Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-928306-01040
Entry Name
UniProt Accession
Theoretical PI
9.17
Molecular Weight
194840.6
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Integrase p46
Protein Synonyms/Alias
Pr180gag-pol; MA; pp12; CA; NC-pol; PR; 3.4.23.-; RT; 2.7.7.49; 2.7.7.7; 3.1.26.4; IN;
Gene Name
gag-pol
Gene Synonyms/Alias
Created Date
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGQTVTTPL
[1]
N-Myristoylation
Organism
Moloney murine leukemia virus (isolate Shinnick) (MoMLV)
NCBI Taxa ID
928306
Reference
[1] Henderson LE, Krutzsch HC, Oroszlan S. Myristyl amino-terminal acylation ofmurine retrovirus proteins: an unusual post-translational proteins modification. Proc Natl Acad Sci U S A. 1983 Jan;80(2):339-43.[PMID:6340098]
Functional Description
Gag-Pol polyprotein plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably link the viral protein to the host ESCRT pathway and facilitate release.Capsid protein p30 forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex.
Sequence Annotation
Domain: 560 631 Peptidase A2.
Domain: 741 932 Reverse transcriptase.
Domain: 1174 1320 RNase H.
Domain: 1444 1602 Integrase catalytic.
Motif: 111 114 PTAP/PSAP motif.
Motif: 130 134 LYPX(n)L motif.
Motif: 162 165 PPXY motif.
Active site: 566 566 Protease; shared with dimeric partner.
Metal binding site: 809 809 Magnesium; catalytic; for reversetranscriptase activity.
Metal binding site: 883 883 Magnesium; catalytic; for reversetranscriptase activity.
Metal binding site: 884 884 Magnesium; catalytic; for reversetranscriptase activity.
Metal binding site: 1183 1183 Magnesium; for RNase H activity.
Metal binding site: 1221 1221 Magnesium; for RNase H activity.
Metal binding site: 1242 1242 Magnesium; for RNase H activity.
Metal binding site: 1312 1312 Magnesium; for RNase H activity.
Metal binding site: 1455 1455 Magnesium; catalytic; for integraseactivity.
Metal binding site: 1514 1514 Magnesium; catalytic; for integraseactivity.
Functional site: 131 132 Cleavage; by viral protease p14.
Functional site: 215 216 Cleavage; by viral protease p14.
Functional site: 478 479 Cleavage; by viral protease p14.
Functional site: 534 535 Cleavage; by viral protease p14.
Functional site: 659 660 Cleavage; by viral protease p14.
Functional site: 1330 1331 Cleavage; by viral protease p14.
Modified residue: 192 192 Phosphoserine; by host.
Protein Length
1738 AA.
Protein Sequence
(Canonical)
MGQTVTTPLS LTLGHWKDVE RIAHNQSVDV KKRRWVTFCS AEWPTFNVGW PRDGTFNRDL  60
ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF VHPKPPPPLP PSAPSLPLEP  120
PRSTPPRSSL YPALTPSLGA KPKPQVLSDS GGPLIDLLTE DPPPYRDPRP PPSDRDGNGG  180
