Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

0 structures for P05960

Entry ID Method Resolution Chain Position Source

No variants for P05960

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P05960

No associated diseases with P05960

8 regional properties for P05960

Type Name Position InterPro Accession
domain Immunodeficiency lentiviral matrix, N-terminal 2 - 132 IPR000071
domain Retroviral nucleocapsid Gag protein p24, N-terminal 144 - 250 IPR000721
domain Zinc finger, CCHC-type 391 - 407 IPR001878-1
domain Zinc finger, CCHC-type 412 - 428 IPR001878-2
active_site Aspartic peptidase, active site 510 - 521 IPR001969
domain Peptidase A2A, retrovirus, catalytic 508 - 550 IPR001995
domain Retropepsins 494 - 549 IPR018061
domain Retroviral nucleocapsid Gag protein p24, C-terminal domain 277 - 349 IPR045345

Functions

Description
EC Number 3.4.23.16 Aspartic endopeptidases
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.

5 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.
lipid binding Binding to a lipid.
RNA binding Binding to an RNA molecule or a portion thereof.
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).

2 GO annotations of biological process

Name Definition
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGARASVLSG GELDRWEKIR LRPGGKKQYR LKHIVWASRK LERFAVNPGL LETSKGCRQI
70 80 90 100 110 120
LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIEVRDTKEA LDKIEEEQNK SKKKAQQAAA
130 140 150 160 170 180
DTGNSSQVSQ NYPIVQNLQG QMVHQAISPR TLNAWVKVIE EKAFSPEVIP MFAALSEGAT
190 200 210 220 230 240
PQDLNTMLNT VGGHQAAMQM LKETINEEAA EWDRLHPVHA GPIAPGQMRE PRGSDIAGTT
250 260 270 280 290 300
STLQEQIGWM TNNPPTPVGE IYKRWIILGL NKIVRMYSPI SILDIRQGPK EPFRDYVDRF
310 320 330 340 350 360
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPA ATLEEMMTAC QGVGGPGHKA
370 380 390 400 410 420
RVLAEAMSQV TNSATIMMQR GNFRRQGKTV KCFNCGKEGH IARNCKAPRK KGCWKCGREG
430 440 450 460 470 480
HQMKDCTERQ ANFLREDLAF PQGKAREFSS EQTRANSPTR GELQVWGRDN NSLSEAGAER
490 500 510 520 530 540
QGTVSFSFPQ ITLWQRPIVT IKIGGQLKEA LLDTGADDTV LEEINLPGRW KPKMIGGIGG
FIKVRQYDEV