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 P16900

Entry ID Method Resolution Chain Position Source

No variants for P16900

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P16900

No associated diseases with P16900

5 regional properties for P16900

Type Name Position InterPro Accession
conserved_site GHMP kinase, ATP-binding, conserved site 125 - 136 IPR006203
domain GHMP kinase N-terminal domain 118 - 185 IPR006204
domain GHMP kinase, C-terminal domain 290 - 370 IPR013750
domain Galactokinase, N-terminal domain 13 - 61 IPR019539
conserved_site Galactokinase, conserved site 30 - 41 IPR019741

Functions

Description
EC Number
Subcellular Localization
  • [Matrix protein p16]: Virion
  • ;
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
viral capsid The protein coat that surrounds the infective nucleic acid in some virus particles. It comprises numerous regularly arranged subunits, or capsomeres.

2 GO annotations of molecular function

Name Definition
nucleic acid binding Binding to a nucleic acid.
zinc ion binding Binding to a zinc ion (Zn).

1 GO annotations of biological process

Name Definition
viral budding via host ESCRT complex Viral budding which uses a host ESCRT protein complex, or complexes, to mediate the budding process.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MATQGSKEKK GYPELKEVIK TTCKIKVGPG KETLTEGNCL WALKTLDFIF EDIKTEPWTL
70 80 90 100 110 120
TKMYTVWEKL KQVTPEETSK REFASLQATL ACIMCSQMGM RPETVQAARG IISMKEGLHE
130 140 150 160 170 180
KQEDKEKKVE QLYPNLEKHR EVYPIVNLQA GGRSWKAVES VTFQQLQTVA MQHGLVSEDF
190 200 210 220 230 240
ERQLAYYATT WTSKDILEVL AMMPGNRAQK ELIQGKLNEE AERWVRQNPP GPNVLTVDQI
250 260 270 280 290 300
MGVGQTNQQA SQANMDQARQ LCLQWVITAL RSVRHMSHRP GNPMLIKQKN SESYEDFIAR
310 320 330 340 350 360
LLEAIDTEPV TDPIKTYLKV TLSFTNASTD CQKQMDRVLG TRVQQASVEE KMQACRDVGS
370 380 390 400 410 420
EGFKMQLLAQ ALRPPRKEGK QGVQKCYYCG KPGHLARQCR QGIICHHCGK RGHMQKDCRQ
430 440
KKGNPTSQQG NSRRGPRVVP SAPPML