ID Q23QF2_TETTS Unreviewed; 673 AA.
AC Q23QF2;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Tubulin tyrosine ligase family protein {ECO:0000313|EMBL:EAR98745.2};
GN ORFNames=TTHERM_01208740 {ECO:0000313|EMBL:EAR98745.2};
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:EAR98745.2, 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; GG662648; EAR98745.2; -; Genomic_DNA.
DR RefSeq; XP_001018990.2; XM_001018990.2.
DR AlphaFoldDB; Q23QF2; -.
DR STRING; 312017.Q23QF2; -.
DR EnsemblProtists; EAR98745; EAR98745; TTHERM_01208740.
DR GeneID; 7842328; -.
DR KEGG; tet:TTHERM_01208740; -.
DR eggNOG; KOG2157; Eukaryota.
DR HOGENOM; CLU_369857_0_0_1; -.
DR InParanoid; Q23QF2; -.
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:EAR98745.2}; 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 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 35..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 79983 MW; 9F33BE5A4A345BC0 CRC64;
MKLKKIFWWI IALNILGIIA VIVMILKSSY QTKKFGDDNS AKTRSRERSF EQKSTKNNTK
SEITTIKDEG RKDQQKVVYD IYQELQKIGQ LSKQEIKAKQ NKTLSLEQTA VSKSDEFQSF
FKQMNVLRMI YDYPQLDRKI HFNDMPDGHP LYDEPYMGLI NDPNYCDYVD AYNVLYPHNI
HNAMNIFNDY NNDGLARQVF KQYGYDVMPD FINKDMPDEE FNSRKYLIPF NTTMIFTKKV
KSYYYHEFNK NLYCVSQIYN HIPGHGTLTR KDLNVESVNN YAKRFENKPH CFKKNQFFPA
SYRLDNETEC RQFFEIFNSK EYKKLKEKEG ISYITKVSYG SHRANGLELV DDEYEVRLRR
KYYNGQLCGQ IEDNLMAQKY VANPHLLEGH KYDFRVYLLI ASTDPLIIYY HDGFLRLSIL
KYDKNSKEKS IHFANTNLAK DLFENAEQYK NITGMTEAEM RNFQMWNMSR YEDFLVSKGK
VKRGWLDDYL RPELQKAFIH AVKMSEHAFL KDPRVFEMFG LDFLFDENLN LWFIECNASP
VLQGTSEEKM IFQSELVRDL LQIQYSYLRS RWLRIRKIIT KLQTQLKEGN PDLKSLREEF
KKVNKNYLEK EYQIKNNSFV KITDLNLPGK AAYGNLFEED CFATDQKNQS KTDRQVDNNN
QKSKAKVSYK EEP
//
