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Database: UniProt
Entry: H3D6J3_TETNG
LinkDB: H3D6J3_TETNG
Original site: H3D6J3_TETNG 
ID   H3D6J3_TETNG            Unreviewed;      1391 AA.
AC   H3D6J3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, 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};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000016133.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000016133.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   STRING; 99883.ENSTNIP00000016133; -.
DR   Ensembl; ENSTNIT00000016344.1; ENSTNIP00000016133.1; ENSTNIG00000013151.1.
DR   GeneTree; ENSGT00930000151028; -.
DR   HOGENOM; CLU_000487_3_0_1; -.
DR   InParanoid; H3D6J3; -.
DR   OMA; AVCPPYN; -.
DR   TreeFam; TF103054; -.
DR   Proteomes; UP000007303; 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:UP000007303};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          250..555
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
SQ   SEQUENCE   1391 AA;  155803 MW;  8B712CE8C587A066 CRC64;
     MVKEQFRETD VAQKISHICF GMKSAEQMRQ QAHIQVVSKN LYSQDTAHTP LAYGVLDHRM
     GTSEKDRPCL TCGKTLADCL GHYGYLDLEL PCFHIGYFKA IIGILQMICK TCSSIMLTKE
     EKLQFMDQLK RPTLTYLHKR GLKKKISEKC RKRTICLNCS AFNALGPVKK CGLLKIIHEK
     YKTTKKVVDP FVSEFLQSFD IAIEHNKVLE PLLSRAQENL NPLVVLNLFK RISREDIPLL
     LMNPEAGIPA DLILTRLLVP PLCIRPSVVS DLKSGTNEDD LTMKLTEIIF LNDVIKKHRM
     TGAKTQMIME DWDFLQLQCA LYINSELSGI PLNMAPKKWT RGFVQRLKGK QGRFRGNLSG
     KRVDFSGRTV ISPDPNLRID EVAVPVHVAK ILTYPERVNK ANLELMRKLV RNGPEVHPGA
     NFIQNRYNQI KRFLKYGNRE KIAQELRYGD IVERHMIDGD IVLFNRQPSL HKLSIMAHIA
     RVKPHRTFRF NECVCTPYNA DFDGDEMNLH LPQTEEAKAE ALILMGTKAN LVTPRNGEPL
     IAAIQDFLTG AYLLTLKDTF FDRSKACQIV ASILVGKDEK VRISFPRPAI MKPMALWTGK
     QIFSVILKPS KDCPVNANLK TKGKQYCGKG EDLCHNDSFV VIHNSELMCG SMDKGTLGSG
     SKNNIFYILL RDWGQLEAAN AMSRLARLAP VYLSNRGFSI GIGDVTPGQG LLKAKHDLLD
     DGYTKCDEYI EALQTGKLQQ QPGCTAEETL EALILRELSV IRDRAGSACL RELDKSNSPL
     TMALCGSKGS FINISQMIAC VGQQAISGSR VPDGFENRSL PHFEKHSKLP AAKGFVANSF
     YSGLTPTEFF FHTMAGREGL VDTAVKTAET GYMQRRLVKS LEDLCSQYDL TVRSSTGDII
     QFIYGGDGLD PAAMEGKDEP LEFKRVLDNI RAVYACSDEP ALSQNELVLT ADAIMKRTDF
     LCCRDSFLEE IKKFVKSFSE RIKKTRDKYG INDNGTSEPK VLYQLDRITP TQLEKFLETC
     RDKYMRAQME PGSAVGALCA QSIGEPGTQM TLKTFHFAGV ASMNITLGVP RIKEIINASK
     NISTPIITAH LDVEDDADFA RLVKGRIEKT LLGEISEYIE EVFLPDDCFI LVKLSLERIR
     LLRLEVNAET VRYSICMSKL RVKPGDAVHG EAVVCVSPRE NSKSSMYYVL QSLKEELPKV
     VVQGIPEVSR AVIHIDEQSG RNKYKLLVEG DNMRAVMATH GVKGSRTTSN NTYEVEKTLG
     IEAARSTIIN EIQYTMVNHG MSIDRRHVML LADLMSYKGE ILGITRFGLA KMKESVLMLA
     SFEKTADHLF DAAYFGQKDS VCGVSECIIM GIPMNIGTGL FKLLHKADKD PSPAKRPLLF
     DNAAFHIPLN T
//
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