Reviewed, UniProtKB/Swiss-Prot P15398 (RPA1_SCHPO)

Names and origin

Protein names

Recommended name:
    DNA-directed RNA polymerase I subunit rpa1
    EC=2.7.7.6
Alternative name(s):
    DNA-directed RNA polymerase I 190 kDa polypeptide
    DNA-directed RNA polymerase I largest subunit

Gene names

Name:	rpa1
Synonyms:	nuc1
ORF Names:	SPBC4C3.05c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	1689 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition By similarity.
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Subunit structure	Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits By similarity.
Subcellular location	Nucleus › nucleolus Ref.1.
Sequence similarities	Belongs to the RNA polymerase beta' chain family.

Ontologies

Keywords
Biological process	Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Ligand	Magnesium Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	mRNA export from nucleus Inferred from mutant phenotype. Source: GeneDB_SPombe nucleolus organization Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe protein localization to nucleolar rDNA repeats Inferred from mutant phenotype. Source: GeneDB_SPombe transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1689	1689	DNA-directed RNA polymerase I subunit rpa1		PRO_0000073929
Regions
	Region	1005 – 1017	13	Bridging helix By similarity
Sites
	Metal binding	63	1	Zinc By similarity
	Metal binding	66	1	Zinc By similarity
	Metal binding	73	1	Zinc By similarity
	Metal binding	76	1	Zinc By similarity
	Metal binding	643	1	Magnesium; catalytic By similarity
	Metal binding	645	1	Magnesium; catalytic By similarity
	Metal binding	647	1	Magnesium; catalytic By similarity
Amino acid modifications
	Modified residue	159	1	Phosphoserine Ref.4
	Modified residue	161	1	Phosphoserine Ref.4
	Modified residue	1438	1	Phosphoserine Ref.4
	Modified residue	1441	1	Phosphoserine Ref.4
Experimental info
	Sequence conflict	69	1	D → A in CAA32887. Ref.1
	Sequence conflict	84	1	I → S in CAA32887. Ref.1
	Sequence conflict	704	1	T → I in CAA32887. Ref.1
	Sequence conflict	1581	1	A → T in CAA32887. Ref.1
	Sequence conflict	1681	1	T → N in CAA32887. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P15398-1 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: 2D2D3A2DEC94A497	FASTA	1,689	189,246
	10 20 30 40 50 60 MNIAQPVSSE IKSVKFGIYD VDDVEKISVK QIVNPVLLDN LNHPTNGGLY DLALGPYLKN 70 80 90 100 110 120 SVCATCHLDE RYCPGHFGHI VLPIPAYHPL FFSQMYNLLR STCLYCHHFK LSKVKVHLFF 130 140 150 160 170 180 CRLKLLDYGL LNESEMVENV SLTEAIIKNS NGTPLEDGSD SEDSGLGHDD IAKDAATLMR 190 200 210 220 230 240 IRDEFVAKSI ADSRQNAHID AQLTTLLLHE RKKVVRAFYH AISSRKQCDN CQSFSPNFRK 250 260 270 280 290 300 EGFAKIFEIP LSGKNLQFME QTGKIRSDVL RDTSKKHHED EGYDGDSDSS NESEVEGIDL 310 320 330 340 350 360 FEEDPNPLKN KSKSPIAHGA KYMTSTEVRN HLRRLFVKEN VVLSRLYAHK RGKPASADMF 370 380 390 400 410 420 FLQNIAVPPT RFRPASKMGD EVHENIQNEL LTRILQSSIQ IASLSKDSTV EVNPDEKEGL 430 440 450 460 470 480 ERRSRAFELL INAFVQLQHD VNSLIDSNRN PSSGGQSRTV PPGIKQILEK KEGLFRKHMM 490 500 510 520 530 540 GKRVNYAARS VISPDPNIET NEIGVPPVFA TKLTYPEPVT LYNFNEMRNA VINGPHKWPG 550 560 570 580 590 600 ASHIQNEDGT LISLMPLTIE QRTALANQLL TPQSNLISSP YSYSRLINTN KKVYRHVRNG 610 620 630 640 650 660 DMLILNRQPT LHKPSMMAHK ARILPGEKTI RMHYANCNSY NADFDGDEMN MHFPQSTNAR 670 680 690 700 710 720 SEAQFIANTD SQYLVPTSGD PLRGLIQDHV VMGVWLTCKD TFYTRDEYQQ LLFQALKPDE 730 740 750 760 770 780 TGMYGRIKTL PPAIQRPGIY WTGKQIISSV LLNLKPSDRP GLNLKSKAKV PGKYWSPDSE 790 800 810 820 830 840 EGSVLFDDGE LLCGILDKSS FGASAFGLVH SVHELYGPDI AGRLLSVLSR LFTAYAQMRG 850 860 870 880 890 900 FTCRMDDLRL DEQGDNWRRQ LLENGKSFGL EAASEYVGLS