPYAI INHLLTKKDI
     GDVIDQVYRH TGQKDTVLFA DAIMTLGFTH AFKAGISFGK DDMIIPDSKD GMIDEAKKLV
     ADYEQQYQDG LITQQEKYNK VIDAWSRTGD QVADAMMEEI KARPKDKDGR EAQINSIYMM
     SHSGARGSPA QMKQLAGMRG LMAKPSGEII ETPIISNFKE GLTVLEYFNS THGARKGLAD
     TALKTANSGY LTRRLVDVSQ DCVIVVENCK TNNSLDMRAI VQGGQVIASL GERILGRTVA
     EDIVNAATDE VIVKKGTLID EPMVVEIEAA EVQVAKIRSP LVCEADQGVC GTCYGRDLAR
     GTPVNIGEAV GVIAAQSIGE PGTQLTMRTF HIGGAAQLNE TSHLEAISDG KVEYRDMPTI
     KDKKGRILSM ARNGELAVID AEGREREIHK VPYGTVLLNA DGAKIKEGDR LAEWDPFSLP
     IITEQSGVVR FKDLIDGTTM EERVDDATGI AQRVVTELRA SGRKKGEDLR PRMTLLSEGD
     TDETEETAAA RYMLAPGTTL SVEDGQQVDA GDILARASRE AAKTRDITGG LPRVAELFEA
     RIPKDNAIIA KISGKIEFVR EYKAKRKIAI VPEEGEPVEY LIPKTKIIDV QEGDFVKKGD
     TLISGSPNPH DILDVLGIEA LAEYLVTEIQ EVYRLQGVKI NDKHIETIVR QMLQKVEITN
     GGDTVLLPGE QVDRDEMDEA NAKLTRSKKP AEGKPVLLGI TKASLQTRSF ISAASFQETT
     RVLTQASVEG KKDTLIGLKE NVIVGRLIPA GTGAGMNRMR VTASSRDAAL RAQWKKNQDA
     LLAAETAEEE RKAELAQEAA NVATGNATMG DMVASGDGSD EAAGDYLRED QSVAPEPIAK
     NEQAKEEAAA DEAASAEAPP ADAAPEEPKA DDGE
//
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