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Q99315 (YG31B_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transposon Ty3-G Gag-Pol polyprotein
Alternative name(s):
Gag3-Pol3
Transposon Ty3-1 TYA-TYB polyprotein

Cleaved into the following 8 chains:

  1. Capsid protein
    Short name=CA
    Alternative name(s):
    p24
  2. Spacer peptide p3
  3. Nucleocapsid protein p11
    Short name=NC
  4. Ty3 protease
    Short name=PR
    EC=3.4.23.-
    Alternative name(s):
    p16
  5. Spacer peptide J
  6. Reverse transcriptase/ribonuclease H
    Short name=RT
    Short name=RT-RH
    EC=2.7.7.49
    EC=2.7.7.7
    EC=3.1.26.4
    Alternative name(s):
    p55
  7. Integrase p61
    Short name=IN
  8. Integrase p58
    Short name=IN
Gene names
Name:TY3B-G
Synonyms:YGRWTy3-1 POL
Ordered Locus Names:YGR109W-B
ORF Names:G5984
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1547 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the genomic RNA-nucleocapsid complex. Ref.1 Ref.6 Ref.10 Ref.12

Nucleocapsid protein p11 (NC) forms the nucleocore that coats the retro-elements dimeric RNA. Binds these RNAs through its zinc fingers By similarity. Promotes primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty3 RNA and initiation of reverse transcription. Ref.1 Ref.6 Ref.10 Ref.12

The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP. Ref.1 Ref.6 Ref.10 Ref.12

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. Ref.1 Ref.6 Ref.10 Ref.12

Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome. Ref.1 Ref.6 Ref.10 Ref.12

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Endonucleolytic cleavage to 5'-phosphomonoester.

Subunit structure

The protease is a homodimer, whose active site consists of two apposed aspartic acid residues.

Subcellular location

Cytoplasm. Nucleus Ref.6.

Domain

Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D35E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein.

Post-translational modification

Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and contain also the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein, and this cleavage is a prerequisite for subsequent processing at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs.

Miscellaneous

Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty3 retrotransposons belong to the gypsy-like elements (metaviridae).

Sequence similarities

Contains 1 CCHC-type zinc finger.

Contains 1 integrase catalytic domain.

Contains 1 peptidase A2 domain.

Contains 1 reverse transcriptase domain.

Contains 1 RNase H Ty3/gyspy-type domain.

Sequence caution

The sequence AAA98435.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAA97115.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAA97117.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence DAA08202.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processDNA integration
DNA recombination
Virion maturation
Virus exit from host cell
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityRibosomal frameshifting
   DomainZinc-finger
   LigandATP-binding
DNA-binding
Magnesium
Metal-binding
Nucleotide-binding
RNA-binding
Zinc
   Molecular functionAspartyl protease
DNA-directed DNA polymerase
Endonuclease
Hydrolase
Nuclease
Nucleotidyltransferase
Protease
RNA-directed DNA polymerase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Reference proteome
Transposable element
Gene Ontology (GO)
   Biological_processDNA integration

Inferred from electronic annotation. Source: UniProtKB-KW

DNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent DNA replication

Inferred from sequence or structural similarity Ref.11. Source: GOC

RNA phosphodiester bond hydrolysis

Inferred from sequence or structural similarity Ref.11. Source: GOC

transposition, RNA-mediated

Inferred from sequence or structural similarity Ref.11. Source: SGD

viral release from host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 9448009. Source: SGD

retrotransposon nucleocapsid

Inferred from sequence or structural similarity Ref.11. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-directed DNA polymerase activity

Inferred from sequence or structural similarity Ref.11. Source: SGD

RNA binding

Inferred from sequence or structural similarity Ref.11. Source: SGD

RNA-DNA hybrid ribonuclease activity

Inferred from electronic annotation. Source: UniProtKB-EC

RNA-directed DNA polymerase activity

Inferred from sequence or structural similarity Ref.11. Source: SGD

aspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

peptidase activity

Inferred from sequence or structural similarity Ref.11. Source: SGD

ribonuclease activity

Inferred from sequence or structural similarity Ref.11. Source: SGD

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]

Note: The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift.
Isoform Transposon Ty3-G Gag-Pol polyprotein (identifier: Q99315-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Produced by +1 ribosomal frameshifting between codon Ala-285 and Val-286 of the YGR109W-A ORF.
Isoform Transposon Ty3-G Gag polyprotein (identifier: Q12173-1)

