ID   TTL3B_TETTS             Reviewed;        1179 AA.
AC   P0CAZ0;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2016, sequence version 2.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Tubulin glycylase 3B;
DE            EC=6.3.2.-;
GN   Name=TTLL3B; ORFNames=TTHERM_00125600;
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, AND DISRUPTION
RP   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: Polyglycylase which modifies tubulin, generating side chains
CC       of glycine on the gamma-carboxyl groups of specific glutamate residues
CC       within the C-terminal tail of tubulin. Polyglycylates tubulin, with a
CC       preference for alpha-tubulin toward beta-tubulin.
CC       {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 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; GG662699; EAR95994.2; -; Genomic_DNA.
DR   RefSeq; XP_001016239.2; XM_001016239.2.
DR   AlphaFoldDB; P0CAZ0; -.
DR   SMR; P0CAZ0; -.
DR   EnsemblProtists; EAR95994; EAR95994; TTHERM_00125600.
DR   GeneID; 7838273; -.
DR   KEGG; tet:TTHERM_00125600; -.
DR   eggNOG; KOG2157; Eukaryota.
DR   HOGENOM; CLU_275415_0_0_1; -.
DR   InParanoid; P0CAZ0; -.
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; IDA:UniProtKB.
DR   GO; GO:0070737; F:protein-glycine ligase activity, elongating; 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..1179
FT                   /note="Tubulin glycylase 3B"
FT                   /id="PRO_0000381798"
FT   DOMAIN          790..1152
FT                   /note="TTL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT   REGION          177..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          853..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         965..968
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         978
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         980
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
SQ   SEQUENCE   1179 AA;  137036 MW;  8D1B99391547256A CRC64;
     MFSIDIQGKS MSLCDPTSKI KQMQQQQQQL QQGTNNGIQK DQQLPNMIIN GNSNSYLNNG
     SNLQQQAVIQ QSNHKQSQIK YNSPLSHQQH HQFKIGHQNK LEYLRQQQAQ KYNQIYQLDP
     QLQQQNQMFQ QHQYMQNVQM QQQLLYQGNQ EVFPPFNQIA NGSAQNSILL QQYLSNNKGQ
     TNNSNRENGG NFHSEQSPKS AAGSVVSGNG SNTQFAANIL RNSNIIQQQN EFRFQQIQQT
     HQLLHSLVQQ QPQPLSQQHS NQSSQSSNPQ SQSPLPLSIS SQQPVISMAN YFNQPSQQSN
     SLFNGQQPTM FNSSENFQQK NILYSCVGNP NNPYNHHINN PYLQEKRYYK SSKLPKIKKE
     NKPQQAFSDI RPSSREKSAR FHLAASINTI LNQNGSTSVN TQNNENMVQT LKGHSYSAVT
     EKSNIGQQEV NIPTTSKTQT LIKEHSLTNI NSASKENNQV TLASNSNQTS KKAYENLMSA
     ENDEEDKLKC IRYFRYNLGQ LLHILGKKEI YFSNLNSKKP IKTFASITQQ LGQKHMNLLS
     KNTINIINKV KKIVATKGKY KYRERFNFLH SAQLKSINYD VRKRLNQIQD KKVLSNTKSK
     DEEESSDDDE TPVKSKSNNQ NAVQQTDLAK WKKYNRLDPK TKVFIIKGGY GDLRKALQER
     GWVENPDYFS PCFDLKWTCK VQDIDYDNLQ ENQVVNHFDN NQTFTSKYGL ARNLRTLIHS
     ENIDVYKFFP RCFDLGDLQE FEDFIENFKV AKAESLVHRF KDMLKNGIES IDDKLELKIR
     LCNEVASRKF IDFYETVDFI FNYDVLPCVS PEEWEIISKD EFQLDNKKIE FYLERLRSHP
     TFKHLYYSNS QSQKQHMNKR KNSHRISVNH NHNDPIEEES AQSSTSLKQD SLQRFSSKSQ
     ELLDLCNQTL KKSSEKDPQH HLNGYRNIWI VKPNFLSRGR GIKCFNSLDK IMDYVVGKET
     QFVVQKYIEN PLLINNKKFD MRQWAIVQDF CPPRIWFFEE CYIRLCSVEH NIDDLNNRFV
     HLTNNIVQKY NKDAYADKDD LMMSQEQFAQ YLKETEGRDV FYEEIQPKLK QMVIQSLKSC
     QDQVGARKNS MEFIGYDFMI DSNYQPWLIE INSSPSMEYS TSITEELVQR VLQDTTKVIV
     DYSMAKKGTK KNVDTGGFKL IYKGEKQTKN NKVLASYKK