CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000222
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transposon Ty1-H Gag-Pol polyprotein 
Protein Synonyms/Alias
 Gag-Pol-p199; TY1A-TY1B; Transposon Ty1 TYA-TYB polyprotein; p190; Capsid protein; CA; Gag-p45; p54; Ty1 protease; PR; Pol-p20; p23; Integrase; IN; Pol-p71; p84; p90; Reverse transcriptase/ribonuclease H; RT; RT-RH; Pol-p63; p60 
Gene Name
 TY1B-H 
Gene Synonyms/Alias
 YHRCTy1-1 POL; YHR214C-B 
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
45SKIQEYDKASTKANSacetylation[1]
245IIPTVNGKPVRQITDacetylation[1]
245IIPTVNGKPVRQITDubiquitination[2]
292DIMKILSKSIEKMQSacetylation[1]
360RGLSGEYKFLRYTRHacetylation[1]
360RGLSGEYKFLRYTRHubiquitination[2]
417RSYTNTTKPKVIARNacetylation[1]
432PQKTNNSKSKTARAHacetylation[3]
434KTNNSKSKTARAHNVacetylation[3]
457TDNDSISKSTTEPIQubiquitination[2]
1520YQRGKYMKLGMENSLacetylation[1]
1530MENSLTEKIPKLNVPubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591] 
Functional Description
 Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity). 
Sequence Annotation
 DOMAIN 698 873 Integrase catalytic.
 DOMAIN 1376 1514 Reverse transcriptase Ty1/copia-type.
 DOMAIN 1648 1790 RNase H Ty1/copia-type.
 REGION 337 439 RNA-binding (By similarity).
 REGION 621 678 Integrase-type zinc finger-like.
 MOTIF 1216 1250 Bipartite nuclear localization signal (By
 ACT_SITE 499 499 For protease activity; shared with
 METAL 709 709 Magnesium; catalytic; for integrase
 METAL 774 774 Magnesium; catalytic; for integrase
 METAL 1384 1384 Magnesium; catalytic; for reverse
 METAL 1465 1465 Magnesium; catalytic; for reverse
 METAL 1466 1466 Magnesium; catalytic; for reverse
 METAL 1648 1648 Magnesium; catalytic; for RNase H
 METAL 1690 1690 Magnesium; catalytic; for RNase H
 METAL 1723 1723 Magnesium; catalytic; for RNase H  
Keyword
 Aspartyl protease; ATP-binding; Capsid maturation; Complete proteome; Cytoplasm; DNA integration; DNA recombination; DNA-binding; DNA-directed DNA polymerase; Endonuclease; Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme; Nuclease; Nucleotide-binding; Nucleotidyltransferase; Nucleus; Protease; Reference proteome; Ribosomal frameshifting; RNA-binding; RNA-directed DNA polymerase; Transferase; Transposable element; Transposition; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1793 AA 
Protein Sequence
MESQQLSNYP HISHGSACAS VTSKEVHTNQ DPLDVSASKI QEYDKASTKA NSQQTTTPAS 60
SAVPENLHHA SPQPASVPPP QNGPYPQQCM MTQNQANPSG WSFYGHPSMI PYTPYQMSPM 120