The sequence of this isoform can be found in the external entry Q12173.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 15471546Transposon Ty3-G Gag-Pol polyprotein
PRO_0000279356
Chain2 – 207206Capsid protein
PRO_0000279357
Peptide208 – 23326Spacer peptide p3
PRO_0000279358
Chain234 – 30976Nucleocapsid protein p11
PRO_0000279359
Chain310 – 442133Ty3 protease
PRO_0000279360
Peptide443 – 53593Spacer peptide J Potential
PRO_0000279361
Chain536 – 1011476Reverse transcriptase/ribonuclease H
PRO_0000279362
Chain1012 – 1547536Integrase p61
PRO_0000279363
Chain1038 – 1547510Integrase p58
PRO_0000279364

Regions

Domain620 – 797178Reverse transcriptase
Domain893 – 1011119RNase H Ty3/gyspy-type
Domain1159 – 1324166Integrase catalytic
Zinc finger265 – 28218CCHC-type
Region1106 – 114540Integrase-type zinc finger-like

Sites

Active site3361For protease activity; shared with dimeric partner By similarity
Metal binding6861Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding7481Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding7491Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding8931Magnesium; catalytic; for RNase H activity By similarity
Metal binding9361Magnesium; catalytic; for RNase H activity By similarity
Metal binding9611Magnesium; catalytic; for RNase H activity By similarity
Metal binding11751Magnesium; catalytic; for integrase activity By similarity
Metal binding12361Magnesium; catalytic; for integrase activity By similarity
Site207 – 2082Cleavage; by Ty3 protease
Site233 – 2342Cleavage; by Ty3 protease
Site309 – 3102Cleavage; by Ty3 protease
Site442 – 4432Cleavage; by Ty3 protease Potential
Site535 – 5362Cleavage; by Ty3 protease
Site1011 – 10122Cleavage; by Ty3 protease
Site1037 – 10382Cleavage; by Ty3 protease; partial

Amino acid modifications

Modified residue21N-acetylserine Ref.15

Experimental info

Mutagenesis2671C → S: Reduces level of VLP formation and maturation. Ref.10
Mutagenesis2751H → Q: Reduces level of VLP formation and maturation. Ref.10

Secondary structure

............................................................... 1547
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Transposon Ty3-G Gag-Pol polyprotein [UniParc].

Last modified March 6, 2007. Version 3.
Checksum: 0E327D91E0575F78

FASTA1,547178,307
        10         20         30         40         50         60 
MSFMDQIPGG GNYPKLPVEC LPNFPIQPSL TFRGRNDSHK LKNFISEIML NMSMISWPND 

        70         80         90        100        110        120 
ASRIVYCRRH LLNPAAQWAN DFVQEQGILE ITFDTFIQGL YQHFYKPPDI NKIFNAITQL 

       130        140        150        160        170        180 
SEAKLGIERL NQRFRKIWDR MPPDFMTEKA AIMTYTRLLT KETYNIVRMH KPETLKDAME 

       190        200        210        220        230        240 
EAYQTTALTE RFFPGFELDA DGDTIIGATT HLQEEYDSDY DSEDNLTQNG YVHTVRTRRS 

       250        260        270        280        290        300 
YNKPMSNHRN RRNNNPSREE CIKNRLCFYC KKEGHRLNEC RARKAVLTDL ELESKDQQTP 

       310        320        330        340        350        360 
FIKTLPIVHY IAIPEMDNTA EKTIKIQNTK VKTLFDSGSP TSFIRRDIVE LLKYEIYETP 

       370        380        390        400        410        420 
PLRFRGFVAT KSAVTSEAVT IDLKINDLHI TLAAYILDNM DYQLLIGNPI LRRYPKILHT 

       430        440        450        460        470        480 
VLNTRESPDS LKPKTYRSET VNNVRTYSAG NRGNPRNIKL SFAPTILEAT DPKSAGNRGD 

       490        500        510        520        530        540 
SRTKTLSLAT TTPAAIDPLT TLDNPGSTQS TFAQFPIPEE ASILEEDGKY SNVVSTIQSV 

       550        560        570        580        590        600 
EPNATDHSNK DTFCTLPVWL QQKYREIIRN DLPPRPADIN NIPVKHDIEI KPGARLPRLQ 

