ID I7MCG4_TETTS Unreviewed; 648 AA.
AC I7MCG4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Tubulin--tyrosine ligase-like protein 9 {ECO:0000256|ARBA:ARBA00030445};
GN ORFNames=TTHERM_00773080 {ECO:0000313|EMBL:EAR83898.2};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR83898.2, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
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DR EMBL; GG662514; EAR83898.2; -; Genomic_DNA.
DR RefSeq; XP_001031561.2; XM_001031561.2.
DR AlphaFoldDB; I7MCG4; -.
DR STRING; 312017.I7MCG4; -.
DR GeneID; 7837349; -.
DR KEGG; tet:TTHERM_00773080; -.
DR eggNOG; KOG2157; Eukaryota.
DR eggNOG; KOG2182; Eukaryota.
DR InParanoid; I7MCG4; -.
DR OrthoDB; 100598at2759; -.
DR BRENDA; 6.3.2.B3; 6245.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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:SF39; TUBULIN POLYGLUTAMYLASE TTLL9-RELATED; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EAR83898.2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168}.
FT REGION 435..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 75425 MW; BA3687CA335E31E5 CRC64;
MSEYFRKYIK KEHYPVHPSS IKFKTTFKNC ILESMKRRQW KEAEFDDWDL NWAEKEWILD
VMDHAHVSSN QRVNHYRNFS ELCRKDLLIK NIKKYKKTLE KENKLEEAAL YNFTPLTYNL
PSEYSIFCEE FKKVNSMSDS KQLWIMKPIG KAQGKGIFLF RNIKEIGNWK NTYRYNPDNP
QADPYVVQKY IADPLLIGGK KFDMRIYALC VSYQPLTVYL YRTGFARFTH HRYDLEDISN
AYVHLTNVAI QKTSENYDEK LGGKWLLQTL KLYLISKYGQ EKVSEAFYQI QQIIIKALQA
VQKVMINDKR CFELYGFDIL FDAQLKPWLL EVNASPSMTA NTQVDSELKI SVLDDTFTII
DIERILTGQE EQIGGFDLIF KGNQIKLPQN STYSSLLGCY NNRNQQLKKL AKSTAIRLAQ
QYAEQQQQQQ QQQQLLLQQQ KQNDLNKQRS SSKGPQQNFN QTFKNNQPIK SGYSRYNAAK
AGPNKLIKKV VLNQGGSSTP LQSQQGQQNL LQPQQQPSSQ IISNTGGVKI GQNQNNNINN
TTNTSQLSSQ ASQQSTSQSS QQSSSQNQIN QVRKQTQPQQ PNIPKQVNSQ LNPNSGQMMM
MVNPTNNMNI NQKLNQYNDD KNNDKFQRYF KEEEKYMELL KGQHRDEE
//
