ID Q248E1_TETTS Unreviewed; 654 AA.
AC Q248E1;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Tubulin tyrosine ligase family protein {ECO:0000313|EMBL:EAS04104.1};
GN ORFNames=TTHERM_00532260 {ECO:0000313|EMBL:EAS04104.1};
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:EAS04104.1, 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; GG662455; EAS04104.1; -; Genomic_DNA.
DR RefSeq; XP_001024349.1; XM_001024349.1.
DR AlphaFoldDB; Q248E1; -.
DR STRING; 312017.Q248E1; -.
DR EnsemblProtists; EAS04104; EAS04104; TTHERM_00532260.
DR GeneID; 7840768; -.
DR KEGG; tet:TTHERM_00532260; -.
DR eggNOG; KOG2157; Eukaryota.
DR HOGENOM; CLU_027769_0_0_1; -.
DR InParanoid; Q248E1; -.
DR OMA; YIMFGDM; -.
DR OrthoDB; 179304at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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: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 Ligase {ECO:0000313|EMBL:EAS04104.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 78138 MW; 5438D5570787EFF2 CRC64;
MGQKFKPNQQ KQDSSAQQLA NKITMRKSDK KTKRFQIIIA ISGILGAAFL YLSFINTQNK
SRVILVDENP DYFTSEAPHY GKQYHIKDHI KREAHPDFQK YNQKVKPEID IDWIEHEREA
RYIVYKFLEY SNITLDEQVH YEGKEIKWSP YLNIINNNKY CLNSDLYHLM HPDSINKNYL
IFSDYDKTTM SREVVSDFGI DLLPELENLD YSKQYTVGTK NMPLETTLIY SQISRMHHYF
EINKQLFCNF QMANHIPGKW SITNKDVVID KYREYQQKQF IDPQVCKKTM TYMPRSFRLY
DENECKQFFT HIQSQEYEES MKKQSFSYLL KQGEDVHRGE GVHLFTSKLR DEILQKYDKG
SKCGEILDKL IAQKYISNPL KYEGHKLELR MYFLIASTNP LIIYVQKQNF LKKCQLPFDI
QSTERASHIC NISAPKGQSQ SSGLDIFLEE LTEYYLEKGI IKNPKWLEET IYPQIYRALV
HLVRSGQQNL LKDSRFFESF AVDLIIDENQ RVWFLENNPN PQIMRLTWRR TRRNYIMFGD
MFQIQYAYLR SRALRLNRFA KFLLPLYQQY KTLDVSDFDR GFRRANQNDL EPEFENEIRK
DSTYIKVYDD NLEGKKKFMG FLPYECLYQI TNTQTDKDKD QEKDKEKEKD NGQS
//
