ID A0EEC1_PARTE Unreviewed; 564 AA.
AC A0EEC1;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Chromosome undetermined scaffold_91, whole genome shotgun sequence {ECO:0000313|EMBL:CAK93639.1};
GN ORFNames=GSPATT00025983001 {ECO:0000313|EMBL:CAK93639.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK93639.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK93639.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK93639.1,
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).
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DR EMBL; CT868673; CAK93639.1; -; Genomic_DNA.
DR RefSeq; XP_001461035.1; XM_001460998.1.
DR AlphaFoldDB; A0EEC1; -.
DR EnsemblProtists; CAK93639; CAK93639; GSPATT00025983001.
DR GeneID; 5046820; -.
DR KEGG; ptm:GSPATT00025983001; -.
DR eggNOG; KOG2157; Eukaryota.
DR HOGENOM; CLU_010494_0_0_1; -.
DR InParanoid; A0EEC1; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR PANTHER; PTHR46069:SF1; LIGASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR46069; TUBULIN TYROSINE LIGASE; 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}.
FT REGION 84..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 66783 MW; E1FA0AC93DFB3D78 CRC64;
MQSAQKLTQQ NQDAFSQFFD KYVSNSSKLQ SYSVRELAQK LAIQYFSAQL PSRYLTENNM
RKKSRNIVYK QMETDAIEKA RAQFKAKKQR KESQQRKLPP VPKKKDTQPR SFSVQPPIKC
LSAQPKRSMP STYFYYLGDG NNHELIKKLL DERQNWVQVK DISLKNINFK WQETEKGYEY
RTLAGNLKDS LPQMLNHFEF HAEISNKYHL ALNFKTHCER NQLNVQDYIP ISFAIECTNQ
NLKAGLFQFL TFYRSQCPQN QLQELDKTIK SYQFKYGTQV EGKVDEYPTL FAGENLWIFK
PANMNQGRGI HVVRNLQEII DIYNRYQNGY REHLLEVKRN EQNEIVTKIV YINTLMTEQF
VIQKYIEKPL LIKGRKFDIR TYVMITSNLG FFFFKEGQLR LATESFDVKQ QSNYVHLTNN
AVQYTHPQYG KTEEGNQYNF DQASQYFKID FRKEVIQKLK QISLLAFTSV KGKLNKYKRK
NCFEIFGMDF ILDVDFKPWL IEVNTNPSLE VTSKLLGTLF PRLIVDDAFK LTVDRLFVQQ
KTPSKYPFLH YSNEENLWEY VCQL
//
