RPA2_NEUCR
ID RPA2_NEUCR Reviewed; 1234 AA.
AC O74633; Q7RVL5;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=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=acr-2; ORFNames=NCU08616;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UN-18;
RX PubMed=9749669; DOI=10.1007/s004380050812;
RA Onai K., Katagiri S., Akiyama M., Nakashima H.;
RT "Mutation of the gene for the second-largest subunit of RNA polymerase I
RT prolongs the period length of the circadian conidiation rhythm in
RT Neurospora crassa.";
RL Mol. Gen. Genet. 259:264-271(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; AB006052; BAA33445.1; -; Genomic_DNA.
DR EMBL; CM002236; EAA35588.1; -; Genomic_DNA.
DR PIR; T30515; T30515.
DR RefSeq; XP_964824.1; XM_959731.3.
DR AlphaFoldDB; O74633; -.
DR SMR; O74633; -.
DR STRING; 5141.EFNCRP00000008643; -.
DR EnsemblFungi; EAA35588; EAA35588; NCU08616.
DR GeneID; 3880984; -.
DR KEGG; ncr:NCU08616; -.
DR VEuPathDB; FungiDB:NCU08616; -.
DR HOGENOM; CLU_000524_5_1_1; -.
DR InParanoid; O74633; -.
DR OMA; FFGVVHY; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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; IEA:EnsemblFungi.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IEA:EnsemblFungi.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IEA:EnsemblFungi.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IEA:EnsemblFungi.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IEA:EnsemblFungi.
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 DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Nucleus; Reference proteome; Transcription; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1234
FT /note="DNA-directed RNA polymerase I subunit RPA2"
FT /id="PRO_0000048078"
FT ZN_FING 1119..1150
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P22138"
FT MUTAGEN 976
FT /note="G->D: In un-18; shows a TS phenotype with respect to
FT both mycelial growth and the period length of the
FT conidiation rhythm."
FT CONFLICT 294..299
FT /note="GVANTF -> ASPTPS (in Ref. 1; BAA33445)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1234 AA; 138601 MW; 8840AA85D52BBAE0 CRC64;
MAPQQPQPTS QDWDVEFNQV RREKLFRDPP TDRTAYPALQ AAVDPHIESF NALFRDDGKP
SLLDHALAEI GTKTFLDGDE RADPQGKNKL TIRYKSIELQ KSQVPPTNRW AKNREIFPAE
CRERHVSYRG KLSATFEYRI NDGEPHEFVR ELGQMPIMVK SNKCHLQNNS PAQLVARKEE
SEELGGYFIV NGIEKLIRML LVNRRNFPLA IVRPSFQNRG ASYTPYGIIM RSVRPDETSQ
TNVLHYLSDG NVTFRFSWRK NEYLIPVMMI MKALVETNDR EIFEGLVGPP QSKGVANTFL
TDRVELLLRT YKKYGLYSKT QTRAYLGQKF RVVLGVPDTM SDYEVGTEFL RKIVLVHLGS
QDVTEQQDAD KFNMLLFMCR KLYALVAGDC AVDNPDAVQN QEILLGGFLY GQIIKERLEE
LLTVSFRASL RDYLRRNPTV SFQSDTFLKD FPIAIFRRAN ENIGQSLEYF LSTGNLVSPS
GLDLQQVSGF TVVAEKLNFL RFISHFRMVH RGSFFAQLKT TTVRKLLPES WGFLCPVHTP
DGSPCGLLNH LAHKCKIMTE SVDASTISRL AFELGVVNIS SAATSESVVV MLDGRIVGWC
TPEECKSIAE TLRYWKVNGE NGVPLQLEIG YVPPSNGGSY PGLYMSSQPA RMVRPVKYLP
LQKEDFVGPQ EQPYMSIACT EQEVIPGDST HVEFDPTNIL SILANMTPFS DFNQSPRNMY
QCQMGKQTMG TPATALAHRT DNKMYRLQTG QTPVVRAPLH NTYGFDNFPN GMNAVVAVIS
YTGYDMDDAM ILNKSAHERG FGHGSIYKTK KVSLKDDSRT RSAKSIVKMF GFAPNSTIRE
STRDMLDNDG LPRVGRLLRE GDVICAWHTV SADYNGQLVN RDGVTHYERY KDSEDAFVEE
VRVIGADNGT EPLQTVSIKL RIPRSPVIGD KFSSRHGQKG VLSQKWPATD MPFSETGIQP
DVIINPHAFP SRMTIGMFVE SLAGKAGALH GLAQDSTPFK FDEQNTAGDY FGHQLMKAGY
NYHGNEPLYS GITGEEFQAD IYIGVVYYQR LRHMVNDKYQ VRTTGPVVPT TGQPIKGRKK
GGGIRVGEME RDALLAHGTS FLLQDRLLNC SDYSKSWMCR QCGSFLSTQP TVSPFIGKRK
AVSTVRCRNC AVRLDDMEDV DLMQIDGEIW EDGSGTQWIG GENTTIVAVP GALKYLDVEL
AAMGIKLKYK VDKKDEIRRG QLVGKKAGDL MLTA