ID   RPA2_DANRE              Reviewed;        1132 AA.
AC   B8JKD7;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=DNA-directed RNA polymerase I subunit RPA2;
DE            Short=RNA polymerase I subunit 2;
DE            EC=2.7.7.6 {ECO:0000250|UniProtKB:Q9H9Y6};
GN   Name=polr1b {ECO:0000312|ZFIN:ZDB-GENE-040426-1598};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=31649276; DOI=10.1038/s41436-019-0669-9;
RA   Sanchez E., Laplace-Builhe B., Mau-Them F.T., Richard E., Goldenberg A.,
RA   Toler T.L., Guignard T., Gatinois V., Vincent M., Blanchet C., Boland A.,
RA   Bihoreau M.T., Deleuze J.F., Olaso R., Nephi W., Luedecke H.J.,
RA   Verheij J.B.G.M., Moreau-Lenoir F., Denoyelle F., Riviere J.B.,
RA   Laplanche J.L., Willing M., Captier G., Apparailly F., Wieczorek D.,
RA   Collet C., Djouad F., Genevieve D.;
RT   "POLR1B and neural crest cell anomalies in Treacher Collins syndrome type
RT   4.";
RL   Genet. Med. 22:547-556(2020).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Second largest core component of RNA polymerase I which synthesizes
CC       ribosomal RNA precursors. Proposed to contribute to the polymerase
CC       catalytic activity and forms the polymerase active center together with
CC       the largest subunit. Pol I is composed of mobile elements and RPA2 is
CC       part of the core element with the central large cleft and probably a
CC       clamp element that moves to open and close the cleft.
CC       {ECO:0000250|UniProtKB:Q9H9Y6}.
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:0000250|UniProtKB:Q9H9Y6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249;
CC         Evidence={ECO:0000250|UniProtKB:Q9H9Y6};
CC   -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC       of at least 13 subunits. {ECO:0000250|UniProtKB:Q9H9Y6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q9H9Y6}. Chromosome
CC       {ECO:0000250|UniProtKB:P70700}.
CC   -!- DISRUPTION PHENOTYPE: Knockdown of the gene by morpholino antisense
CC       oligomer reduces neural crest cell migration and causes severe
CC       craniofacial defects. {ECO:0000269|PubMed:31649276}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000305}.
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DR   EMBL; CT583720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU137726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; B8JKD7; -.
DR   SMR; B8JKD7; -.
DR   STRING; 7955.ENSDARP00000100185; -.
DR   PaxDb; B8JKD7; -.
DR   PeptideAtlas; B8JKD7; -.
DR   Ensembl; ENSDART00000114741; ENSDARP00000100185; ENSDARG00000077469.
DR   Ensembl; ENSDART00000169546; ENSDARP00000133883; ENSDARG00000115880.
DR   ZFIN; ZDB-GENE-040426-1598; polr1b.
DR   eggNOG; KOG0216; Eukaryota.
DR   GeneTree; ENSGT00950000183132; -.
DR   HOGENOM; CLU_000524_5_1_1; -.
DR   InParanoid; B8JKD7; -.
DR   OMA; FFGVVHY; -.
DR   PhylomeDB; B8JKD7; -.
DR   TreeFam; TF103055; -.
DR   Reactome; R-DRE-5250924; B-WICH complex positively regulates rRNA expression.
DR   Reactome; R-DRE-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-DRE-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-DRE-73863; RNA Polymerase I Transcription Termination.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 13.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0001054; F:RNA polymerase I activity; IMP:ZFIN.
DR   GO; GO:0001755; P:neural crest cell migration; IMP:ZFIN.
DR   GO; GO:0014029; P:neural crest formation; IMP:UniProtKB.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.40.270.10; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR   InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR   InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR   InterPro; IPR007121; RNA_pol_bsu_CS.
DR   InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR   InterPro; IPR007642; RNA_pol_Rpb2_2.
DR   InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR   InterPro; IPR007645; RNA_pol_Rpb2_3.
DR   InterPro; IPR007641; RNA_pol_Rpb2_7.
DR   InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR   InterPro; IPR009674; Rpa2_dom_4.
DR   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF06883; RNA_pol_Rpa2_4; 1.
DR   Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR   Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR   Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   Chromosome; DNA-directed RNA polymerase; Metal-binding;
KW   Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1132
FT                   /note="DNA-directed RNA polymerase I subunit RPA2"
FT                   /id="PRO_0000452843"
FT   ZN_FING         1067..1098
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250|UniProtKB:P22138"
SQ   SEQUENCE   1132 AA;  127612 MW;  A329BA318FA2AA93 CRC64;
     MDLSKWCNLK TEPSLKHLTE AGFGVPKEKQ SVPVQELVKA HIESFDQAVT DGLCRVVEAI
     PPMEFLYKGD RISLSFVEAI IHTPSVSKGG ISRDLRVFPA ECRGRRCTYR AKLVADVSWS
     VNGVPKGIIK QSLGQMPIMV KSKLCNLHGL SPKELLEHHE EAEEMGGYFI VNGIEKVIRL
     LIMPRRNYPI AVSRPKFKSR GQGYTQYAIS MRCVKEEHTA INMNLHYLDN GTVMVNFIYR
     KELFFLPLGF ALKALVDYSD YQIYQELIKG REDNSFYKSC VSEMLRIVMD QGCTTKIKVL
     NYLGERFRVK LNLPEWFTHE QCAHFLLDEC LCIHLKTDVE KFYMLCLMTR KLFSFAKQEC
     MEENPDSPMF HEVLTPGQLY LMFLKEKMEG WLVSVKLALE KKPQRVGGLT PDSMTKLFNM
     GTDLTKAFEY LLATGNLMSK TGLGMLQNSG LCVVADKLNF IRYLSHFRCV HRGAAFAKMR
     TTTVRKLLPE SWGFLCPVHT PDGEPCGLMN HMTAHCEIVA PVYPTSTLPG LLCSLGVNAA
     DGNPGQAYSD CYPVILDGAM IGWVEKEVAP SVIESLRRFK VLGEKKVPPW TEIVLVPQTG
     KASLYPGLYL FTTPCRMVRT VRNLSLGKQE LIGIFEQVYL NVGIFEKEIE DGVTTHQELF
     PHSMLSVVAE FIPFSDHNQS PRNMYQCQMS KQTMGFPLHS YQYRSDNKLY RLQTPQSPLV
     RPAMYDHYDV DNYPIGTNAI VAVISYTGYD MEDAMIVNKS SWERGFAHGS VYKTEIIDLS
     EKVKGDDSIV FGVKPGDPKV MGKLDADGLP FIGSVLKYGD PFYGYISLNT GQSHVYFYKY
     QESCVVDNIK VCSNETGTGR FKRICVTSRV PRNPTIGDKF ASRHGQKGIL SRLWPAEDMP
     FTESGMSPDI LFNPHGFPSR MTIGMLIESM AGKSASLHGL CHDATPFTFS EENSALEHFG
     ELLKAAGYNY YGTERLYSGL SGLELEADIF IGVVYYQRLR HMVSDKFQVR TTGARDKVTN
     QPMGGRNVQG GIRFGEMERD ALLAHGTSFL LHDRLFNCSD RSVAQVCMDC GSLLSPLLEK
     PPPNWSATRH RKTICLLCNK SDSIETVSVP YVFKYFVAEL AAMNIKIKLD VK