RPA2_SCHPO
ID RPA2_SCHPO Reviewed; 1174 AA.
AC Q9P7X8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Probable DNA-directed RNA polymerase I subunit RPA2;
DE EC=2.7.7.6 {ECO:0000250|UniProtKB:P22138};
DE AltName: Full=DNA-directed RNA polymerase I polypeptide 2;
DE Short=RNA polymerase I subunit 2;
GN Name=rpa2; ORFNames=SPBP23A10.07;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P22138}.
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:P22138};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249;
CC Evidence={ECO:0000250|UniProtKB:P22138};
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of 14 subunits. {ECO:0000250|UniProtKB:P22138}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P22138}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB66435.2; -; Genomic_DNA.
DR PIR; T50394; T50394.
DR RefSeq; NP_595819.2; NM_001021723.3.
DR PDB; 7AOC; EM; 3.84 A; B=1-1174.
DR PDB; 7AOD; EM; 4.50 A; B/N=1-1174.
DR PDB; 7AOE; EM; 3.90 A; B=1-1174.
DR PDBsum; 7AOC; -.
DR PDBsum; 7AOD; -.
DR PDBsum; 7AOE; -.
DR AlphaFoldDB; Q9P7X8; -.
DR SMR; Q9P7X8; -.
DR BioGRID; 277793; 14.
DR IntAct; Q9P7X8; 1.
DR STRING; 4896.SPBP23A10.07.1; -.
DR MaxQB; Q9P7X8; -.
DR PaxDb; Q9P7X8; -.
DR PRIDE; Q9P7X8; -.
DR EnsemblFungi; SPBP23A10.07.1; SPBP23A10.07.1:pep; SPBP23A10.07.
DR GeneID; 2541280; -.
DR KEGG; spo:SPBP23A10.07; -.
DR PomBase; SPBP23A10.07; rpa2.
DR VEuPathDB; FungiDB:SPBP23A10.07; -.
DR eggNOG; KOG0216; Eukaryota.
DR HOGENOM; CLU_000524_5_1_1; -.
DR InParanoid; Q9P7X8; -.
DR OMA; FFGVVHY; -.
DR PhylomeDB; Q9P7X8; -.
DR Reactome; R-SPO-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR PRO; PR:Q9P7X8; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005736; C:RNA polymerase I complex; ISO:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006360; P:transcription by RNA polymerase I; ISO:PomBase.
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 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transcription;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1174
FT /note="Probable DNA-directed RNA polymerase I subunit RPA2"
FT /id="PRO_0000048079"
FT ZN_FING 1089..1118
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P22138"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 131687 MW; 43D5E6A638F6996A CRC64;
MSFQTLERER TFKNPPKDGT SFPDLQKAVK PHVDSFNALT NAGLLNYAVK EIGEKCAFDS
ITQEEGGALK FGNKISFRVD EVQIAKPMLS SRERSSINRK VYPAEARERL TTYKSRLVLK
FSWSVNGGPR QSEMREVGMI PIMVRSNRCH LEGLSPAELI AHKEESEEMG GYFIVNGIEK
LIRMLILPKR NHPTAIIRPS FANRGTSYSQ YGLSIRCVRP DQSSLTNTLH YLNNGVTMFR
FHWRKNEYLI PSMMILKALL ETSDKEIFEG IVGKDLGNTF LTDRVELMLR AYKSYGLYSQ
TETLQYLGSK FRVVLGVAED LTDVEVGRFL LQKVVLVHLR EAKDKFRLLL FMIRKLYALV
AGECCADNPD SPQHQEILLG GFLYGQILKE KIEDWLNSIR AQINLDVRRS APGVDFSDRK
YLTRVFSKIN NDIGTKLQYF LSTGNLVSNT GLDLQQATGY TVVAEKLNFY RFLSHFRMVH
RGAFFAELKT TTVRKLLPEA WGFMCPVHTP DGSPCGLLNH LARKCEIVTH PSDVSQIPSL
LLSLGVDPPS VVGHESGWGC VQLDGKIVGW CTYKLAKHVA DVLRLMKIEY AVKLRNGTAT
EPAKVPLDLE IGYVPPSHNG QYPGLYLFSN PARMVRPVKH ISTGELDMLG PFEQVYMDIA
CFPKEIVPKV STHVEYSPTN VLSIVANMTP FSDFNQSPRN MYQCQMGKQT MGTPGTALRY
RTDNKLYRLQ TGQTPVVRPK LHNTYGLDHY PNGTNAVVAV ISYTGYDMED AMILNKSAHE
RGFGYGTVYK GESFDLSQKR RRGEPVVHHF GFAPGSTPRR EWLQKLDADG LPFIGIKLED
GDPIVAYYDE STGQNFIETY HGTEPGFVDE VRLLGNDVGD SECQQIHVKL RITRSPIIGD
KFSSRHGQKG ICSQKWPTVD MPFTESGMQP DIIINPHAFP SRMTIGMFIE SLAGKAGACH
GLAQDSTPFI YSEQQTAADY FGEQLVKAGY NYHGNEPMYS GITGQEMKAD IYIGVVYYQR
LRHMVSDKFQ VRTTGPIHNL TRQPVKGRKR AGGIRFGEME RDAVIGHGTS FLMQDRLMNC
SDYAQSWVCR DCGSIISIMS TISMNGVGSA SEVRCRSCAK PALGLEDTSD IWQDGSGKKF
VGGTNTTLIA LPSVFNYLTA ELTAMNIKMM LEVK
