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Database: UniProt
Entry: E6ZHI0_DICLA
LinkDB: E6ZHI0_DICLA
Original site: E6ZHI0_DICLA 
ID   E6ZHI0_DICLA            Unreviewed;      1390 AA.
AC   E6ZHI0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   Name=POLR3A {ECO:0000313|EMBL:CBN81514.1};
GN   ORFNames=DLA_Ib03560 {ECO:0000313|EMBL:CBN81514.1};
OS   Dicentrarchus labrax (European seabass) (Morone labrax).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Moronidae; Dicentrarchus.
OX   NCBI_TaxID=13489 {ECO:0000313|EMBL:CBN81514.1};
RN   [1] {ECO:0000313|EMBL:CBN81514.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kuhl H., Tine M., Hecht J., Knaust F., Reinhardt R.;
RT   "Analysis of single nucleotide polymorphisms in three chromosomes of
RT   European sea bass Dicentrarchus labrax.";
RL   Comp. Biochem. Physiol. Part D Genomics Proteomics 6:70-75(2011).
RN   [2] {ECO:0000313|EMBL:CBN81514.1}
RP   NUCLEOTIDE SEQUENCE.
RX   DOI=10.1016/j.ygeno.2011.06.004;
RA   Kuhl H., Tine M., Beck A., Timmermann B., Kodira C., Reinhardt R.;
RT   "Directed sequencing and annotation of three Dicentrarchus labrax L.
RT   chromosomes by applying Sanger- and pyrosequencing technologies on pooled
RT   DNA of comparatively mapped BAC clones.";
RL   Genomics 0:0-0(2011).
RN   [3] {ECO:0000313|EMBL:CBN81514.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tine M., Kuhl H., Beck A., Bargelloni L., Reinhardt R.;
RT   "Comparative analysis of intronless genes in teleost fish genomes: Insights
RT   into their evolution and molecular function.";
RL   Mar. Genomics 4:109-119(2011).
RN   [4] {ECO:0000313|Ensembl:ENSDLAP00005046691.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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|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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR   EMBL; FQ310507; CBN81514.1; -; Genomic_DNA.
DR   Ensembl; ENSDLAT00005049813.2; ENSDLAP00005046691.1; ENSDLAG00005020605.2.
DR   GeneTree; ENSGT00930000151028; -.
DR   Proteomes; UP000694389; Unassembled WGS sequence.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0031981; C:nuclear lumen; IEA:UniProt.
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:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd02736; RNAP_III_Rpc1_C; 1.
DR   CDD; cd02583; RNAP_III_RPC1_N; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 6.10.250.2940; -; 1.
DR   Gene3D; 6.20.50.80; -; 1.
DR   Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
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   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; IPR035698; RNAP_III_Rpc1_C.
DR   InterPro; IPR035697; RNAP_III_RPC1_N.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF32; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1; 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|RuleBase:RU004279};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694389};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          248..553
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
SQ   SEQUENCE   1390 AA;  155823 MW;  89ACE7890CAECD44 CRC64;
     MVKEQFRETD VAKKISHICF GMKSAEQMRQ QAHIQVVSKN LYSQDTKHTP LSYGVLDHRM
     GTSEKDRPCL TCGKNLADCL GHYGYLDLEL PCFHVGYFKA IIGILQMICK TCSSIMLTKE
     DKLQFMDHLK RPNLAYLQKR GLKKKISDKC RKRTICLNCS AFNGPVKKCG LLKIIHEKYK
     TTKKVVDPFV SDFMQSFDIA IEHNKMVEPL LTRAQENLNP LVVLNMFKRI PQEDIPLLLM
     NPEAGKPADL ILTRLLVPPL CIRPSVVSDL KSGTNEDDLT MKLTEIIFLN DVIKKHRMTG
     AKTQMIMEDW DFLQLQCALY INSELSGIPL NMAPKKWTRG FVQRLKGKQG RFRGNLSGKR
     VDFSGRTVIS PDPNLRIDEV AVPVHVAKIL TYPERVNKAN LELMRKLVRN GPEVHPGANF
     IQNRHTQMKR FLKYGNREKI AQELRFGDVV ERHLIDGDIV LFNRQPSLHK LSIMAHIAKV
     KPHRTFRFNE CVCTPYNADF DGDEMNLHLP QTEEAKAEAL VLMGTKANLV TPRNGEPLIA
     AIQDFLTGAY LLTLKDTFFD RSKACQIVAS ILVGKDEKIR VTLPRPAIMK PMALWTGKQI
     FSVILKPSKE CPVKANLRTK GKQYCGKGED LCYNDSFVVI HNSELMCGSL DKGTLGSGSK
     NNIFYILLRD WGQLEAANAM SRLARLAPVF LSNRGFSIGI GDVTPGQGLL KAKHDLLDDG
     YKKCDEYIEA LKTGKLQQQP GCTAEETLEA LILRELSVIR DRAGSACLRE LDKSNSPLIM
     ALCGSKGSFI NISQMIACVG QQAISGSRVP DGFENRSLPH FEKHSKLPAA KGFVADSFYS
     GLTPTEFFFH TMAGREGLVD TAVKTAETGY MQRRLVKSLE DLCSQYDLTV RSSTGDIIQF
     IYGGDGLDPA DMEGKDEPLE FKRVLDNIRA VYTCPYEPAL SQNELVLTAD AIMKRADFLC
     CRDSFLEEIK KFIKSVSERI KKTRDKYGIN DNGTSEPKVL YQLDRITPTQ LEKYLETCRD
     KYMRAQMEPG SAVGALCAQS IGEPGTQMTL KTFHFAGVAS MNITLGVPRI KEIINASKNI
     STPIITANLD VEDDADFARL VKGRIEKTLL GEISEYIEEV FLPDDCFILV KLSLERIRLL
     RLEVNAETVR YSICMSKLRV KPGDIAVHGE AVVCVSPREN SKSSMYYVLQ SLKEELPKVV
     VQGIPEVARA VIHIDEQSGK NKYKLLVEGD NLRAVMATHG VNGSRTTSNN TYEVEKTLGI
     EAARSTIINE IQYTMVNHGM SIDRRHVMLL ADLMSYKGEI LGITRFGLAK MKESVLMLAS
     FEKTADHLFD AAYFGQKDSV CGVSECIIMG IPMNIGTGLF KLLHKADKDP SPVKRPLLFD
     NADFHIPLIT
//
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