Q9VW09

PR
Gene name
Ltn1
Protein name
E3 ubiquitin-protein ligase listerin
Names
Listerin E3 ubiquitin protein ligase 1, RING-type E3 ubiquitin transferase listerin
Species
Drosophila melanogaster (Fruit fly)
KEGG Pathway
dme:Dmel_CG32210
EC number
2.3.2.27: Aminoacyltransferases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-57 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9VW09

Entry ID Method Resolution Chain Position Source
AF-Q9VW09-F1 Predicted AlphaFoldDB

No variants for Q9VW09

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9VW09

No associated diseases with Q9VW09

2 regional properties for Q9VW09

Type Name Position InterPro Accession
domain Zinc finger, RING-type 1697 - 1744 IPR001841
domain Listerin, zinc finger, RING-type 1695 - 1744 IPR039804

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Cytoplasm, cytosol
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
RQC complex A multiprotein complex that forms a stable complex with large ribosomal subunits (60S in eukaryotes and 50S in prokaryotes) containing stalled polypeptides and triggers their degradation (ribosomal quality control). In budding yeast, this complex includes Cdc48p, Rkr1p, Tae2p, Rqc1p, Npl4p and Ufd1p proteins.

3 GO annotations of molecular function

Name Definition
ribosomal large subunit binding Binding to a large ribosomal subunit.
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
rescue of stalled ribosome A process of translational elongation that takes place when a ribosome has stalled during translation, and results in freeing the ribosome from the stalled translation complex.
ribosome-associated ubiquitin-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide encoded by an aberrant message and associated with a stalled ribosome. Degradation is initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the ribosome-associated protein.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q6A009 Ltn1 E3 ubiquitin-protein ligase listerin Mus musculus (Mouse) PR
10 20 30 40 50 60
MGGKTKQAPR TKNNAKPSSS SRTAELLGSS TPIFVGFSAQ TDGGGLVPFA PGFASAEQMP
70 80 90 100 110 120
DSFDAAISPQ TQIILRKLSK KDPMTKKKAL QELHELIEQS DVEVLKNILP LWPKYYLNLA
130 140 150 160 170 180
SDPEHTVREQ TQTVLQLLMA KCKKAMAPYL KLLVPVWLGS RFDTYAPAAS IASQSFRDTF
190 200 210 220 230 240
AGNANRSREV CMHCQVEILE YATRNLTFHT AATLSIGKSL TPEDAEQKYQ RVIISSLKLL
250 260 270 280 290 300
SFFMGQTAQT EELSQVKEGF GTLVAHQKFW SFAKHKVPAI KAAWFECIYH ILQSVALLDV
310 320 330 340 350 360
ITPQKTQLTN LCFQFIDDAD PVVAPHIWGC VLLLQSNYVD WFVPLNIRKT LLPKLSSLLQ
370 380 390 400 410 420
NGFNRNAQAI CPNLLPFLSK VTQASLQDLD IYDFYQRFFD DMKLAVTKKF DPPLSKSDCI
430 440 450 460 470 480
VIHNAYFECL RFLMQQINNN KQREQKEEEF SFSLLDNNVL EPIAWLLKSD STHVKIFFQH
490 500 510 520 530 540
SSALVAFWDR QINNRLDNGD LYAKLLNKFW IRIFELVTQD LSAEEVNEQL LGHVLLLVQD
550 560 570 580 590 600
LHMANPSLES PSVKFVEGPN EKIEKSEPTT PVKKAQEAAA FIQKELKQLV IKLVRICLDK
610 620 630 640 650 660
ANKGSGSGTS SSRYIEQIRT LTKMFNDAAF YKSLTDDGDL ASALNKFVSL LGQLSCQACE
670 680 690 700 710 720
SVVEIVFEIL PLLETGKRFE YIENTLMKLP QHGVQNLLLH RLLSYPLCAE AAVRQMLSGP
730 740 750 760 770 780
ETCEMIARIA EEVVVDNDRE KLNLLHKCFF QTDTGDILIN AKTVDKILLS MCGPLEQPVV
790 800 810 820 830 840
DDAVEVCGSF IAQIMPVICS NNNSSLHVRQ HIFLKLFKFS LEHRPEDYLS EDTLWEITTC
850 860 870 880 890 900
WQDGLSSKDI EIDDDMLKCC AGIVEELANS AELKADTLDG MAEAMAKFVI CSTENIEDEY
910 920 930 940 950 960
KRLERIDETL TALLETPLKT TDKVQQFENH CVLLEALHGS VTAGVPFENA CLSRNEILPL
970 980 990 1000 1010 1020
LQRSTLNFST IYKLVYQFPP PQDTNDPEDE LTEDYCDPNA DVLKKWNEPL IAELLQCIRV
1030 1040 1050 1060 1070 1080
AGTAECWLEM SVLQSSTEEL VLILSEKVQS FMGNSSDLVA IVKERLQQAA VQQSSVIDCR
1090 1100 1110 1120 1130 1140
LLSYLRFCPQ YAAFEESASI LLHEDLSENL VTQGALKTYV IALQFLLPKL SQKAITLSSA
1150 1160 1170 1180 1190 1200
IMGTEPPEIW VKAAVFHALL LNNFEGDVNE QTDRNIIVSA VQFMTSIGER QASQKDLLHY
1210 1220 1230 1240 1250 1260
NVEIQRQPYE SVINTVEFIK LLTEVLKRFP YELSIKNWDA IRIGLSSWVL SVSKSIAQYQ
1270 1280 1290 1300 1310 1320
DPKTSLFIVA VYELFAALID FIRSEKQKSS TELLKNMIDE WDSLFAKEVN LVLFKSYYLL
1330 1340 1350 1360 1370 1380
THEVSVDPGF QACYEALLEQ ITPVIERLDY SFVYSFCKSN SNITLDHLCN FLFKQLYSVQ
1390 1400 1410 1420 1430 1440
HSVRLSAVHS LRQLTPHFVA DDIELNEKQS ESLDASTTIC KWHFLNRFED YLTRYDALIT
1450 1460 1470 1480 1490 1500
KYLEEFTFKL SELDDLEPID RHNALSYLFL WDCIINACAK SPVALRAVYT NWLNDNKYEE
1510 1520 1530 1540 1550 1560
NFLHFLFRAM PVDILKNHGA KVHSNGVYKE LTWSQQKDRH LPLERYACHL YTEVLRKLPA
1570 1580 1590 1600 1610 1620
VVRRWWNATQ SRQKNFIDNL TTNYVSSLIC SEELKAIANR KEKHENMQVT VHSSTREVLA
1630 1640 1650 1660 1670 1680
VYAIDEARME LVITLAPNYP LGAVKVECGK QIGGRASSRN VGMQLTIFLT HQNGTIYDGL
1690 1700 1710 1720 1730 1740
TMWKNNLDKK FEGVEECYVC YTVIHQETCQ LPKLTCKTCK KKFHGPCLYK WFTTSSKSTC
PICRNVF