P04584

PR
Gene name
gag-pol
Protein name
Gag-Pol polyprotein
Names
Pr160Gag-Pol
Species
Human immunodeficiency virus type 2 subtype A (isolate ROD) (HIV-2)
KEGG Pathway
EC number
2.7.7.7: Nucleotidyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

417-526 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

24 structures for P04584

Entry ID Method Resolution Chain Position Source
1E0E NMR - A/B 1172-1226 PDB
1HII X-ray 230 A A/B 514-612 PDB
1HSH X-ray 190 A A/B/C/D 514-612 PDB
1HSI X-ray 250 A A/B 514-612 PDB
1IDA X-ray 170 A A/B 514-612 PDB
1IDB X-ray 220 A A/B 514-612 PDB
1IVP X-ray 250 A A/B 514-612 PDB
1IVQ X-ray 260 A A/B 514-612 PDB
1JLD X-ray 250 A A/B 514-612 PDB
1MU2 X-ray 235 A PDB
2HPE X-ray 200 A A/B 514-612 PDB
2HPF X-ray 300 A A/B 514-612 PDB
2K4E NMR - A 2-135 PDB
2K4H NMR - A 2-135 PDB
2K4I NMR - A 2-135 PDB
2MIP X-ray 220 A A/B/C/D 514-612 PDB
3EBZ X-ray 120 A A/B 514-612 PDB
3EC0 X-ray 118 A A/B 514-612 PDB
3ECG X-ray 118 A A/B 514-612 PDB
3F9K X-ray 320 A A/B/E/F/I/J/M/N/Q/R/U/V/Y/Z/c/d/g/h/k/l/o/p/s/t 1173-1380 PDB
3UPJ X-ray 250 A A/B 514-612 PDB
4UPJ X-ray 190 A A/B 514-612 PDB
5UPJ X-ray 230 A A/B 514-612 PDB
6UPJ X-ray 234 A A/B 514-612 PDB

No variants for P04584

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P04584

No associated diseases with P04584

16 regional properties for P04584

Type Name Position InterPro Accession
domain Immunodeficiency lentiviral matrix, N-terminal 2 - 123 IPR000071
domain Reverse transcriptase domain 656 - 846 IPR000477
domain Retroviral nucleocapsid Gag protein p24, N-terminal 146 - 271 IPR000721
domain Integrase, C-terminal, retroviral 1394 - 1441 IPR001037
domain Integrase, catalytic core 1224 - 1375 IPR001584
domain Zinc finger, CCHC-type 390 - 406 IPR001878-1
domain Zinc finger, CCHC-type 411 - 427 IPR001878-2
active_site Aspartic peptidase, active site 535 - 546 IPR001969
domain Peptidase A2A, retrovirus, catalytic 533 - 602 IPR001995
domain Ribonuclease H domain 1045 - 1168 IPR002156
domain Integrase, N-terminal zinc-binding domain 1174 - 1216 IPR003308
domain Reverse transcriptase connection 930 - 1030 IPR010659
domain Reverse transcriptase thumb 853 - 916 IPR010661
domain Retropepsins 519 - 610 IPR018061
domain Retropepsin-like catalytic domain 524 - 604 IPR034170
domain Retroviral nucleocapsid Gag protein p24, C-terminal domain 278 - 351 IPR045345

Functions

Description
EC Number 2.7.7.7 Nucleotidyltransferases
Subcellular Localization
  • [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor
  • Host endosome, host multivesicular body
  • These locations are linked to virus assembly sites
  • The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
host cell nucleus A membrane-bounded organelle as it is found in the host cell in which chromosomes are housed and replicated. The host is defined as the larger of the organisms involved in a symbiotic interaction.
host cell plasma membrane The plasma membrane surrounding a host cell.
host multivesicular body A late endosome in which regions of the limiting host cell endosomal membrane invaginate to form internal vesicles; host membrane proteins that enter the internal vesicles are sequestered from the host cytoplasm.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
viral nucleocapsid The complete protein-nucleic acid complex that is the packaged form of the genome in a virus particle.
virion membrane The lipid bilayer surrounding a virion.

10 GO annotations of molecular function

Name Definition
aspartic-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA-directed DNA polymerase activity Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a DNA template and a 3'hydroxyl group.
exoribonuclease H activity Catalysis of the exonucleolytic cleavage of RNA to 5'-phosphomonoester oligonucleotides in both 5' to 3' and 3' to 5' directions.
lipid binding Binding to a lipid.
RNA binding Binding to an RNA molecule or a portion thereof.
RNA-directed DNA polymerase activity Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). Catalyzes RNA-template-directed extension of the 3'- end of a DNA strand by one deoxynucleotide at a time.
RNA-DNA hybrid ribonuclease activity Catalysis of the endonucleolytic cleavage of RNA in RNA-DNA hybrids to 5'-phosphomonoesters.
structural molecule activity The action of a molecule that contributes to the structural integrity of a complex or its assembly within or outside a cell.
zinc ion binding Binding to a zinc ion (Zn).

