ID   TTL3F_TETTS             Reviewed;         899 AA.
AC   P0CAZ1;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 2.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Tubulin glycylase 3F;
DE            EC=6.3.2.-;
GN   Name=TTLL3F; ORFNames=TTHERM_00316230;
OS   Tetrahymena thermophila (strain SB210).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=312017;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB210;
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).
RN   [2]
RP   SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19531357; DOI=10.1016/j.devcel.2009.04.008;
RA   Wloga D., Webster D.M., Rogowski K., Bre M.-H., Levilliers N.,
RA   Jerka-Dziadosz M., Janke C., Dougan S.T., Gaertig J.;
RT   "TTLL3 Is a tubulin glycine ligase that regulates the assembly of cilia.";
RL   Dev. Cell 16:867-876(2009).
CC   -!- FUNCTION: Probable glycylase which modifies tubulin, generating side
CC       chains of glycine on the gamma-carboxyl groups of specific glutamate
CC       residues within the C-terminal tail of tubulin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking TTLL3A, TTLL3B, TTLL3C, TTLL3D,
CC       TTLL3E and TTLL3F display shortened axonemes that are resistant to
CC       paclitaxel, indicating that tubulin glycylation changes the lattice
CC       properties of axonemal microtubules. Axonemes are however normal at the
CC       ultrastructural level. {ECO:0000269|PubMed:19531357}.
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DR   EMBL; GG662605; EAS01070.2; -; Genomic_DNA.
DR   RefSeq; XP_001021315.2; XM_001021315.2.
DR   AlphaFoldDB; P0CAZ1; -.
DR   EnsemblProtists; EAS01070; EAS01070; TTHERM_00316230.
DR   GeneID; 7829708; -.
DR   KEGG; tet:TTHERM_00316230; -.
DR   eggNOG; KOG2157; Eukaryota.
DR   HOGENOM; CLU_319721_0_0_1; -.
DR   InParanoid; P0CAZ1; -.
DR   OrthoDB; 626048at2759; -.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
DR   GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0070735; F:protein-glycine ligase activity; TAS:UniProtKB.
DR   GO; GO:0018094; P:protein polyglycylation; TAS:UniProtKB.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   Pfam; PF03133; TTL; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell projection; Cilium; Cytoplasm; Cytoskeleton; Ligase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..899
FT                   /note="Tubulin glycylase 3F"
FT                   /id="PRO_0000381802"
FT   DOMAIN          471..835
FT                   /note="TTL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT   BINDING         642..645
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         663
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         665
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
SQ   SEQUENCE   899 AA;  106983 MW;  E6DAF37D74060420 CRC64;
     MSDRIYHSYV NNFYQKAKSP KNTQLIKQIQ RSNPTSPKKN LQIYKNINPF NHENCQRIIE
     ENAIRFSDKK TVQLGTVYGC NILLTTKNSQ PKVFEKLIQL SDNSNFRQVT LLKSISPVSV
     VKAKDFLNDS ISNRSRSAQK MYSDKDKFQV GNNKSSLRSL IYFPLANIKD QISEESKSKR
     NKIKVIKDMP IQLDNSFQTI NHQINSPNNN IVGDQSHVIL HNIFKKRQQA EEGLQIQEEP
     QNYIKNKLEL QERKMYLENQ NPKSLSPIKI HFNEKSMPFK NKIQKKITYN EQSSIQQTIT
     LIKKKILGPP SLYSRLKKNS EQFKNIENLI KNKAKESHEQ NMQEYLKRIG CTDKNKKVFC
     INSQDQFVQE VLIELGWIEN KLFKSDLFHL KWIYTDINKD YENLKEGQFY NHFQNNQELT
     NKGRLLRNIK LYLVSYPHLQ KYFPIQFDVI YKQQKEEFLN EFQKFEIFRK FKDVIQIIKN
     DLTQELINQL TQIYHTKFIK KEEEEELQYG LITYFRQNQQ FKQYIEYINQ VNKDIINLLS
     KIPNPNINEM LIKYLNDLSI LQVDKLECDQ EQGDKNIQAQ IINLSISIEL DNILEQIYPY
     TNFCNFWIIK PCGSSKGQGL QIMSDDNQIV NYTTQLQARL VQKYIERIYI CKSQEYPQLY
     NKKFDLRLWV LVKSFNPLTV YYYKHAYLRV CSSEYDLSDT RNIFSHFTNY SINRNKFIQN
     KNVEDSAISL KLLKHIIKKE HGISYQKKIQ PQINEIIIHS LKSVQKKIKQ NNSCFEIYGF
     DIIFDEQFNP YLLEVNLSPA CSKRNEFISK LQKEMFISTL NILFNTEYYQ IQNWKKIKIQ
     DQIQKVINES THTQLQEEVI LNSNNFQSED SEERFISAAI TIQKWYRQIK LMKNENQKI