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Database: UniProt
Entry: H2Z3P4_CIOSA
LinkDB: H2Z3P4_CIOSA
Original site: H2Z3P4_CIOSA 
ID   H2Z3P4_CIOSA            Unreviewed;      1660 AA.
AC   H2Z3P4;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
OS   Ciona savignyi (Pacific transparent sea squirt).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000012206.1, ECO:0000313|Proteomes:UP000007875};
RN   [1] {ECO:0000313|Proteomes:UP000007875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA   Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA   Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA   Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA   Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA   Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA   Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA   Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA   Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA   Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA   Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA   Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA   Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA   Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA   Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA   Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA   Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA   Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA   Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA   Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA   Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA   Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA   Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA   Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA   Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA   Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA   Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA   Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA   Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA   Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA   Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA   Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA   Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA   Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA   Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAVP00000012206.1}
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|ARBA:ARBA00024550,
CC         ECO:0000256|RuleBase:RU004279};
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR   Ensembl; ENSCSAVT00000012348.1; ENSCSAVP00000012206.1; ENSCSAVG00000007184.1.
DR   GeneTree; ENSGT00920000149138; -.
DR   Proteomes; UP000007875; 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; cd02735; RNAP_I_Rpa1_C; 1.
DR   CDD; cd01435; RNAP_I_RPA1_N; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 1.
DR   Gene3D; 1.10.357.120; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.70.2850; -; 1.
DR   Gene3D; 6.10.250.2940; -; 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; IPR047107; DNA-dir_RNA_pol1_lsu_C.
DR   InterPro; IPR015699; DNA-dir_RNA_pol1_lsu_N.
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:SF11; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA1; 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:UP000007875};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          286..616
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1344..1433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1344..1363
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1364..1381
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1382..1398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1399..1414
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1415..1429
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1660 AA;  186507 MW;  97EEF5211EAFB385 CRC64;
     MMIRQIGKPY KTLSSIKFSC YNADEIRQLS VKRVTNPHSL DALLNPTEGG LYDAAYGASS
     RDELCSTCGK GSVQCTGHMG HIELPLPVYH PLFFKTLIYL LRGSCMKCQK LLIPRQKIFL
     MTMQLQALEK GMVQTAVGIS VYEKSNDDVA TMQEIQEHLE RVLLKHYDDI ANYKIESNAE
     GMKSNHGKLD FLLIVEIYRG LFCALENVMQ TCFKSFLNLF VTLYFFKPDC EEATNGWSRN
     AAELHLTLVS EFIHLLAKPV SRCPHCGKLI NIYLSDNNSD TTSAVDVLFL SVLSVPPSRF
     RPIGCVNDRH FESPQTTSYS KVLMDCAILR ALLKKMKEAD KENQQEDKKM DLLSSIPGKT
     LSEKLENAWH RLQQHINCLM DSDLDRLTVN GGDKIPGIKQ LLEKKDGLFR KHMMGKRVNY
     AARSVISPDP YIATNEIGLP MVFATKLTYP CPVTPWNLKM LRQAVMNGPL KHPGATHVVS
     EGRTVLLSAT DQSQRESVAK QLTASDTHTP KTVLRHIQTG DVMLLNRQPT LHKGSIMAHR
     VRVLPGEKTL RMHYANCKSY NADFDGDEMN AHPQTELCRS EAYQLMSTDR QYLSGKDGKP
     LSCLIQDHMV AGVNISIRGR FFTREQYQQL TYNALMHLPY KVKLLTPAIL KPQPLWSGKQ
     VFSTIFMNIT PNGLPRINLT GKSKIGPKNW QNAPPRNAVV APIDNGDMCE SQVIIRDGEL
     LCGVLDKAHY GATEHGLVHA TYELYSGEIS GRLLTCLARL FTAFLQFYRG FTLGVEDILV
     KDWANKSRTD VVVDTKDNGM AAVAKTLNVK RKENTEATKI TVNKGEDKLA AVDHAMKTVS
     NDVNDKIAKC CTGNGLLKTF PTNNLQLMVI SGAKGGAVNC MQISCLLGQI ELEGRRPPLM
     PSGRSAPSFM PYDTTIRAGG FISQRFLTGI RPQEYFYHCM AGREGLVDTA VKTSRSGYLQ
     RCLIKHLEGL LLSYDMTVRD SDGSVVQFLY GEDGIDINKT SYLNQQQYDF VVKNYDAIAK
     QLPDVDTFES SAYGRSITRK WSKFDKLRKK RNKRLRKTQE GRTSGFLNFS VQCKSGNLPI
     SKIFFNYFQI KNQWMKLDIE GRAKYLDKTS KLRLPDTIIS QYRPDIYFGS TSDHFHDEMK
     KYIKQNPLNL PANDTTNSLP LLKMRYQRSL CQPGESVGLL AAQSIGEPST QMTLNTFHFA
     GRGEMNVTLG IPRLREILMV ASKQIKTPQI TVPVKEGRQK RAKRLCKELT KVLLSQVLHK
     FTVDERLVVG SGDIGDRYRR CVVTIQLLPE RQFGKEMAMS RDTVLRHIEK NFFRALLFAI
     TKQLKKRESE VLQIDQRVAR ETVRRAKNAD GEDASRDAET FEAEKNADDD DVDEEAGFDD
     GDAAAEGQRR KKREEVDYEE QDDELPDEND NSTMIEPDED SRDSAPPMME EQDTEAVKNL
     GHGNISIEDY EFDAASSGWC RVTFLMPLTS VHVDVVSLVR SEACQSAVRQ VPGISRCILV
     PVQGQACVDA GAVNLVTEGI NFYKIFENED SLDVNRLYSN CVHSVAQIYG VEAARRVVVK
     EIANVFAVYG IEVDSRHLSL IGDYMCYEGV YKPFNRLAIA SCVSPLQQMS FETTMKFLNS
     AALHGKLSSL DRLQSPSARI VAGQVVKGGT GNFSLLYPMT
//
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