ID   TTL3C_TETTS             Reviewed;        1065 AA.
AC   Q23FE2;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2016, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Tubulin glycylase 3C;
DE            EC=6.3.2.-;
GN   Name=TTLL3C; ORFNames=TTHERM_00378750;
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 assembling
CC       locomotory 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; GG662706; EAR95211.2; -; Genomic_DNA.
DR   RefSeq; XP_001015456.2; XM_001015456.2.
DR   AlphaFoldDB; Q23FE2; -.
DR   SMR; Q23FE2; -.
DR   EnsemblProtists; EAR95211; EAR95211; TTHERM_00378750.
DR   GeneID; 7828273; -.
DR   KEGG; tet:TTHERM_00378750; -.
DR   eggNOG; KOG1836; Eukaryota.
DR   eggNOG; KOG2157; Eukaryota.
DR   HOGENOM; CLU_285063_0_0_1; -.
DR   InParanoid; Q23FE2; -.
DR   OrthoDB; 1137333at2759; -.
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..1065
FT                   /note="Tubulin glycylase 3C"
FT                   /id="PRO_0000381799"
FT   DOMAIN          633..1009
FT                   /note="TTL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT   REGION          1..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..326
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..477
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..754
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         821..824
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         834
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         836
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
SQ   SEQUENCE   1065 AA;  125946 MW;  821DA2EF6FB71B0C CRC64;
     MSSLDEGLKQ MSQQEYRNEE QNQEGNQEDL NNQNDHNLNN NELDSLSSPP SDNYNEEEFE
     QEDDIKPDIK IYQNASQNNI SQTQRISQTQ LPQQQGGGGK RNSSLLQKEH YHQKNQEIIQ
     KLMEKKKKEQ EEKEKKELKL KKREDKLRKR MLEEAAKIRE QKEVNLESQT EQSDHSNVTK
     SKKLKFKSVQ DIYQLVVIQG KYQREQLTDK QQQELNEFES RLNEEKTTII KMQQVYRSRQ
     ITFLEELKKK QEKKKQEEEQ QKLKQEKIQT KLREQYENVN SNLYAETELF KQKKQEITKV
     STQKQLVRAS SAEGDKEKDD KKDIAKKIQQ KNQEYIEKLK EKKRQEIAKE EEEKKKKEQL
     KEKMKDFVLV NIKKDIENGV FFVDVPEKKP KKEKKKNESK EDNIQITSPK LNSTKSLSSQ
     ITRKTNDAKK VEKLPKIKDS NKENHSKERN EDNEEGDDGE YECDEGDEGA SDGEDEDDGN
     GSAIKRKLRK YPFITDLELW KKKQRLPADI KVFIVTGGYH DISKALKKRG WIANPDTKSP
     CYNFRWSLQT KDIDYENLKD FQIVNHFQKS ACITTKVGLC KSLRNLVWHE NVDIDTFYPR
     CFDLNDTEDF ENFVEEFKSS KAESILKRYM RMYFEKDPDI EKIKKQAVIA FNVCERKMKE
     LDEIIDDPNS IQLITKKEWN ILSADELTEE KLAQKKYEQW LERIEGKNKQ KPKKKKKKSK
     KDKQQGDTEK KEEEEGEAED EEEDEEDEEE EEKQMDEFTL KVHQILKRYK VKYPQDCLTG
     EDNVWIIKPA GLSRGRGITC YNNLVEILDH VKSKESQWVI QKYIENPLII KKRKFDIRVW
     ILVTDWNPLT IWHYTDCYVR FSVDDYDTEN LQNKFTHLTN NMVSKLKQRD EKDDITELGS
     MYFKENFINY LKEKEGYDVF TDKIEPQIVR AIIMSLKSVQ DNIENRKNSI EMYGYDFMVD
     DLYNTWLIEI NSSPSMEYST PVTERLVKAV SEDIVKVVID YGMEKSKKAR KNIETGAFKR
     IYKGKYVEEK TNVVGLNLIC EGVALKKGKK NSNVAKVNNL KPNFS