       610        620        630        640        650        660 
PYHVTEKNEQ EINKIVQKLL DNKFIVPSKS PCSSPVVLVP KKDGTFRLCV DYRTLNKATI 

       670        680        690        700        710        720 
SDPFPLPRID NLLSRIGNAQ IFTTLDLHSG YHQIPMEPKD RYKTAFVTPS GKYEYTVMPF 

       730        740        750        760        770        780 
GLVNAPSTFA RYMADTFRDL RFVNVYLDDI LIFSESPEEH WKHLDTVLER LKNENLIVKK 

       790        800        810        820        830        840 
KKCKFASEET EFLGYSIGIQ KIAPLQHKCA AIRDFPTPKT VKQAQRFLGM INYYRRFIPN 

       850        860        870        880        890        900 
CSKIAQPIQL FICDKSQWTE KQDKAIDKLK DALCNSPVLV PFNNKANYRL TTDASKDGIG 

       910        920        930        940        950        960 
AVLEEVDNKN KLVGVVGYFS KSLESAQKNY PAGELELLGI IKALHHFRYM LHGKHFTLRT 

       970        980        990       1000       1010       1020 
DHISLLSLQN KNEPARRVQR WLDDLATYDF TLEYLAGPKN VVADAISRAV YTITPETSRP 

      1030       1040       1050       1060       1070       1080 
IDTESWKSYY KSDPLCSAVL IHMKELTQHN VTPEDMSAFR SYQKKLELSE TFRKNYSLED 

      1090       1100       1110       1120       1130       1140 
EMIYYQDRLV VPIKQQNAVM RLYHDHTLFG GHFGVTVTLA KISPIYYWPK LQHSIIQYIR 

      1150       1160       1170       1180       1190       1200 
TCVQCQLIKS HRPRLHGLLQ PLPIAEGRWL DISMDFVTGL PPTSNNLNMI LVVVDRFSKR 

      1210       1220       1230       1240       1250       1260 
AHFIATRKTL DATQLIDLLF RYIFSYHGFP RTITSDRDVR MTADKYQELT KRLGIKSTMS 

      1270       1280       1290       1300       1310       1320 
SANHPQTDGQ SERTIQTLNR LLRAYASTNI QNWHVYLPQI EFVYNSTPTR TLGKSPFEID 

      1330       1340       1350       1360       1370       1380 
LGYLPNTPAI KSDDEVNARS FTAVELAKHL KALTIQTKEQ LEHAQIEMET NNNQRRKPLL 

      1390       1400       1410       1420       1430       1440 
LNIGDHVLVH RDAYFKKGAY MKVQQIYVGP FRVVKKINDN AYELDLNSHK KKHRVINVQF 

      1450       1460       1470       1480       1490       1500 
LKKFVYRPDA YPKNKPISST ERIKRAHEVT ALIGIDTTHK TYLCHMQDVD PTLSVEYSEA 

      1510       1520       1530       1540 
EFCQIPERTR RSILANFRQL YETQDNPERE EDVVSQNEIC QYDNTSP 

« Hide

Isoform Transposon Ty3-G Gag polyprotein [UniParc].

See Q12173.

