ID F7XYL4_TREPP Unreviewed; 1343 AA.
AC F7XYL4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=rpoC {ECO:0000313|EMBL:AEI75190.1};
GN OrderedLocusNames=TPPCIT_134 {ECO:0000313|EMBL:AEI75190.1};
OS Tremblaya princeps (strain PCIT).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Tremblaya.
OX NCBI_TaxID=891398 {ECO:0000313|EMBL:AEI75190.1, ECO:0000313|Proteomes:UP000000505};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCIT;
RA McCutcheon J.P., von Dohlen C.D.;
RT "An interdependent metabolic patchwork in the nested three-way symbiosis of
RT mealybugs.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEI75190.1, ECO:0000313|Proteomes:UP000000505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCIT {ECO:0000313|EMBL:AEI75190.1,
RC ECO:0000313|Proteomes:UP000000505};
RX PubMed=21835622; DOI=10.1016/j.cub.2011.06.051;
RA McCutcheon J.P., von Dohlen C.D.;
RT "An interdependent metabolic patchwork in the nested symbiosis of
RT mealybugs.";
RL Curr. Biol. 21:1366-1372(2011).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {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|RuleBase:RU004279};
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|RuleBase:RU004279}.
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DR EMBL; CP002244; AEI75190.1; -; Genomic_DNA.
DR KEGG; tpn:TPPCIT_134; -.
DR HOGENOM; CLU_000524_3_1_4; -.
DR Proteomes; UP000000505; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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:DNA-templated transcription; IEA:InterPro.
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; 2.40.40.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 2.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
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 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; 2.
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|RuleBase:RU004279};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 238..513
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1263..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1343 AA; 144759 MW; 4EADF71CDC54302B CRC64;
MNVAERFVLG SLRGAMCTPF DRVKVCMASP LQIRSWSHGE VLTAATVNQR SMIPEAHGLF
CTEIFGTAMA HECMCGRYAG AQHSGIICEC CGVEIGPSYA RRLRMGHIEL ASPVLHAWFS
RPSSPHVGTI LGVPHRDVVR VARRQACLIR PPGATLCRDL TMASMEDLIA RPVGMQQGRA
FSGCDGLRRL LASISMEREV HDTTARIASP RVTDSQRGSM ISRLRMLSSL LEFGARPEWM
ILTVIPVLPA GLRPMIRSAG RDAASSDLND LYRGVINGNN RLRRLMALRA PQSIVAAEHD
LLQRSVDDLI DGTARQGNAR SHCRPRSLSE ALRGKTGRFR QHMLGKRVDY SGRSVIVVGP
DLGMHQCGIP ICMALELYRP FVAGALIRGG MAAQRARAEV SAGSTAAVGA LRHAIRHHPV
LLNRAPTLHR LSLQAFYPTL VEGLAIRLNP LVCAPFNADF DGDQMAVHLP LSIEAQTEAR
MLLLPSNNLL LPASGYPASA PSQDMVLGIY YMTCGPEDGY HGELGIAASA ALQMESGWSR
SHSRAMVVVR ESLRHRGSYS EFSVLHNTTV GRALLSHALP AGTPFHKVNR TISKVVLVEV
MNETARRCGP LYLKGMAESL MVAGFNAATR AGISLCIDDM CTPVSKAVTI AGAWRMSSRL
HRSHKSGVLT GTRLGHATTR LWQETSELVS CMLALELARQ SSSTLAATNA VHLMSASGSR
GSTEQVKQLS GMRGLMVRPD GTILGTPVTS SFRDGLKAVE YAMSAHGARK GLADTALRTA
DSGYLTRRLV DASHDVIITE LDCGTCAGVT VARPQLNSTA VDRALAWCIG RYTASDVEYD
VGGVLYQRNT PITRDVLEDS LLRSVAGINI RSPLHCESQH GVCAMCYGQD LCTLSRVNMG
AAVGVVAAQS IGEPGTQLTM RTFHIGGIAS SRSHDVIACQ PGVVRYSPCT HRVTPDGVRV
AASHNGSVQI HDWRGCSRES HAIPHGSILH RAEGDIVAAG EVLISWDAVT TPVLAKHDSL
ATMFAEGIRL TRSDGRCCTV MLSAGAEVAI GATQYVRRGQ VIATEPAHAE GNTDITGGLA
SMASLFEARQ AQRRHNAPDA SCWLQGILRR KGPTALLQRM QDDVQAILEP QGVRVNNKHL
EIIARQMLRC VRVVHPGDSS FHEGEHVARS EAARANAALR LQNRRTAAYE HTLLGITKSA
LSTESFISAA SFQETTRVIA TAAAFGRRDL LRGLKENVIV GRMIPAGTGL VYHAHRRLNA
DAEPASKAGE EEVRSQEQEP CTQRLSTASR GMHESLHHDA KEAKLSAPKG SKGKAVKPSG
SHILHRRRGA QSTGACNGAG ARR
//
