ID   TTL3D_TETTS             Reviewed;        1034 AA.
AC   Q23K29;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2016, sequence version 2.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Tubulin glycylase 3D;
DE            EC=6.3.2.-;
GN   Name=TTLL3D; ORFNames=TTHERM_00196050;
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 {ECO:0000269|PubMed:19531357}.
CC       Note=Present in the cell body and not in 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; GG662673; EAR97014.2; -; Genomic_DNA.
DR   RefSeq; XP_001017259.2; XM_001017259.2.
DR   AlphaFoldDB; Q23K29; -.
DR   SMR; Q23K29; -.
DR   EnsemblProtists; EAR97014; EAR97014; TTHERM_00196050.
DR   GeneID; 7825803; -.
DR   KEGG; tet:TTHERM_00196050; -.
DR   eggNOG; KOG2157; Eukaryota.
DR   HOGENOM; CLU_297097_0_0_1; -.
DR   InParanoid; Q23K29; -.
DR   OrthoDB; 143220at2759; -.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1034
FT                   /note="Tubulin glycylase 3D"
FT                   /id="PRO_0000381800"
FT   DOMAIN          571..930
FT                   /note="TTL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1002..1034
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         741..744
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         754
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         756
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
SQ   SEQUENCE   1034 AA;  121283 MW;  DEFF8B6E51BF0AF7 CRC64;
     MINSHHTSQQ TLNKESKSQM DKSYNIDDSI VDAKFENYTK KYQDDKLNKI LHTYIKNPQI
     LMDEEKEIKE RFLAKQMKDV AATKQKFDTK NKLQQLELEN ENSQNNSYKT SNNLSKEEVI
     AVLQKQNRKS QVNSVLADNS NIQNDFYPQY RKPKNPTTKK RQSTDYTKRN TFQLENLNIQ
     QQLNNKDSLN QQNQQQQDLA KNRVDNSQNQ DIQARLYERT ELQKLRIKQK EEEQAALKNK
     RQTNRSQSIE QNVNFVQNDN QKLIDRHKEY LKQLKQQVTI EKETQKQLKK KDEENKIRLR
     NSVLASIKND LTEQRKLIQE NHNLFLSKST VSQSAKQISL PEINQSLTIC LEKQKSEVEQ
     EKKAVLTSQA FFRQSSLREI EETNEKIESK TNLSKVKKLR PLPFISSMVE WKKKQRIPAD
     SKIFIVMGGY KDFKKALLKR GWIENPQTNS PCFDLKWTLL GKDIDYDNIL PNQIVNHFEN
     NSKICSKIGL LNSLKNLYWF DNADLNCFFP QCFDMNDPDE FNDFVKNFKL SKAVSVLKKY
     LRLYLEKDEK YNNCKIQAQV ALQVLTRYYN DINNVIDDEK QASEYFKSIP DDEWEILASD
     EMSNEDLAKK KHFEWIKKIK LAYQGIKVKA QVKKKKKKSL AMIKKMISNE AIKRKQDGEK
     QQIDSSDSED EEVEMDDFTS AVNQFLNQRE KCDPQFNLKG EDNIWIVKPA GLSRGRGITC
     YKNLVEIIDH AKSMELQMIV QKYIENPVLI KQRKFDIRIW VLVTDWNPLA IWYFDECYVR
     FSADSYSTKN LSNKFQHLTN NAISKKKAQQ GQDEITLQGN MYTQEQLENF FIETEGYNVF
     QQKIKPQIIN IIKWSILSCS DTVESRKNSM ELFGYDIMID TNFNPWLLEV NTSPSLEYST
     EITKKLVKQV LEDVAKVVVD YGMAQKSGIK KSELQKIGTG KFIKIYQGLE IQDKGINSIQ
     KNFICEGSKM KIRKPKKQKK NTKLDKKQNL QQDLTINNQI NHDQKQFSSQ QANNIETYSR
     PQTAKSQTQS SKKL