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 P31625

Entry ID Method Resolution Chain Position Source

No variants for P31625

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P31625

No associated diseases with P31625

12 regional properties for P31625

Type Name Position InterPro Accession
domain G-patch domain 819 - 866 IPR000467
domain Retroviral nucleocapsid Gag protein p24, N-terminal 267 - 389 IPR000721
domain Zinc finger, CCHC-type 508 - 524 IPR001878-1
domain Zinc finger, CCHC-type 535 - 551 IPR001878-2
active_site Aspartic peptidase, active site 736 - 747 IPR001969
domain Peptidase A2A, retrovirus, catalytic 734 - 810 IPR001995
domain Beta-retroviral matrix protein 7 - 90 IPR003322
domain Retropepsins 720 - 818 IPR018061
domain dUTPase-like 591 - 710 IPR029054
domain dUTPase, trimeric 601 - 688 IPR033704
domain Retropepsin-like catalytic domain 725 - 812 IPR034170
domain Retroviral nucleocapsid Gag protein p24, C-terminal domain 391 - 463 IPR045345

Functions

Description
EC Number 3.6.1.23 In phosphorus-containing anhydrides
Subcellular Localization
  • [Matrix protein p10]: Virion
  • ;
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
viral nucleocapsid The complete protein-nucleic acid complex that is the packaged form of the genome in a virus particle.

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.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
dUTP diphosphatase activity Catalysis of the reaction: dUTP + H2O = dUMP + H+ + diphosphate.
structural constituent of virion The action of a molecule that contributes to the structural integrity of a virion.
zinc ion binding Binding to a zinc ion (Zn).

3 GO annotations of biological process

Name Definition
nucleotide metabolic process The chemical reactions and pathways involving a nucleotide, a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic nucleotides (nucleoside cyclic phosphates).
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
viral process A multi-organism process in which a virus is a participant. The other participant is the host. Includes infection of a host cell, replication of the viral genome, and assembly of progeny virus particles. In some cases the viral genetic material may integrate into the host genome and only subsequently, under particular circumstances, 'complete' its life cycle.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGHTHSRQLF VHMLSVMLKH RGITVSKTKL INFLSFIEEV CPWFPREGTV NLETWKKVGE
70 80 90 100 110 120
QIRTHYTLHG PEKVPVETLS FWTLIRDCLD FDNDELKRLG NLLKQEEDPL HTPDSVPSYD
130 140 150 160 170 180
PPPPPPPSLK MHPSDNDDSL SSTDEAELDE EAAKYHQEDW GFLAQEKGAL TSKDELVECF
190 200 210 220 230 240
KNLTIALQNA GIQLPSNNNT FPSAPPFPPA YTPTVMAGLD PPPGFPPPSK HMSPLQKALR
250 260 270 280 290 300
QAQRLGEVVS DFSLAFPVFE NNNQRYYESL PFKQLKELKI ACSQYGPTAP FTIAMIESLG
310 320 330 340 350 360
TQALPPNDWK QTARACLSGG DYLLWKSEFF EQCARIADVN RQQGIQTSYE MLIGEGPYQA
370 380 390 400 410 420
TDTQLNFLPG AYAQISNAAR QAWKKLPSSS TKTEDLSKVR QGPDEPYQDF VARLLDTIGK
430 440 450 460 470 480
IMSDEKAGMV LAKQLAFENA NSACQAALRP YRKKGDLSDF IRICADIGPS YMQGIAMAAA
490 500 510 520 530 540
LQGKSIKEVL FQQQARNKKG LQKSGNSGCF VCGQPGHRAA VCPQKHQTSV NTPNLCPRCK
550 560 570 580 590 600
KGKHWARDCR SKTDVQGNPL PPVSGNLGEG PAPGPETMLW GNTAGSKRTI ADLCRATRGS
610 620 630 640 650 660
AGLDLCATSY TVLTPEMGVQ TLATGVFGPL PPGTVGLLLG RSSASLKGIL IHPGVIDSDY
670 680 690 700 710 720
TGEIKILASA PNKIIVINAG QRIAQLLLVP LVIQGKTINR DRQDKGFGSS DAYWVQNVTE
730 740 750 760 770 780
ARPELELRIN ANFFRGVLDT GADISVISDK YWPTTWPKQM AISTLQGIGQ TTNPEQSSSL
790 800 810 820 830 840
LTWKDKDGHT GQFKPYILPY LPVNLWGRDI LSKMGVYLYS PSPTVTDLML DQGLLPNQGL
850 860
GKQHQGIILP LDLKPNQDRK GLGCFP