ID A0CVD0_PARTE Unreviewed; 593 AA.
AC A0CVD0;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Chromosome undetermined scaffold_29, whole genome shotgun sequence {ECO:0000313|EMBL:CAK74747.1};
GN ORFNames=GSPATT00010915001 {ECO:0000313|EMBL:CAK74747.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK74747.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK74747.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK74747.1,
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; CT868196; CAK74747.1; -; Genomic_DNA.
DR RefSeq; XP_001442144.1; XM_001442107.1.
DR AlphaFoldDB; A0CVD0; -.
DR EnsemblProtists; CAK74747; CAK74747; GSPATT00010915001.
DR GeneID; 5027929; -.
DR KEGG; ptm:GSPATT00010915001; -.
DR eggNOG; KOG2158; Eukaryota.
DR HOGENOM; CLU_010131_7_5_1; -.
DR InParanoid; A0CVD0; -.
DR OMA; HINISNC; -.
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:SF147; TUBULIN POLYGLUTAMYLASE TTLL7; 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 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 69548 MW; 3597B57C875FCE01 CRC64;
MQQKQSKKSK EEEPIFNGTF KDNSDDENDD KRKKQTLIIN VSDTKYDVVK FVGKKIFKWI
LQYEPDGVNW DMFWTDAAVQ PETLGKMQPH QKINHFPGMY SLARKNHLGR NLMKMRKQFP
NDYKFFPQTW LLPAEYGDFK NQFVKGKVRT FIVKPEASCQ GRGIFLTRSI NDINPTDHYV
AQRYMHRPFL IDGLKFDLRI YVLLAGTDPM RIYVYQDGLV RFATEQYVTP TTNNLEDVCM
HLTNYAINKE NPNFVFNNDA TKMDVGHKRS IKSVFGKLQE EGHNIQKLWQ DMYKLFIKTF
CTVQPILNHH YKSCQPDNYA NNMCFEILGM DIFINDKLRP SLLEVNHTPS FTTDTPLDSL
IKKNLIRDTL KLMNVSLKAK EEIIASRREQ LQQRVLTGKK QKLTQEEKQL LIKQWSEQRD
QHENNNLGDY IKIYPLEDAH EYDKFIEFSS QLQDNWTGAN IRRNQKKEPS ETQQFQISKP
PTIPVKKPNT PQMLPKISER QNRIHQSIEP NAEIKSKTQS SLGKSTKESK RQVSDPPIPK
QHQSMRNVQQ PPQQQQQLPL KSCLQPKLFE LDILSSQNRS NSQSKKLNQF KLQ
//