8 GO annotations of biological process

Name Definition
DNA integration The process in which a DNA segment is incorporated into another, usually larger, DNA molecule such as a chromosome.
DNA recombination Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction.
establishment of integrated proviral latency A process by which the virus integrates into the host genome and establishes as a stable provirus or prophage.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
suppression by virus of host gene expression Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of gene expression in the host organism. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein. Some protein processing events may be included when they are required to form an active form of a product from an inactive precursor form.
viral entry into host cell The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm.
viral genome integration into host DNA The insertion into a host genome of viral DNA, usually by the action of an integrase enzyme. Once integrated, the provirus persists in the host cell and serves as a template for the transcription of viral genes and replication of the viral genome, leading to the production of new viruses.
viral penetration into host nucleus The crossing by the virus of the host nuclear membrane, either as naked viral genome or for small viruses as an intact capsid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGARNSVLRG KKADELERIR LRPGGKKKYR LKHIVWAANK LDRFGLAESL LESKEGCQKI
70 80 90 100 110 120
LTVLDPMVPT GSENLKSLFN TVCVIWCIHA EEKVKDTEGA KQIVRRHLVA ETGTAEKMPS
130 140 150 160 170 180
TSRPTAPSSE KGGNYPVQHV GGNYTHIPLS PRTLNAWVKL VEEKKFGAEV VPGFQALSEG
190 200 210 220 230 240
CTPYDINQML NCVGDHQAAM QIIREIINEE AAEWDVQHPI PGPLPAGQLR EPRGSDIAGT
250 260 270 280 290 300
TSTVEEQIQW MFRPQNPVPV GNIYRRWIQI GLQKCVRMYN PTNILDIKQG PKEPFQSYVD
310 320 330 340 350 360
RFYKSLRAEQ TDPAVKNWMT QTLLVQNANP DCKLVLKGLG MNPTLEEMLT ACQGVGGPGQ
370 380 390 400 410 420
KARLMAEALK EVIGPAPIPF AAAQQRKAFK CWNCGKEGHS ARQCRAPRRQ GCWKCGKPGH
430 440 450 460 470 480
IMTNCPDRQA GFLRTGPLGK EAPQLPRGPS SAGADTNSTP SGSSSGSTGE IYAAREKTER
490 500 510 520 530 540
AERETIQGSD RGLTAPRAGG DTIQGATNRG LAAPQFSLWK RPVVTAYIEG QPVEVLLDTG
550 560 570 580 590 600
ADDSIVAGIE LGNNYSPKIV GGIGGFINTK EYKNVEIEVL NKKVRATIMT GDTPINIFGR
610 620 630 640 650 660
NILTALGMSL NLPVAKVEPI KIMLKPGKDG PKLRQWPLTK EKIEALKEIC EKMEKEGQLE
670 680 690 700 710 720
EAPPTNPYNT PTFAIKKKDK NKWRMLIDFR ELNKVTQDFT EIQLGIPHPA GLAKKRRITV
730 740 750 760 770 780
LDVGDAYFSI PLHEDFRPYT AFTLPSVNNA EPGKRYIYKV LPQGWKGSPA IFQHTMRQVL
790 800 810 820 830 840
EPFRKANKDV IIIQYMDDIL IASDRTDLEH DRVVLQLKEL LNGLGFSTPD EKFQKDPPYH
850 860 870 880 890 900
WMGYELWPTK WKLQKIQLPQ KEIWTVNDIQ KLVGVLNWAA QLYPGIKTKH LCRLIRGKMT
910 920 930 940 950 960
LTEEVQWTEL AEAELEENRI ILSQEQEGHY YQEEKELEAT VQKDQENQWT YKIHQEEKIL
970 980 990 1000 1010 1020
KVGKYAKVKN THTNGIRLLA QVVQKIGKEA LVIWGRIPKF HLPVEREIWE QWWDNYWQVT
1030 1040 1050 1060 1070 1080
WIPDWDFVST PPLVRLAFNL VGDPIPGAET FYTDGSCNRQ SKEGKAGYVT DRGKDKVKKL
1090 1100 1110 1120 1130 1140
EQTTNQQAEL EAFAMALTDS GPKVNIIVDS QYVMGISASQ PTESESKIVN QIIEEMIKKE
1150 1160 1170 1180 1190 1200
AIYVAWVPAH KGIGGNQEVD HLVSQGIRQV LFLEKIEPAQ EEHEKYHSNV KELSHKFGIP
1210 1220 1230 1240 1250 1260
NLVARQIVNS CAQCQQKGEA IHGQVNAELG TWQMDCTHLE GKIIIVAVHV ASGFIEAEVI
1270 1280 1290 1300 1310 1320
PQESGRQTAL FLLKLASRWP ITHLHTDNGA NFTSQEVKMV AWWIGIEQSF GVPYNPQSQG
1330 1340 1350 1360 1370 1380
VVEAMNHHLK NQISRIREQA NTIETIVLMA IHCMNFKRRG GIGDMTPSER LINMITTEQE
1390 1400 1410 1420 1430 1440
IQFLQAKNSK LKDFRVYFRE GRDQLWKGPG ELLWKGEGAV LVKVGTDIKI IPRRKAKIIR
1450 1460
DYGGRQEMDS GSHLEGARED GEMA