CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000221
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Truncated transposon Ty1-A Gag-Pol polyprotein 
Protein Synonyms/Alias
 TY1B; Transposon Ty1 TYB polyprotein; Integrase; IN; Pol-p71; p84; p90; Reverse transcriptase/ribonuclease H; RT; RT-RH; Pol-p63; p60 
Gene Name
 TY1B-A 
Gene Synonyms/Alias
 YARCTy1-1 POL; YAR009C 
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
193TLHKFLEKNGITPCYubiquitination[1]
291NDHNPNSKIHPRGIPubiquitination[1]
398QPRNVLSKAVSPTDSacetylation[2]
631EDNETEIKVSRDTWNubiquitination[1]
683DEAITYNKDIKEKEKubiquitination[1]
697KYIEAYHKEVNQLLKacetylation[2]
979EKVHEMQKLIGLASYacetylation[2]
990LASYVGYKFRFDLLYubiquitination[3]
1150RNRFFGTKAMRLRDEubiquitination[1]
1172VYYIETKKNIADVMTubiquitination[1]
1180NIADVMTKPLPIKTFubiquitination[1]
1193TFKLLTNKWIH****acetylation[2]
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]
 [3] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047] 
Functional Description
 Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro- elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity). 
Sequence Annotation
 DOMAIN 101 276 Integrase catalytic.
 DOMAIN 779 917 Reverse transcriptase Ty1/copia-type.
 DOMAIN 1051 1193 RNase H Ty1/copia-type.
 MOTIF 619 653 Bipartite nuclear localization signal (By
 METAL 112 112 Magnesium; catalytic; for integrase
 METAL 177 177 Magnesium; catalytic; for integrase
 METAL 787 787 Magnesium; catalytic; for reverse
 METAL 868 868 Magnesium; catalytic; for reverse
 METAL 869 869 Magnesium; catalytic; for reverse
 METAL 1051 1051 Magnesium; catalytic; for RNase H
 METAL 1093 1093 Magnesium; catalytic; for RNase H
 METAL 1126 1126 Magnesium; catalytic; for RNase H  
Keyword
 Complete proteome; Cytoplasm; DNA integration; DNA recombination; DNA-binding; DNA-directed DNA polymerase; Endonuclease; Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme; Nuclease; Nucleotidyltransferase; Nucleus; Reference proteome; RNA-binding; RNA-directed DNA polymerase; Transferase; Transposable element; Transposition. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1196 AA 
Protein Sequence
METFTGYLKS TCFHQISPYP PSIMSIQVKV HANILILSFI ECLRMPMHRQ IRYSLKNNTI 60
TYFNESDVDW SSAIDYQCPD CLIGKSTKHR HIKGSRLKYQ NSYEPFQYLH TDIFGPVHNL 120
PKSAPSYFIS FTDETTKLRW VYPLHDRRED SILDVFTTIL AFIKNQFQAS VLVIQMDRGS 180
EYTNRTLHKF LEKNGITPCY TTTADSRAHG VAERLNRTLL DDCRTQLQCS GLPNHLWFSA 240
IEFSTIVRNS LASPKSKKSA RQHAGLAGLD ISTLLPFGQP VIVNDHNPNS KIHPRGIPGY 300
ALHPSRNSYG YIIYLPSLKK TVDTTNYVIL QGKESRLDQF NYDALTFDED LNRLTASYHS 360
FIASNEIQES NDLNIESDHD FQSDIELHPE QPRNVLSKAV SPTDSTPPST HTEDSKRVSK 420
TNIRAPREVD PNISESNILP SKKRSSTPQI SNIESTGSGG MHKLNVPLLA PMSQSNTHES 480
SHASKSKDFR HSDSYSENET NHTNVPISST GGTNNKTVPQ ISDQETEKRI IHRSPSIDAS 540
PPENNSSHNI VPIKTPTTVS EQNTEESIIA DLPLPDLPPE SPTEFPDPFK ELPPINSHQT 600
NSSLGGIGDS NAYTTINSKK RSLEDNETEI KVSRDTWNTK NMRSLEPPRS KKRIHLIAAV 660
KAVKSIKPIR TTLRYDEAIT YNKDIKEKEK YIEAYHKEVN QLLKMNTWDT DKYYDRKEID 720
PKRVINSMFI FNKKRDGTHK ARFVARGDIQ HPDTYDTGMQ SNTVHHYALM TSLSLALDNN 780
YYITQLDISS AYLYADIKEE LYIRPPPHLG MNDKLIRLKK SLYGLKQSGA NWYETIKSYL 840
IKQCGMEEVR GWSCVFKNSQ VTICLFVDDM ILFSKDLNAN KKIITTLKKQ YDTKIINLGE 900
SDNEIQYDIL GLEIKYQRGK YMKLGMEKSL TEKLPKLNVP LNPKGKKLRA PGQPGLYIDQ 960
DELEIDEDEY KEKVHEMQKL IGLASYVGYK FRFDLLYYIN TLAQHILFPS RQVLDMTYEL 1020
IQFMWDTRDK QLIWHKNKPT EPDNKLVAIS DASYGNQPYY KSQIGNIYLL NGKVIGGKST 1080
KASLTCTSTT EAEIHAISES VPLLNNLSYL IQELNKKPII KGLLTDSRST ISIIKSTNEE 1140
KFRNRFFGTK AMRLRDEVSG NNLYVYYIET KKNIADVMTK PLPIKTFKLL TNKWIH 1196 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0000943; C:retrotransposon nucleocapsid; ISS:SGD.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003887; F:DNA-directed DNA polymerase activity; ISS:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008233; F:peptidase activity; ISS:SGD.
 GO:0004540; F:ribonuclease activity; ISS:SGD.
 GO:0004523; F:ribonuclease H activity; IEA:EC.
 GO:0003723; F:RNA binding; ISS:SGD.
 GO:0003964; F:RNA-directed DNA polymerase activity; ISS:SGD.
 GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
 GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
 GO:0032197; P:transposition, RNA-mediated; ISS:SGD. 
Interpro
 IPR001584; Integrase_cat-core.
 IPR012337; RNaseH-like_dom.
 IPR013103; RVT_2. 
Pfam
 PF00665; rve
 PF07727; RVT_2 
SMART
  
PROSITE
 PS00141; ASP_PROTEASE
 PS50994; INTEGRASE 
PRINTS