EATPAGEAPD PSPMASRLRG RREPPVADST TSQAFPLRAG GNGQLQYWPF SSSDLYNWKN  240
NNPSFSEDPG KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR  300
PTQLPNEVDA AFPLERPDWD YTTQAGRNHL VHYRQLLLAG LQNAGRSPTN LAKVKGITQG  360
PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ SAPDIGRKLE RLEDLKNKTL  420
GDLVREAEKI FNKRETPEER EERIRRETEE KEERRRTEDE QKEKERDRRR HREMSKLLAT  480
VVSGQKQDRQ GGERRRSQLD RDQCAYCKEK GHWAKDCPKK PRGPRGPRPQ TSLLTLDDGG  540
GQGQEPPPEP RITLKVGGQP VTFLVDTGAQ HSVLTQNPGP LSDKSAWVQG ATGGKRYRWT  600
TDRKVHLATG KVTHSFLHVP DCPYPLLGRD LLTKLKAQIH FEGSGAQVMG PMGQPLQVLT  660
LNIEDEHRLH ETSKEPDVSL GSTWLSDFPQ AWAETGGMGL AVRQAPLIIP LKATSTPVSI  720
KQYPMSQEAR LGIKPHIQRL LDQGILVPCQ SPWNTPLLPV KKPGTNDYRP VQDLREVNKR  780
VEDIHPTVPN PYNLLSGLPP SHQWYTVLDL KDAFFCLRLH PTSQPLFAFE WRDPEMGISG  840
QLTWTRLPQG FKNSPTLFDE ALHRDLADFR IQHPDLILLQ YVDDLLLAAT SELDCQQGTR  900
ALLQTLGNLG YRASAKKAQI CQKQVKYLGY LLKEGQRWLT EARKETVMGQ PTPKTPRQLR  960
EFLGTAGFCR LWIPGFAEMA APLYPLTKTG TLFNWGPDQQ KAYQEIKQAL LTAPALGLPD  1020
LTKPFELFVD EKQGYAKGVL TQKLGPWRRP VAYLSKKLDP VAAGWPPCLR MVAAIAVLTK  1080
DAGKLTMGQP LVILAPHAVE ALVKQPPDRW LSNARMTHYQ ALLLDTDRVQ FGPVVALNPA  1140
TLLPLPEEGL QHNCLDILAE AHGTRPDLTD QPLPDADHTW YTDGSSLLQE GQRKAGAAVT  1200
TETEVIWAKA LPAGTSAQRA ELIALTQALK MAEGKKLNVY TDSRYAFATA HIHGEIYRRR  1260
GLLTSEGKEI KNKDEILALL KALFLPKRLS IIHCPGHQKG HSAEARGNRM ADQAARKAAI  1320
TETPDTSTLL IENSSPYTSE HFHYTVTDIK DLTKLGAIYD KTKKYWVYQG KPVMPDQFTF  1380
ELLDFLHQLT HLSFSKMKAL LERSHSPYYM LNRDRTLKNI TETCKACAQV NASKSAVKQG  1440
TRVRGHRPGT HWEIDFTEIK PGLYGYKYLL VFIDTFSGWI EAFPTKKETA KVVTKKLLEE  1500
IFPRFGMPQV LGTDNGPAFV SKVSQTVADL LGIDWKLHCA YRPQSSGQVE RMNRTIKETL  1560
TKLTLATGSR DWVLLLPLAL YRARNTPGPH GLTPYEILYG APPPLVNFPD PDMTRVTNSP  1620
SLQAHLQALY LVQHEVWRPL AAAYQEQLDR PVVPHPYRVG DTVWVRRHQT KNLEPRWKGP  1680
YTVLLTTPTA LKVDGIAAWI HAAHVKAADP GGGPSSRLTW RVQRSQNPLK IRLTREAP    1738
FASTA
(Canonical)
>LipidDB-928306-01040|P03355
MGQTVTTPLSLTLGHWKDVERIAHNQSVDVKKRRWVTFCSAEWPTFNVGWPRDGTFNRDL
ITQVKIKVFSPGPHGHPDQVPYIVTWEALAFDPPPWVKPFVHPKPPPPLPPSAPSLPLEP
PRSTPPRSSLYPALTPSLGAKPKPQVLSDSGGPLIDLLTEDPPPYRDPRPPPSDRDGNGG
EATPAGEAPDPSPMASRLRGRREPPVADSTTSQAFPLRAGGNGQLQYWPFSSSDLYNWKN
NNPSFSEDPGKLTALIESVLITHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGDDGR
PTQLPNEVDAAFPLERPDWDYTTQAGRNHLVHYRQLLLAGLQNAGRSPTNLAKVKGITQG
PNESPSAFLERLKEAYRRYTPYDPEDPGQETNVSMSFIWQSAPDIGRKLERLEDLKNKTL
GDLVREAEKIFNKRETPEEREERIRRETEEKEERRRTEDEQKEKERDRRRHREMSKLLAT
VVSGQKQDRQGGERRRSQLDRDQCAYCKEKGHWAKDCPKKPRGPRGPRPQTSLLTLDDGG
GQGQEPPPEPRITLKVGGQPVTFLVDTGAQHSVLTQNPGPLSDKSAWVQGATGGKRYRWT
TDRKVHLATGKVTHSFLHVPDCPYPLLGRDLLTKLKAQIHFEGSGAQVMGPMGQPLQVLT
LNIEDEHRLHETSKEPDVSLGSTWLSDFPQAWAETGGMGLAVRQAPLIIPLKATSTPVSI
KQYPMSQEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKPGTNDYRPVQDLREVNKR
VEDIHPTVPNPYNLLSGLPPSHQWYTVLDLKDAFFCLRLHPTSQPLFAFEWRDPEMGISG
QLTWTRLPQGFKNSPTLFDEALHRDLADFRIQHPDLILLQYVDDLLLAATSELDCQQGTR
ALLQTLGNLGYRASAKKAQICQKQVKYLGYLLKEGQRWLTEARKETVMGQPTPKTPRQLR
EFLGTAGFCRLWIPGFAEMAAPLYPLTKTGTLFNWGPDQQKAYQEIKQALLTAPALGLPD
LTKPFELFVDEKQGYAKGVLTQKLGPWRRPVAYLSKKLDPVAAGWPPCLRMVAAIAVLTK
DAGKLTMGQPLVILAPHAVEALVKQPPDRWLSNARMTHYQALLLDTDRVQFGPVVALNPA
TLLPLPEEGLQHNCLDILAEAHGTRPDLTDQPLPDADHTWYTDGSSLLQEGQRKAGAAVT
TETEVIWAKALPAGTSAQRAELIALTQALKMAEGKKLNVYTDSRYAFATAHIHGEIYRRR
GLLTSEGKEIKNKDEILALLKALFLPKRLSIIHCPGHQKGHSAEARGNRMADQAARKAAI
TETPDTSTLLIENSSPYTSEHFHYTVTDIKDLTKLGAIYDKTKKYWVYQGKPVMPDQFTF
ELLDFLHQLTHLSFSKMKALLERSHSPYYMLNRDRTLKNITETCKACAQVNASKSAVKQG
TRVRGHRPGTHWEIDFTEIKPGLYGYKYLLVFIDTFSGWIEAFPTKKETAKVVTKKLLEE
IFPRFGMPQVLGTDNGPAFVSKVSQTVADLLGIDWKLHCAYRPQSSGQVERMNRTIKETL
TKLTLATGSRDWVLLLPLALYRARNTPGPHGLTPYEILYGAPPPLVNFPDPDMTRVTNSP
SLQAHLQALYLVQHEVWRPLAAAYQEQLDRPVVPHPYRVGDTVWVRRHQTKNLEPRWKGP
YTVLLTTPTALKVDGIAAWIHAAHVKAADPGGGPSSRLTWRVQRSQNPLKIRLTREAP
Gene Ontology
GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW
GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW
GO:0003677; F:DNA binding; IEA:UniProtKB-KW
GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW
GO:0003723; F:RNA binding; IEA:UniProtKB-KW
GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW
GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC
GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW
GO:0008270; F:zinc ion binding; IEA:InterPro
GO:0015074; P:DNA integration; IEA:UniProtKB-KW
GO:0006310; P:DNA recombination; IEA:UniProtKB-KW
GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW
GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW
GO:0019068; P:virion assembly; IEA:InterPro
Interpro
InterPro; IPR001969; Aspartic_peptidase_AS
InterPro; IPR000840; G_retro_matrix_N
InterPro; IPR002079; Gag_p12
InterPro; IPR003036; Gag_P30
InterPro; IPR001584; Integrase_cat-core
InterPro; IPR018061; Pept_A2A_retrovirus_sg
InterPro; IPR001995; Peptidase_A2_cat
InterPro; IPR021109; Peptidase_aspartic_dom
InterPro; IPR008919; Retrov_capsid_N
InterPro; IPR010999; Retrovr_matrix_N
InterPro; IPR012337; RNaseH-like_dom
InterPro; IPR002156; RNaseH_domain
InterPro; IPR000477; RT_dom
InterPro; IPR001878; Znf_CCHC
Pfam
Pfam; PF01140; Gag_MA;
Pfam; PF01141; Gag_p12;
Pfam; PF02093; Gag_p30;
Pfam; PF00075; RNase_H;
Pfam; PF00665; rve;
Pfam; PF00077; RVP;
Pfam; PF00078; RVT_1;
SMART
SMART; SM00343; ZnF_C2HC;
PROSITE
PROSITE; PS50175; ASP_PROT_RETROV;
PROSITE; PS00141; ASP_PROTEASE;
PROSITE; PS50994; INTEGRASE;
PROSITE; PS50879; RNASE_H;
PROSITE; PS50878; RT_POL;
PROSITE; PS50158; ZF_CCHC;
PRINTS