| Tag | Content |
|---|
| CPLM ID | CPLM-003866 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | DNA-directed RNA polymerase I subunit RPA190 |
Protein Synonyms/Alias | DNA-directed RNA polymerase I 190 kDa polypeptide; A190; DNA-directed RNA polymerase I largest subunit |
Gene Name | RPA190 |
Gene Synonyms/Alias | RPA1; RRN1; YOR341W; O6276 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 30 | EIRNLSAKQITNPTV | ubiquitination | [1] | | 182 | STLLNELKSKRSEYV | acetylation | [2] | | 410 | LSKLQKDKVSLEDRR | ubiquitination | [1] | | 1256 | EQADTFCKSISKVLL | ubiquitination | [1] | | 1363 | ANSSSNSKRLEEDND | ubiquitination | [1] | | 1379 | EQSHKKTKQAVSYDE | ubiquitination | [1] |
|
Reference | [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J. Nat Methods. 2013 Jul;10(7):676-82. [ PMID: 23749301] [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | 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). |
Sequence Annotation | REGION 992 1004 Bridging helix (By similarity).
METAL 62 62 Zinc 1 (By similarity).
METAL 65 65 Zinc 1 (By similarity).
METAL 72 72 Zinc 1 (By similarity).
METAL 75 75 Zinc 1 (By similarity).
METAL 627 627 Magnesium; catalytic (By similarity).
METAL 629 629 Magnesium; catalytic (By similarity).
METAL 631 631 Magnesium; catalytic (By similarity).
MOD_RES 889 889 Phosphoserine.
MOD_RES 1636 1636 Phosphoserine. |
Keyword | Complete proteome; DNA-directed RNA polymerase; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transferase; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1664 AA |
Protein Sequence | MDISKPVGSE ITSVDFGILT AKEIRNLSAK QITNPTVLDN LGHPVSGGLY DLALGAFLRN 60
LCSTCGLDEK FCPGHQGHIE LPVPCYNPLF FNQLYIYLRA SCLFCHHFRL KSVEVHRYAC 120
KLRLLQYGLI DESYKLDEIT LGSLNSSMYT DDEAIEDNED EMDGEGSKQS KDISSTLLNE 180
LKSKRSEYVD MAIAKALSDG RTTERGSFTA TVNDERKKLV HEFHKKLLSR GKCDNCGMFS 240
PKFRKDGFTK IFETALNEKQ ITNNRVKGFI RQDMIKKQKQ AKKLDGSNEA SANDEESFDV 300
GRNPTTRPKT GSTYILSTEV KNILDTVFRK EQCVLQYVFH SRPNLSRKLV KADSFFMDVL 360
VVPPTRFRLP SKLGEEVHEN SQNQLLSKVL TTSLLIRDLN DDLSKLQKDK VSLEDRRVIF 420
SRLMNAFVTI QNDVNAFIDS TKAQGRTSGK VPIPGVKQAL EKKEGLFRKH MMGKRVNYAA 480
RSVISPDPNI ETNEIGVPPV FAVKLTYPEP VTAYNIAELR QAVINGPDKW PGATQIQNED 540
GSLVSLIGMS VEQRKALANQ LLTPSSNVST HTLNKKVYRH IKNRDVVLMN RQPTLHKASM 600
MGHKVRVLPN EKTLRLHYAN TGAYNADFDG DEMNMHFPQN ENARAEALNL ANTDSQYLTP 660
TSGSPVRGLI QDHISAGVWL TSKDSFFTRE QYQQYIYGCI RPEDGHTTRS KIVTLPPTIF 720
KPYPLWTGKQ IITTVLLNVT PPDMPGINLI SKNKIKNEYW GKGSLENEVL FKDGALLCGI 780
LDKSQYGASK YGIVHSLHEV YGPEVAAKVL SVLGRLFTNY ITATAFTCGM DDLRLTAEGN 840
KWRTDILKTS VDTGREAAAE VTNLDKDTPA DDPELLKRLQ EILRDNNKSG ILDAVTSSKV 900
NAITSQVVSK CVPDGTMKKF PCNSMQAMAL SGAKGSNVNV SQIMCLLGQQ ALEGRRVPVM 960
VSGKTLPSFK PYETDAMAGG YVKGRFYSGI KPQEYYFHCM AGREGLIDTA VKTSRSGYLQ 1020
RCLTKQLEGV HVSYDNSIRD ADGTLVQFMY GGDAIDITKE SHMTQFEFCL DNYYALLKKY 1080
NPSALIEHLD VESALKYSKK TLKYRKKHSK EPHYKQSVKY DPVLAKYNPA KYLGSVSENF 1140
QDKLESFLDK NSKLFKSSDG VNEKKFRALM QLKYMRSLIN PGEAVGIIAS QSVGEPSTQM 1200
TLNTFHFAGH GAANVTLGIP RLREIVMTAS AAIKTPQMTL PIWNDVSDEQ ADTFCKSISK 1260
VLLSEVIDKV IVTETTGTSN TAGGNAARSY VIHMRFFDNN EYSEEYDVSK EELQNVISNQ 1320
FIHLLEAAIV KEIKKQKRTT GPDIGVAVPR LQTDVANSSS NSKRLEEDND EEQSHKKTKQ 1380
AVSYDEPDED EIETMREAEK SSDEEGIDSD KESDSDSEDE DVDMNEQINK SIVEANNNMN 1440
KVQRDRQSAI ISHHRFITKY NFDDESGKWC EFKLELAADT EKLLMVNIVE EICRKSIIRQ 1500
IPHIDRCVHP EPENGKRVLV TEGVNFQAMW DQEAFIDVDG ITSNDVAAVL KTYGVEAARN 1560
TIVNEINNVF SRYAISVSFR HLDLIADMMT RQGTYLAFNR QGMETSTSSF MKMSYETTCQ 1620
FLTKAVLDNE REQLDSPSAR IVVGKLNNVG TGSFDVLAKV PNAA 1664 |
Gene Ontology | GO:0005736; C:DNA-directed RNA polymerase I complex; IDA:SGD. GO:0003677; F:DNA binding; IEA:InterPro. GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0042790; P:transcription of nuclear large rRNA transcript from RNA polymerase I promoter; IMP:SGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |