ID   TTL3E_TETTS             Reviewed;        1394 AA.
AC   Q23AS2;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Tubulin glycylase 3E;
DE            EC=6.3.2.-;
GN   Name=TTLL3E; ORFNames=TTHERM_00770730;
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: Cell projection, cilium
CC       {ECO:0000269|PubMed:19531357}. Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000269|PubMed:19531357}. Note=Mainly present in locomotory and
CC       oral cilia.
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; GG662723; EAR93620.1; -; Genomic_DNA.
DR   RefSeq; XP_001013865.1; XM_001013865.1.
DR   AlphaFoldDB; Q23AS2; -.
DR   SMR; Q23AS2; -.
DR   EnsemblProtists; EAR93620; EAR93620; TTHERM_00770730.
DR   GeneID; 7823109; -.
DR   KEGG; tet:TTHERM_00770730; -.
DR   eggNOG; KOG2157; Eukaryota.
DR   HOGENOM; CLU_254769_0_0_1; -.
DR   InParanoid; Q23AS2; -.
DR   OMA; EDCKIND; -.
DR   OrthoDB; 1766818at2759; -.
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; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   Pfam; PF03133; TTL; 1.
DR   PROSITE; PS50096; IQ; 2.
DR   PROSITE; PS51221; TTL; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell projection; Cilium; Cytoplasm; Cytoskeleton; Ligase;
KW   Nucleotide-binding; Reference proteome; Repeat.
FT   CHAIN           1..1394
FT                   /note="Tubulin glycylase 3E"
FT                   /id="PRO_0000381801"
FT   DOMAIN          911..1250
FT                   /note="TTL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT   DOMAIN          1320..1349
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1348..1377
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          201..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..230
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1058..1061
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         1079
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         1081
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
SQ   SEQUENCE   1394 AA;  164098 MW;  8CD961987E3A94B1 CRC64;
     MILPFEYYFL NDADNSSKSN YNNIQFINEN QNNNLRQKPK FYPNNQFLIE QEQDKYENKK
     IKNYISDQIQ LQPKNTPINK MNHFANINNY QDNKFSLESL NQAQQDNLQK EEDLSILSFD
     SQEELNYLQE GEENNQFLNE GDIFGYQTRY TFFENRNNLL VEDATNKNNN NYNYNYNNNN
     SSTQRNYDFN YQNTNEMLQK KKKSNFQNKS QSQLNNHKNE EKKPSQQRKE QLMKRFESLS
     RIYNKELSQT VTNGWLKPSQ AKTISQDNNL GSSAAKSSKV FYQQQKPFSA QITNSSLKYA
     AASNGFQNLD FSYKQKQQLI QQETKNKIKE QQNVESNNRI SMKPPKSANL NSYKNISNLK
     NFKEIILTRP NSKQVKFQQQ NSVNSQPSSL VSQPLKIQSI EKNNLNSNLN DQNFYDDFAE
     LGSTETTGFS FQNVFQLAGV PKDFIASPRS PVQELNQKQE NRENELDQML NDHHIYVASS
     VTNQNQIKNE QTERKPNMFG KTLTTLARPF SKEYSNRKDI LKSAQQNVRF NKNLDYLDSQ
     NKVVAKNKKR TIFKINQNNL QGNQKDLQSN QTSSVISQQN SIQQYGDDNY QQNQVLNDDQ
     SPLIKQNSID LNAAEIIQND ENENTQKENV LQQKKNQSNQ IVTSQQQSNN YFKQETTTNT
     SNFSTTSNRI ISLQALRQKN NSTVKNSDNN NQNQTNPQNQ NTNLKENNDK QNLKKTKIQS
     ASANQAGQSN NQLQKTFFIN SQDEYVRRTL LRMGWKENKL LLNNNFDLKW IYIDSNDDYK
     FLNDNQFYNH FKNNTELTQK GRLLYNLKNN TQFGVNQELF FPRCYDLGND QERGEFSNEF
     NRMNVMNLLK KHIQYIKLRR SQTYQEIKQA YQQKQANKLN AQVKDGIFFA KVTKQKFFSP
     LMYEDTKRDN RFIFNITVIA EAVEILKKLK RQQEEYIDET RQSRDCQLYI YQTNFKLESM
     ISQYVKINVP FDEEKFVFEK IVGMSKEHWS SPSMKLMKKL YSLYKYFKDA DPQFKVSGTK
     NIWIIKPSAN SRGSGIYLVD KLDEAIDSGL KMQARIVQKY IERPLIFQGA KYKKLNNKKF
     DIRQWVLVTS FKPLKIYFFT SSYLRVCSQS FDLDNIKILS KHLTNFSLNK NSLAKENWDE
     TVVELKDFIS YLKEFKNIDY QEDVKPKIKD LVIETIKCAA DKIVNRKKSF ELYGFDILLD
     EYAHPWLLEV NLSPACSERS SFLTEMLDAM AYKMFQIVFK QNNLQEDLEI NKETAISTAP
     ASCQNPDYDW EEIYNEEQKE YFCEEDNNMQ LAFNNDIQLM VIGQKADLKK EKNLDKKYFQ
     YWGAIKIQSK IRSFLAKKKL QRLKNQKFTF AAIKIQQKMR QFLAKKQLNI LKKQQQTNIN
     IPIEDFNQVS VIEV