TTLL4_CAEBR
ID TTLL4_CAEBR Reviewed; 597 AA.
AC A8X9V4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Tubulin polyglutamylase ttll-4;
DE EC=6.3.2.- {ECO:0000250|UniProtKB:Q09647};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 4 {ECO:0000250|UniProtKB:Q09647};
GN Name=ttll-4; ORFNames=CBG09874;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Monoglutamylase which modifies tubulin, adding a single
CC glutamate on the gamma-carboxyl group of specific glutamate residues of
CC target proteins. Involved in the side-chain initiation step of the
CC polyglutamylation reaction but not in the elongation step.
CC Preferentially modifies beta-tail tubulin over the alpha-tubulin.
CC Involved in side-chain glutamylation of tubulin in sensory cilia.
CC Together with ttll-5 and ttll-11, required for male mating.
CC {ECO:0000250|UniProtKB:Q09647}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-
CC glutamyl-L-glutamyl-[protein] + H(+) + phosphate;
CC Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q09647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145;
CC Evidence={ECO:0000250|UniProtKB:Q09647};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC {ECO:0000305}.
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DR EMBL; HE601459; CAP29419.1; -; Genomic_DNA.
DR RefSeq; XP_002641573.1; XM_002641527.1.
DR AlphaFoldDB; A8X9V4; -.
DR SMR; A8X9V4; -.
DR STRING; 6238.CBG09874; -.
DR EnsemblMetazoa; CBG09874.1; CBG09874.1; WBGene00031388.
DR GeneID; 8583564; -.
DR KEGG; cbr:CBG_09874; -.
DR CTD; 8583564; -.
DR WormBase; CBG09874; CBP02521; WBGene00031388; Cbr-ttll-4.
DR eggNOG; KOG2156; Eukaryota.
DR HOGENOM; CLU_010131_8_1_1; -.
DR InParanoid; A8X9V4; -.
DR OMA; HRWSQIP; -.
DR OrthoDB; 219807at2759; -.
DR Proteomes; UP000008549; Chromosome III.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070739; F:protein-glutamic acid ligase activity; ISS:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0070740; F:tubulin-glutamic acid ligase activity; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0018095; P:protein polyglutamylation; IBA:GO_Central.
DR GO; GO:0034606; P:response to hermaphrodite contact; IEA:EnsemblMetazoa.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR027748; TTLL-4.
DR PANTHER; PTHR12241:SF145; PTHR12241:SF145; 1.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..597
FT /note="Tubulin polyglutamylase ttll-4"
FT /id="PRO_0000403766"
FT DOMAIN 134..472
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..341
FT /note="L-glutamate"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 256..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 256
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_part="L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:29973"
FT /ligand_part_note="L-glutamate acceptor residue in protein
FT target"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 278..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 291..293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 317
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 338..339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 358
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 418
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 433
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 449
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 256
FT /note="Essential for specifying initiation versus
FT elongation step of the polyglutamylase activity"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
SQ SEQUENCE 597 AA; 68666 MW; 246D8EC8C756D5D2 CRC64;
MSSGYSSAPS VSHTSSEADL NRIESYEDGV DEEASDEQRM CGLSELVTSC LTSSKSSRQK
DSFEDDDDVP IEIVGTLKKS KSKKKKQCPP NITIEKKNGN SSPFLKSSQF TDVPPTIRFY
TKGTKVTKPA RKIQSRLTWC HNSLLPIVMR QTLSASHFTI VDESLFHIGY WGRHLKSAQY
KALQPHQKVN HFPGAFHIGR KDRLWMHIRN RLEHFGEEFE IMPFTYILPT DRQELLKYLE
TDVNRHVIIK PPASARGSGI TVTRKPKDFP TTATLVAQHY IERPLTINRA KFDLRLYAYV
PTFEPLRVYI YDQGLVRFAS VPYNPSVTNI SNKYMHLTNY SINKLAEADG IANKPVPKWA
LHQLWDYFDQ MGVNSQKIQK EIEDVIVKAF ISCEKPIREH MSRFLEQEFI CYELFGIDII
LDEDYKPWLL EVNISPSLHS GTSLDVSVKA PLAKDVLNLA GIHVPPSFDK LHTADYSCRP
RNGTKTREQL VKEASWVAAY RDQHGAIDNR IFKRLTPEDT RALVEFEDEL DRIGDFKLVF
PTAQTAHYQK FFAEPIYMNI LLQQWQIAQE GDRSIGIDRL EQLCRQKHMQ SDQEISF
