Q99315 (YG31B_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1547 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Capsid maturation DNA integration DNA recombination
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Ribosomal frameshifting
Domain	Zinc-finger
Ligand	ATP-binding DNA-binding Magnesium Metal-binding Nucleotide-binding RNA-binding Zinc
Molecular function	Aspartyl protease DNA-directed DNA polymerase Endonuclease Hydrolase Nuclease Nucleotidyltransferase Protease RNA-directed DNA polymerase Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome Transposable element
Gene Ontology (GO)
Biological_process	DNA integration Inferred from electronic annotation. Source: UniProtKB-KW DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW RNA-dependent DNA replication Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW transposition, RNA-mediated Inferred from sequence or structural similarity Ref.11. Source: SGD viral procapsid maturation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell retrotransposon nucleocapsid Inferred from sequence or structural similarity Ref.11. Source: SGD
Molecular_function	ATP 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-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 H activity Inferred from electronic annotation. Source: EC 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.15
	Chain	2 – 1547	1546	Transposon Ty3-G Gag-Pol polyprotein		PRO_0000279356
	Chain	2 – 207	206	Capsid protein		PRO_0000279357
	Peptide	208 – 233	26	Spacer peptide p3		PRO_0000279358
	Chain	234 – 309	76	Nucleocapsid protein p11		PRO_0000279359
	Chain	310 – 442	133	Ty3 protease		PRO_0000279360
	Peptide	443 – 535	93	Spacer peptide J Potential		PRO_0000279361
	Chain	536 – 1011	476	Reverse transcriptase/ribonuclease H		PRO_0000279362
	Chain	1012 – 1547	536	Integrase p61		PRO_0000279363
	Chain	1038 – 1547	510	Integrase p58		PRO_0000279364
Regions
	Domain	620 – 797	178	Reverse transcriptase
	Domain	893 – 1011	119	RNase H Ty3/gyspy-type
	Domain	1159 – 1324	166	Integrase catalytic
	Zinc finger	265 – 282	18	CCHC-type
	Region	1106 – 1145	40	Integrase-type zinc finger-like
Sites
	Active site	336	1	For protease activity; shared with dimeric partner By similarity
	Metal binding	686	1	Magnesium; catalytic; for reverse transcriptase activity By similarity
	Metal binding	748	1	Magnesium; catalytic; for reverse transcriptase activity By similarity
	Metal binding	749	1	Magnesium; catalytic; for reverse transcriptase activity By similarity
	Metal binding	893	1	Magnesium; catalytic; for RNase H activity By similarity
	Metal binding	936	1	Magnesium; catalytic; for RNase H activity By similarity
	Metal binding	961	1	Magnesium; catalytic; for RNase H activity By similarity
	Metal binding	1175	1	Magnesium; catalytic; for integrase activity By similarity
	Metal binding	1236	1	Magnesium; catalytic; for integrase activity By similarity
	Site	207 – 208	2	Cleavage; by Ty3 protease
	Site	233 – 234	2	Cleavage; by Ty3 protease
	Site	309 – 310	2	Cleavage; by Ty3 protease
	Site	442 – 443	2	Cleavage; by Ty3 protease Potential
	Site	535 – 536	2	Cleavage; by Ty3 protease
	Site	1011 – 1012	2	Cleavage; by Ty3 protease
	Site	1037 – 1038	2	Cleavage; by Ty3 protease; partial
Experimental info
	Mutagenesis	267	1	C → S: Reduces level of VLP formation and maturation. Ref.10
	Mutagenesis	275	1	H → Q: Reduces level of VLP formation and maturation. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	Isoform Transposon Ty3-G Gag-Pol polyprotein [UniParc]. Last modified March 6, 2007. Version 3. Checksum: 0E327D91E0575F78	FASTA	1,547	178,307
	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
	Isoform Transposon Ty3-G Gag polyprotein [UniParc]. See Q12173.		–	–

References

	« Hide 'large scale' referencesShow '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. , 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 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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, 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.
PIR	S22875. S69842.
RefSeq	NP_011624.1. NM_001184381.1.
3D structure databases
ProteinModelPortal	Q99315.
SMR	Q99315. Positions 582-931, 1111-1333.
ModBase	Search...
Protein family/group databases
MEROPS	A02.022.
Proteomic databases
PaxDb	Q99315.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	853006.
KEGG	sce:YGR109W-B.
Organism-specific databases
SGD	S000007347. YGR109W-B.
Phylogenomic databases
eggNOG	COG2801.
HOGENOM	HOG000172599.
KO	K07497.
OrthoDB	EOG44N213.
Gene expression databases
Genevestigator	Q99315.
Family and domain databases
InterPro	IPR001584. Integrase_cat-core. IPR024650. Peptidase_A2B. IPR021109. Peptidase_aspartic. IPR005162. Retrotrans_gag. IPR012337. RNaseH-like_dom. IPR000477. RVT. IPR001878. Znf_CCHC. [Graphical view]
Pfam	PF12384. Peptidase_A2B. 1 hit. PF03732. Retrotrans_gag. 1 hit. PF00665. rve. 1 hit. PF00078. RVT_1. 1 hit. [Graphical view]
SMART	SM00343. ZnF_C2HC. 1 hit. [Graphical view]
SUPFAM	SSF50630. Pept_Aspartic. 1 hit. SSF53098. RNaseH_fold. 1 hit.
PROSITE	PS50994. INTEGRASE. 1 hit. PS50878. RT_POL. 1 hit. PS50158. ZF_CCHC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	972854.
PMAP-CutDB	Q99315.

Entry information

Entry name

YG31B_YEAST

Accession

Primary (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:	May 1, 2013
This is version 92 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program