ID A0E561_PARTE Unreviewed; 592 AA.
AC A0E561;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Chromosome undetermined scaffold_79, whole genome shotgun sequence {ECO:0000313|EMBL:CAK90428.1};
GN ORFNames=GSPATT00023605001 {ECO:0000313|EMBL:CAK90428.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK90428.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK90428.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK90428.1,
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; CT868659; CAK90428.1; -; Genomic_DNA.
DR RefSeq; XP_001457825.1; XM_001457788.1.
DR AlphaFoldDB; A0E561; -.
DR EnsemblProtists; CAK90428; CAK90428; GSPATT00023605001.
DR GeneID; 5043610; -.
DR KEGG; ptm:GSPATT00023605001; -.
DR eggNOG; KOG2158; Eukaryota.
DR HOGENOM; CLU_010131_7_5_1; -.
DR InParanoid; A0E561; -.
DR OMA; NIIRYTI; -.
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..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 69621 MW; 126DC2E2940FCF67 CRC64;
MKQQQLKEPH FNGEFEDSDS QTEDNNSKKK TTLIMNVSDT QYDVVKFVGK RLFKWILQYE
SDATNWDMFW TDTAVQPETL GKMQPYQKIN HFPGMYSLAR KNHLGRNLMK MRKQFTQEYK
FFPQTWLLPA EYGDFKTQFV KGKARTFIIK PEASCQGRGI FLTRNLNDIN PNDHYVAQRY
LLRPFLIEGL KFDLRVYVLL AGTDPMRIYV YQDGLVRFAT EPYVPPNTSN LDDMCMHLTN
YAINKENPNF VFNKDASRMD IGHKRSIKAV FAKLEEEGRD IKKLWQDMNE IFIKTFCAVQ
PILSHHYRSC QPDNYANNMC FEILGFDIFL NHKLQPILLE VNHTPSFTTD TPLDSMIKKN
LIRDTLKLMN VSLKAKEQII ASRKESLQQR VLTGKKVKLT MEEKMSQMKQ QEQQRNDYEN
SHLGDYVKIY PLEDSQEYDQ YIEFASSLQD SWTGTSINLM YLLDIKRNQK KNTQTPQQQQ
QIKNNVVRAP FKPNTPANNL PKLQKILRPE SINVHGEDEQ VCAKVNKLSN IKMQPRQQSE
PPVLRFKQTV KKQLQLVIPK PYLQPKLFDM ESIGQDKFNN KRQQFQDMMF TK
//