YFPPGPQSQF PQYPSSVGTP LSTPSPESGN TFTDSSSADS DMTSTKKYVR PPPMLTSPND 180
FPNWVKTYIK FLQNSNLGGI IPTVNGKPVP PMLTSPNDFP NWVKTYIKFL QNSNLGGIIP 240
TVNGKPVRQI TDDELTFLYN TFQIFAPSQF LPTWVKDILS VDYTDIMKIL SKSIEKMQSD 300
TQEANDIVTL ANLQYNGSTP ADAFETKVTN IIDRLNNNGI HINNKVACQL IMRGLSGEYK 360
FLRYTRHRHL NMTVAELFLD IHAIYEEQQG SRNSKPNYRR NPSDEKNDSR SYTNTTKPKV 420
IARNPQKTNN SKSKTARAHN VSTSNNSPST DNDSISKSTT EPIQLNNKHD LHLGQKLTES 480
TVNHTNHSDD ELPGHLLLDS GASRTLIRSA HHIHSASSNP DINVVDAQKR NIPINAIGDL 540
QFHFQDNTKT SIKVLHTPNI AYDLLSLNEL AAVDITACFT KNVLERSDGT VLAPIVKYGD 600
FYWVSKKYLL PSNISVPTIN NVHTSESTRK YPYPFIHRML AHANAQTIRY SLKNNTITYF 660
NESDVDWSSA IDYQCPDCLI GKSTKHRHIK GSRLKYQNSY EPFQYLHTDI FGPVHNLPKS 720
APSYFISFTD ETTKFRWVYP LHDRREDSIL DVFTTILAFI KNQFQASVLV IQMDRGSEYT 780
NRTLHKFLEK NGITPCYTTT ADSRAHGVAE RLNRTLLDDC RTQLQCSGLP NHLWFSAIEF 840
STIVRNSLAS PKSKKSARQH AGLAGLDIST LLPFGQPVIV NDHNPNSKIH PRGIPGYALH 900
PSRNSYGYII YLPSLKKTVD TTNYVILQGK ESRLDQFNYD ALTFDEDLNR LTASYHSFIA 960
SNEIQQSNDL NIESDHDFQS DIELHPEQLR NVLSKAVSPT DSTPPSTHTE DSKRVSKTNI 1020
RAPREVDPNI SESNILPSKK RSSTPQISDI ESTGSGGMHR LDVPLLAPMS QSNTHESSHA 1080
SKSKDFRHSD SYSDNETNHT NVPISSTGGT NNKTVPQTSE QETEKRIIHR SPSIDTSSSE 1140
SNSLHHVVPI KTSDTCPKEN TEESIIADLP LPDLPPEPPT ELSDSFKELP PINSHQTNSS 1200
LGGIGDSNAY TTINSKKRSL EDNETEIKVS RDTWNTKNMR SLEPPRSKKR IHLIAAVKAV 1260
KSIKPIRTTL RYDEAITYNK DIKEKEKYIQ AYHKEVNQLL MMKTWDTDRY YDRKEIDPKR 1320
VINSMFIFNR KRDGTHKARF VARGDIQHPD TYDPGMQSNT VHHYALMTSL SLALDNNYYI 1380
TQLDISSAYL YADIKEELYI RPPPHLGMND KLIRLKKSLY GLKQSGANWY ETIKSYLIKQ 1440
CGMEEVRGWS CVFKNSQVTI CLFVDDMILF SKDLNANKKI ITTLKKQYDT KIINLGESDN 1500
EIQYDILGLE IKYQRGKYMK LGMENSLTEK IPKLNVPLNP KGRKLSAPGQ PGLYIDQDEL 1560
EIDEDEYKEK VHEMQKLIGL ASYVGYKFRF DLLYYINTLA QHILFPSRQV LDMTYELIQF 1620
MWDTRDKQLI WHKNKPTEPD NKLVAISDAS YGNQPYYKSQ IGNIYLLNGK VIGGKSTKAS 1680
LTCTSTTEAE IHAISESVPL LNNLSHLVQE LNKKPITKGL LTDSKSTISI IISNNEEKFR 1740
NRFFGTKAMR LRDEVSGNHL HVCYIETKKN IADVMTKPLP IKTFKLLTNK WIH 1793 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0000943; C:retrotransposon nucleocapsid; ISS:SGD.
 GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0032197; P:transposition, RNA-mediated; ISS:SGD.
 GO:0046797; P:viral procapsid maturation; IEA:UniProtKB-KW. 
Interpro
 IPR001584; Integrase_cat-core.
 IPR001969; Peptidase_aspartic_AS.
 IPR015820; Retrotransposon_Ty1A_N.
 IPR012337; RNaseH-like_dom.
 IPR013103; RVT_2. 
Pfam
 PF00665; rve
 PF07727; RVT_2
 PF01021; TYA 
SMART
  
PROSITE
 PS00141; ASP_PROTEASE
 PS50994; INTEGRASE 
PRINTS