Q09647

PR
Gene name
ttll-4
Protein name
Tubulin polyglutamylase ttll-4
Names
Tubulin--tyrosine ligase-like protein 4
Species
Caenorhabditis elegans
KEGG Pathway
cel:CELE_ZK1128.6
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-137 (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 Q09647

Entry ID Method Resolution Chain Position Source
AF-Q09647-F1 Predicted AlphaFoldDB

No variants for Q09647

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q09647

No associated diseases with Q09647

2 regional properties for Q09647

Type Name Position InterPro Accession
conserved_site Isocitrate/isopropylmalate dehydrogenase, conserved site 242 - 261 IPR019818
domain Isopropylmalate dehydrogenase-like domain 5 - 348 IPR024084

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cilium A specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface and of some cytoplasmic parts. Each cilium is largely bounded by an extrusion of the cytoplasmic (plasma) membrane, and contains a regular longitudinal array of microtubules, anchored to a basal body.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
protein-glutamic acid ligase activity Catalysis of the posttranslational transfer of one or more glutamate residues to a specific residue on a target protein.
tubulin binding Binding to monomeric or multimeric forms of tubulin, including microtubules.
tubulin-glutamic acid ligase activity Catalysis of the posttranslational transfer of one or more glutamate residues to the gamma-carboxyl group(s) of one or more specific glutamate residues on a tubulin molecule.

3 GO annotations of biological process

Name Definition
microtubule cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising microtubules and their associated proteins.
protein polyglutamylation The addition of one or more alpha-linked glutamyl units to the gamma carboxyl group of peptidyl-glutamic acid.
response to hermaphrodite contact The response by the male to a hermaphrodite after initial contact following mate finding. The male stops forward locomotion, presses the ventral side of his tail against his partner's body, and begins moving backward along the hermaphrodite. Male response behavior is initiated when sensory neurons located in the rays of his tail contact a potential mate.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q14679 TTLL4 Tubulin monoglutamylase TTLL4 Homo sapiens (Human) PR
10 20 30 40 50 60
MSSGYSSAPS VSHTSSDTDL NRIDSYDDGA EETTDEQRMC GLSELVTSCL TSSRLKAIDE
70 80 90 100 110 120
EDEEENCNDI EIVGLSKTTT KVKRSKKVLS CPIVSSSTKK ENGNAAPFLK SSQFTDVPPT
130 140 150 160 170 180
IRFYTKGTKV TKPARKIQAR LTWCHNSLLP IVMRQTLAAS HFTVVDESLF YVGYWGRHLK
190 200 210 220 230 240
SAQYRALQPH QKVNHFPGAF HIGRKDRLWM HIRKQQERFE GEFDIMPFTY ILPTDRQELL
250 260 270 280 290 300
KYLETDASRH VIVKPPASAR GTGISVTRKP KDFPTTATLV AQHYIERPLT INRAKFDLRL
310 320 330 340 350 360
YAYVPTFEPL RVYIYDQGLV RFASVPYSHS VSTISNKYMH LTNYSINKLA EADGVANKPV
370 380 390 400 410 420
PKWTLHHLWE HFDEMGVDRE KIQREIEEVI IKAFISTEKP IREHMSRFLE QEFICYELFG
430 440 450 460 470 480
IDIILDEDYK PWLLEVNISP SLHSGTPLDV SVKAPLAKDV LNLAGVYVPP SFDKLSDADY
490 500 510 520 530 540
STRPRNGRKN REQLIKEASW VAAYKDQLGV IDNRIFKRLT PEDTRALVEF EDELERIGDF
550 560 570 580 590 600
KLVFPTAHTS HYQKYFAETI YMNILLQQWQ IAQEDDRSIG INRLEQLCRQ KHMQSDQETS
F