TDSPIALLNA NLEEVYRDDE 910 920 930 940 950 960 KLQGLDAAMK GKMNGLTSSI INKCIPDGLL TKFPYNHMQT MTVSGAKGSN VNVSQISCLL 970 980 990 1000 1010 1020 GQQELEGRRV PLMVSGKSLP SFVPYETSAK SGGFIASRFL TGIAPQEYYF HCMAGREGLI 1030 1040 1050 1060 1070 1080 DTAVKTSRSG YLQRCLMKHL EGLCVQYDHT VRDSDGSIVQ FHYGEDSLDV TKQKHLTQFE 1090 1100 1110 1120 1130 1140 FSAKNYKSLI QKYKVKSVLS AVDSETASSY AKKALKKPYK YDPVLDKYPP SRYLGSVSEK 1150 1160 1170 1180 1190 1200 FQRAVDEYTQ KNPDKLIASK KESKLDDSLL NESKFKALMQ LRYQQSLVDP GESVGVLASQ 1210 1220 1230 1240 1250 1260 SIGEPSTQMT LNTFHFAGFG AKNVTLGIPR LREIIMTASA NIQTPTMTLR LNDGVSDKRA 1270 1280 1290 1300 1310 1320 SAFCKEVNKL VLSEVVRQVR VTEKISGQGS DEQSKTYAIR LDLYSRDEYQ DEYGVLQEEI 1330 1340 1350 1360 1370 1380 ESTFSNRFLK ILNRIIKSYL AKSKQRKSGG KDDTVPEVGQ ALKPLEDIDE APIEGRAQEA 1390 1400 1410 1420 1430 1440 LEDEDNDATN EKMVSRSKQH ASYEGPDEAD KVALRQLKGS NKVEDVNMDE EEDEGFKSDE 1450 1460 1470 1480 1490 1500 SVSDFKERKL LEKQNTVSIS ERRELQLKTA KEILSNCKHL DFDYVNGEWA TVELVFPINT 1510 1520 1530 1540 1550 1560 EKLLMVSLVE KACSETVIHE IPGITRCFSK PPDSALDTVP KVITEGVNLK AIWEFYNEIS 1570 1580 1590 1600 1610 1620 MNDIYTNDIA AILRIYGVEA ARNAIVHEVS SVFGVYGIAV DPRHLSLIAD YMTFEGGYKA 1630 1640 1650 1660 1670 1680 FNRMGIEYNT SPFAKMSFET TCHFLTEAAL RGDVDDLSNP SSRLVVGRVG NFGTGSFDIF TPVVDSPAN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Essential roles of the RNA polymerase I largest subunit and DNA topoisomerases in the formation of fission yeast nucleolus." Hirano T., Konoha G., Toda T., Yanagida M. J. Cell Biol. 108:243-253(1989) [PubMed: 2537310] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
[2]	"Cloning and sequence determination of the gene encoding the largest subunit of the fission yeast Schizosaccharomyces pombe RNA polymerase I." Yamagishi M., Nomura M. Gene 74:503-515(1988) [PubMed: 2854522] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 972 / HM123.
[3]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[4]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159; SER-161; SER-1438 AND SER-1441, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X14783 Genomic DNA. Translation: CAA32887.1. M37411 Genomic DNA. Translation: AAA35326.1. CU329671 Genomic DNA. Translation: CAA16827.1.
PIR	JS0080.
RefSeq	NP_596300.1.
3D structure databases
SMR	P15398. Positions 1542-1680.
ModBase	Search...
Protein-protein interaction databases
STRING	P15398.
Genome annotation databases
GeneID	2540873.
GenomeReviews	Gene locus rpa1 in contig CU329671_GR.
KEGG	spo:SPBC4C3.05c.
NMPDR	fig|4896.1.peg.2166.
Organism-specific databases
GeneDB_Spombe	SPBC4C3.05c.
Phylogenomic databases
eggNOG	fuNOG06538.
HOGENOM	HBG598940.
OMA	VPPTRFR.
OrthoDB	EOG9KD83V.
PhylomeDB	P15398.
Enzyme and pathway databases
BRENDA	2.7.7.6. 653.
Gene expression databases
ArrayExpress	P15398.
Family and domain databases
InterPro	IPR015699. DNA-dir_RNA_pol1_lsu. IPR000722. RNA_pol_asu. IPR006592. RNA_pol_N. IPR007080. RNA_pol_Rpb1_1. IPR007066. RNA_pol_Rpb1_3. IPR007083. RNA_pol_Rpb1_4. IPR007081. RNA_pol_Rpb1_5. [Graphical view]
Gene3D	G3DSA:2.40.40.30. RNA_pol_A. 1 hit. G3DSA:3.90.1120.10. RNA_pol_Rpb1_1. 1 hit.
PANTHER	PTHR19376:SF11. RNA_polyI. 1 hit.
Pfam	PF04997. RNA_pol_Rpb1_1. 1 hit. PF00623. RNA_pol_Rpb1_2. 1 hit. PF04983. RNA_pol_Rpb1_3. 1 hit. PF05000. RNA_pol_Rpb1_4. 1 hit. PF04998. RNA_pol_Rpb1_5. 1 hit. [Graphical view]
SMART	SM00663. RPOLA_N. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RPA1_SCHPO

Accession

Primary (citable) accession number: P15398

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	July 15, 1998
Last modified:	January 19, 2010
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)