ID A0DAT4_PARTE Unreviewed; 531 AA.
AC A0DAT4;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
GN ORFNames=GSPATT00015058001 {ECO:0000313|EMBL:CAK80151.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK80151.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK80151.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK80151.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
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:0000256|ARBA:ARBA00036640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145;
CC Evidence={ECO:0000256|ARBA:ARBA00036640};
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DR EMBL; CT868352; CAK80151.1; -; Genomic_DNA.
DR RefSeq; XP_001447548.1; XM_001447511.1.
DR AlphaFoldDB; A0DAT4; -.
DR STRING; 5888.A0DAT4; -.
DR EnsemblProtists; CAK80151; CAK80151; GSPATT00015058001.
DR GeneID; 5033333; -.
DR KEGG; ptm:GSPATT00015058001; -.
DR eggNOG; KOG2157; Eukaryota.
DR HOGENOM; CLU_010131_1_1_1; -.
DR InParanoid; A0DAT4; -.
DR OMA; ITCINPL; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR PANTHER; PTHR12241:SF145; TUBULIN POLYGLUTAMYLASE TTLL5; 1.
DR Pfam; PF03133; TTL; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS51221; TTL; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000600}.
SQ SEQUENCE 531 AA; 62044 MW; C39AFDF9AD2090A2 CRC64;
MNSPGDSIDD IISLLNKHYH PNCNQEQQSQ QNSRPKAGIG NVMLPQIKQQ LNVLSAIPNT
YNNNSDKFKR KAASLNRQQQ PKSQTKDTNS FLIPMTRYLT FKPYSGSTDI IINDVGYYYK
FGSSPIKLVK GLLEENGFKE NNDKNWTLYW SSCAIRSEIY TNLFAYQKVC HFPKSYEMTR
KDLMHRNISK MQINHGFINF NFIPKTYILP AEMSYFLEEH EKIKNNNPVY ICKPHASSQG
KGIFITDKIQ DILNKQNSNN SYVVSHYIDK PLLINNLKFD LRIYVAITCI NPLRIYVYQD
GLARFATEAY NPDSVKQNRF VHLTNYSVNK DSPNFVANQD PTLDYLGSKW SLLALREYLK
LNKINEQQIF ERIEDLIIKT IISVESAIFQ ACEMNVPFRS NCFSLFGFDV LVDQFLKPWL
LEVNFSPSLN IDAPLDLKIK GEMLADLFTL IGIVPLDQRF SQDLSYVRNQ SNYDVKKHQQ
EFEKYILKET EEEFKRSRGW KRLYPSDQSS RYSKYFESDR PLNALLRNYY K
//