Q82851

PR
Gene name
gag-pol
Protein name
Gag-Pol polyprotein
Names
Pr170Gag-Pol
Species
Jembrana disease virus (JDV)
KEGG Pathway
EC number
2.7.7.49: Nucleotidyltransferases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

80-161 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

0 structures for Q82851

Entry ID Method Resolution Chain Position Source

No variants for Q82851

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q82851

No associated diseases with Q82851

2 regional properties for Q82851

Type Name Position InterPro Accession
domain LacI-type HTH domain 1 - 70 IPR000843
domain Transcriptional regulator LacI/GalR-like, sensor domain 164 - 330 IPR046335

Functions

Description
EC Number 2.7.7.49 Nucleotidyltransferases
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 nucleocapsid The complete protein-nucleic acid complex that is the packaged form of the genome in a virus particle.

9 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.
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 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).

6 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.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKLSKLEKAL KKVRVTPQRD DTYTIGNVLW AIRMCRLMGL DCCIDEATAA EVAILIGRFQ
70 80 90 100 110 120
SLDLQDSPLK GKDEKAILTT LKVLWSLLAG HHPENSDMAE KYWEAWTIRE RESQKEEEGE
130 140 150 160 170 180
ITSIYPQLRK NFPAVSTSDG SPRYDPDLTK QLKIWADATE KHGVDHHAVN ILGVITANLT
190 200 210 220 230 240
QSEIRLLLQS TPQWRLDIQL IESKLNAREH AHRVWKESHP EAPKTDEIIG KGLTAAEQAT
250 260 270 280 290 300
LTTQECRDTY RQWVLEAALE VAQGKHDRPG PINIHQGPKE PYPEFVNKLV TALEGMAAPE
310 320 330 340 350 360
TTKQYLLDHL SVDHANEDCR AVLLPLGPSA PMERKLEACR AVGSSKQKMQ FLAEAFAAIN
370 380 390 400 410 420
VKGDGEVQRC YGCGKPGHIR RDCKNQKCFK CGKPGHLQRN CKSKNREALL CPFWAEERIP
430 440 450 460 470 480
SGEDFCDPVC SPVGIRLNRQ PFIKIFLGGR WVRALIDTGA DEVVLKDIHW DRIKGVPAAS
490 500 510 520 530 540
VVQVGVTGRN IARRKSNVEW RFKNRYGIVD VLFSNTPVNL LGRSVLQSIV TKFTLAAHTK
550 560 570 580 590 600
QIQPLPVKLH GPGPRVPQWP LTLEKYKALK EIVEELLKDG KISRTPWDNP FNTPVFVIKK
610 620 630 640 650 660
KGGSKWRMLM DFRALNKVTN KGQEFQIGLP YPPGIQQCEH ITAIDIKDAY FTIPLDENFR
670 680 690 700 710 720
QYTAFSVVPV NREGPLERYH WNVLPQGWVC SPAIYQTTTQ EIIAEIKDRF PDIVLYQYMD
730 740 750 760 770 780
DLLIGSDRPD HKRVVSEIRE ELGAYGFKTP EEKIQEEQVQ WLGYELTPKR WRFQPRQIKI
790 800 810 820 830 840
KKVVTVNELQ QMIGNCVWVQ PEVKIPLSPL SDLLKGKTDL KDKIKLTEEA IQCLETVNKR
850 860 870 880 890 900
LKDPEWKERI KEGTELVVKI QLIPEGVVYD LLQDGNPIWG GVKGWDYNHA NKIKKMLSIM
910 920 930 940 950 960
KKLSRIVMIM TGREVSFLIP GDSEDWESAL QRINTLTEIP EVKFYKHACR WTSVCGPVIE
970 980 990 1000 1010 1020
RYPTYYTDGG KKGSKAAAAY WREGKIRREV FPGTNQQAEL KAVLMALQDG PAKMNIITDS
1030 1040 1050 1060 1070 1080
RYAFEGMREE PETWGREGLW KEIGEELRRK EYVGVSWVPG HKGIGGNTEV DQEVQKALQG
1090 1100 1110 1120 1130 1140
PITVSLPQEI LLEAGETKLV KTGIFWEGLR PCKLRPEEGL KLKGSLIDEE LQLEITNTQN
1150 1160 1170 1180 1190 1200
SRVGIRQGQT IGTCFIEAIP QAIEEHEKWH TTAEILAREF QLPRRVAREI VHRCQACKRT
1210 1220 1230 1240 1250 1260
VSCPRRGTNP RERFLWQMDN THLEGKIIWV AVETNSGLIE ARVIPEESAQ SIVFCILMLV
1270 1280 1290 1300 1310 1320
YRYTVYHIHS DNGPCFIAQK VEALCKYLKI TKTTGIPYNP QAQAIVERTH RDIKDKIAAF
1330 1340 1350 1360 1370 1380
REDCETVEAA LSLTLVALNK KRGGIGGHTP YEIYLESEYN KYQEQQNHYN NFKTEKWAYV
1390 1400 1410 1420 1430
RDKRKVWKGP YKVLWDGEGA AVVEENAMPT LYPHRHMRFI PPPNTDTQDG NL