ID   TTL3A_TETTS             Reviewed;         875 AA.
AC   Q23TC2;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Tubulin glycylase 3A;
DE            EC=6.3.2.-;
GN   Name=TTLL3A; ORFNames=TTHERM_00666600;
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   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP   AND MUTAGENESIS OF GLU-818.
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: Monoglycylase which modifies alpha- and beta-tubulin,
CC       generating side chains of glycine on the gamma-carboxyl groups of
CC       specific glutamate residues within the C-terminal tail of alpha- and
CC       beta-tubulin. Involved in the side-chain initiation step of the
CC       glycylation reaction by adding a single glycine chain to generate
CC       monoglycine side chains. Not involved in elongation step of the
CC       polyglycylation reaction. {ECO:0000269|PubMed:19531357}.
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 and TTLL3B show a strongly
CC       reduced level of monoglycylated tubulin and a moderately reduced level
CC       of polycylated tubulin. 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; GG662636; EAR99784.1; -; Genomic_DNA.
DR   RefSeq; XP_001020029.1; XM_001020029.1.
DR   AlphaFoldDB; Q23TC2; -.
DR   SMR; Q23TC2; -.
DR   EnsemblProtists; EAR99784; EAR99784; TTHERM_00666600.
DR   GeneID; 7842499; -.
DR   KEGG; tet:TTHERM_00666600; -.
DR   eggNOG; KOG2157; Eukaryota.
DR   HOGENOM; CLU_016035_0_0_1; -.
DR   InParanoid; Q23TC2; -.
DR   OMA; ISKHADN; -.
DR   OrthoDB; 92966at2759; -.
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; IDA:UniProtKB.
DR   GO; GO:0070736; F:protein-glycine ligase activity, initiating; IDA:UniProtKB.
DR   GO; GO:0035082; P:axoneme assembly; IMP:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR   GO; GO:0018094; P:protein polyglycylation; IDA:UniProtKB.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   Pfam; PF03133; TTL; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell projection; Cilium; Cytoplasm; Cytoskeleton; Ligase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..875
FT                   /note="Tubulin glycylase 3A"
FT                   /id="PRO_0000381797"
FT   DOMAIN          517..859
FT                   /note="TTL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT   REGION          48..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         673..676
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         686
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         688
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   MUTAGEN         818
FT                   /note="E->G: Dominant negative mutant; causes severe
FT                   defects in axoneme assembly."
FT                   /evidence="ECO:0000269|PubMed:19531357"
SQ   SEQUENCE   875 AA;  103066 MW;  7796CB3BD02B17EF CRC64;
     MFQQNQQSQN QQAQNLMHIQ LNGNTQLGLG ALQTINVKPI KLQSRAQSLN PNLRISERNK
     QTTQTSSNRQ NISNKSPNNL QTSKSGGLQT QNANQKLSSS SAPKKISGNF SSRVIYRAKT
     KNEDEIIKKQ SSQTSISTNG QEKKGEIIRF ATESQINNEN STPNSKIQLP PIQEKNSYKF
     YINSQSSNNQ VSQDQSPPLQ GLQAFNINKN KENQFTKKRH FDFLERTKVK NQSEETDLLK
     MHRYFRCKVS NLITGSGKKQ YYLQYLKDMK DLMTKVKQYE RVAKQNLFIN DVMNKLKKIV
     ATRAKYKYKE KIDFTRSIIM RTLGYESRQI IQQLKENMAL EEQEYEDLED DADREYEELK
     KKQEQQALDK NQKKELISSE IIANWKKMRG YQPNQKVFIC IGQYTDLKNY LKEQGWIENP
     NPESLVFDLK WVTKKKDVDK DLLLDQQITN HFQKNHNLTS KNGIALNLRN LIWYDSVDID
     TFYPRCFDLS DVQEFEDFIE EFKFTQAESI LKQYVENKLV IDQKAKQYEK YLRLKILLAC
     VALKRRTFSI EKKISLISVN TLPIISPEEW SVLNRQDNNY LFLEQNPDVY HRLSQIITRE
     MDSEESNAVD LSKLAQKYLE ASKEYDPQYD LNEKNLWIVK PAGLSRGRGI RAFDQLEPLL
     NYIMGKDVMW VAQKYMENPL TIHKKKFDIR QWVLVTEWNP LTIYFYDTCY IRICFDEYDP
     SDLQNKFAHL ANNCISKHAD NFEEKVNDTM MYLEDFVEYI KKIEGKDMFY SKIQKEMMNI
     AINSIKSCKD SIEPRRNSLE LYGYDFMVDQ NYNTWLLEIN SSPSMEYSTP VTTKLVKMGL
     EDTAKVIHHH FVEGEKRFNK NIEYGLWKNI YREQK