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 P24107

Entry ID Method Resolution Chain Position Source

No variants for P24107

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P24107

No associated diseases with P24107

3 regional properties for P24107

Type Name Position InterPro Accession
domain Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic 6 - 287 IPR006075
conserved_site Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site 142 - 156 IPR017958
domain Asn/Gln amidotransferase 326 - 473 IPR018027

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 KKADELEKVR LRPGGKKKYK LKHIVWAANE LDRFGLAESL LESKEGCQRI
70 80 90 100 110 120
LKVLDPLVPT GSENLKSLFN TVCVIWCIHA EEKVKDTEEA KRIALRHLAA ETGTAEKMPD
130 140 150 160 170 180
TSRPTAPPSG KGGNYPVQSI GGNYTHVPLS PRTLNAWVKL VEEKKFGAEV VPGFQALSEG
190 200 210 220 230 240
CTPYDINQML NCVGDHQAAM QIIREIINEE AADWDANHPI PGPLPAGQLR DPRGSDIAGT
250 260 270 280 290 300
TSTVEEQIQW MFRAQNPVPV GNIYRRWIQI GLQKCVRMYN PTNILDIKQG PKESFQSYVD
310 320 330 340 350 360
RFYKSLRAEQ TDPAVKNWMT QTLLVQNANP DCKLVLKGLG MNPTLEEMLT ACQGVGGPGQ
370 380 390 400 410 420
KARLMAEALK EAMGPPPIPF AAAQQRRTIK CWNCGKEGHS ARQCRAPRRQ GCWKCGKPGH
430 440 450 460 470 480
IMTNCPDRQA GFLRDWPLGK EAPQFPRGPS STGANTNSTP IGSSSGSTGE IYAAREKAEG
490 500 510 520 530 540
AETETIQRGD RGLTAPRTRR GPMQGDNRGL AAPQFSLWKR PVVTAHIEGQ PVEVLLDTGA
550 560 570 580 590 600
DDSIVAGIEL GSNYSPKIVG GIGGFINTKE YKNVEIEVLG KRVRATIMTG DTPINIFGRN
610 620 630 640 650 660
ILTALGMSLN LPVAKIEPIK IMLKPGKDGP RLRQWPLTKE KIEALKEICE KMEKEGQLEE
670 680 690 700 710 720
APPTNPYNTP TFAIRKKDKN KWRMLIDFRE LNKVTQDFTE IQLGIPHPAG LAKKRRITVL
730 740 750 760 770 780
DVGDAYFSIP LHEDFRQYTA FTLPSVNNAE PGKRYIYKVL PQGWKGSPAI FQYTMRQVLE
790 800 810 820 830 840
PFRKANSDVI IIQYMDDILI ASDRTDLEHD KVVLQLKELL NNLGFSTPDE KFQKDPPYRW
850 860 870 880 890 900
MGYELWPTKW KLQKIQLPQK EVWTVNDIQK LVGVLNWAAQ IYPGIKTKHL CRLIRGKMTL
910 920 930 940 950 960
TEEVQWTELA EAELEENRII LSQEQEGHYY QEEKELEATV QKDQDNQWTY KIHQEEKILK
970 980 990 1000 1010 1020
VGKYAKIKHT HTNGVKLLAQ VVQKIGKEAL VIGRIPKFHL PVEREVWEQW WDNYWQVTWI
1030 1040 1050 1060 1070 1080
PDWDFVSTPP LVRLAFNLVG DPIPGTETFY TDGSCNRQSK EGKAGYVTDR GRDKVKILEQ
1090 1100 1110 1120 1130 1140
TTNQQAELEA FAMALTDSGP KANIIVDSQY VMGIVAGQPT ESENRIVNQI IEEMIKKEAI
1150 1160 1170 1180 1190 1200
YVAWVPAHKG IGGNQEVDHL VSQGIRQVLF LEKIEPAQEE HEKYHTNVKE LCHKFDIPQL
1210 1220 1230 1240 1250 1260
VARQIVNTCA QYQQKGEAIH GQVNAEVGTW QMDCTHLEGK IIIVAVHVAS GFIEAEVIPQ
1270 1280 1290 1300 1310 1320
ESGRQTALFL LKLASRWPIT HLHTDNGANF TSQEVKMVAW WVGIEQTFGV PYNPQSQGVV
1330 1340 1350 1360 1370 1380
EAMNHHLKNQ ISRIREQANT VETIVLMAVH CMNFKRRGGI GDMTPSERLI NMITTEQEIQ
1390 1400 1410 1420 1430 1440
FLQAKNSKLK NFRVYFREGR DQLWKGPGEL LWKGDGAVIV KVGTDIKIIP RRKAKIIRDY
1450 1460
GGRQELDSSS HLEGARENGE VA