References

« Hide 'large scale' references
[1]"Characterization of a transpositionally active Ty3 element and identification of the Ty3 integrase protein."
Hansen L.J., Sandmeyer S.B.
J. Virol. 64:2599-2607(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: AB950.
[2]"The sequence of a 23.4 kb segment on the right arm of chromosome VII from Saccharomyces cerevisiae reveals CLB6, SPT6, RP28A and NUP57 genes, a Ty3 element and 11 new open reading frames."
Hansen M., Albers M., Backes U., Coblenz A., Leuther H., Neu R., Schreer A., Schaefer B., Zimmermann M., Wolf K.
Yeast 12:1273-1277(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"A yeast sigma composite element, TY3, has properties of a retrotransposon."
Clark D.J., Bilanchone V.W., Haywood L.J., Dildine S.L., Sandmeyer S.B.
J. Biol. Chem. 263:1413-1423(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[6]"Ty3 GAG3 and POL3 genes encode the components of intracellular particles."
Hansen L.J., Chalker D.L., Orlinsky K.J., Sandmeyer S.B.
J. Virol. 66:1414-1424(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF REVERSE TRANSCRIPTASE, SUBCELLULAR LOCATION.
[7]"A novel programed frameshift expresses the POL3 gene of retrotransposon Ty3 of yeast: frameshifting without tRNA slippage."
Farabaugh P.J., Zhao H., Vimaladithan A.
Cell 74:93-103(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: RIBOSOMAL FRAMESHIFT SITE.
[8]Erratum
Farabaugh P.J., Zhao H., Vimaladithan A.
Cell 75:826-826(1993)
[9]"Proteolytic processing of Ty3 proteins is required for transposition."
Kirchner J., Sandmeyer S.B.
J. Virol. 67:19-28(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING, CLEAVAGE SITES.
[10]"The Cys-His motif of Ty3 NC can be contributed by Gag3 or Gag3-Pol3 polyproteins."
Orlinsky K.J., Sandmeyer S.B.
J. Virol. 68:4152-4166(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF NUCLEOCAPSID, MUTAGENESIS OF CYS-267 AND HIS-275.
[11]"Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence."
Kim J.M., Vanguri S., Boeke J.D., Gabriel A., Voytas D.F.
Genome Res. 8:464-478(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[12]"Characterization of active reverse transcriptase and nucleoprotein complexes of the yeast retrotransposon Ty3 in vitro."
Cristofari G., Gabus C., Ficheux D., Bona M., Le Grice S.F.J., Darlix J.-L.
J. Biol. Chem. 274:36643-36648(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF REVERSE TRANSCRIPTASE.
[13]"Ten-kilodalton domain in Ty3 Gag3-Pol3p between PR and RT is dispensable for Ty3 transposition."
Claypool J.A., Malik H.S., Eickbush T.H., Sandmeyer S.B.
J. Virol. 75:1557-1560(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF PEPTIDE J.
[14]"Happy together: the life and times of Ty retrotransposons and their hosts."
Lesage P., Todeschini A.L.
Cytogenet. Genome Res. 110:70-90(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[15]"Investigation by atomic force microscopy of the structure of Ty3 retrotransposon particles."
Kuznetsov Y.G., Zhang M., Menees T.M., McPherson A., Sandmeyer S.B.
J. Virol. 79:8032-8045(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, CLEAVAGE SITE GLY-207-208-ALA, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34549 Genomic DNA. Translation: AAA98435.1. Sequence problems.
Z72894 Genomic DNA. Translation: CAA97115.1. Sequence problems.
Z72895 Genomic DNA. Translation: CAA97117.1. Sequence problems.
M18353 Genomic DNA. Translation: AAA66936.1.
BK006941 Genomic DNA. Translation: DAA08202.1. Sequence problems.
PIRS22875.
S69842.
RefSeqNP_011624.1. NM_001184381.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4OL8X-ray3.10A/B/E/F536-1011[»]
ProteinModelPortalQ99315.
SMRQ99315. Positions 550-1011, 1111-1333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33356. 2 interactions.

Protein family/group databases

MEROPSA02.022.

Proteomic databases

PaxDbQ99315.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID853006.
KEGGsce:YGR109W-B.

Organism-specific databases

SGDS000007347. YGR109W-B.

Phylogenomic databases

eggNOGCOG2801.
HOGENOMHOG000172599.
KOK07497.
OrthoDBEOG7HF1TD.

Gene expression databases

GenevestigatorQ99315.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
InterProIPR001584. Integrase_cat-core.
IPR024650. Peptidase_A2B.
IPR021109. Peptidase_aspartic_dom.
IPR005162. Retrotrans_gag_dom.
IPR012337. RNaseH-like_dom.
IPR000477. RT_dom.
IPR001878. Znf_CCHC.
[Graphical view]
PfamPF12384. Peptidase_A2B. 1 hit.
PF03732. Retrotrans_gag. 1 hit.
PF00665. rve. 1 hit.
PF00078. RVT_1. 1 hit.
[Graphical view]
SMARTSM00343. ZnF_C2HC. 1 hit.
[Graphical view]
SUPFAMSSF50630. SSF50630. 1 hit.
SSF53098. SSF53098. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEPS50994. INTEGRASE. 1 hit.
PS50878. RT_POL. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972854.
PMAP-CutDBQ99315.

Entry information

Entry nameYG31B_YEAST
AccessionPrimary (citable) accession number: Q99315
Secondary accession number(s): D6VUP1, Q07096
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: March 6, 2007
Last modified: July 9, 2014
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references