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 24-JAN-2024, entry version 48.
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 STRING; 312017.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; 7265at2759; -.
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 Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR PANTHER; PTHR45870; TUBULIN MONOGLYCYLASE TTLL3; 1.
DR PANTHER; PTHR45870:SF2; TUBULIN MONOGLYCYLASE TTLL3; 1.
DR Pfam; PF03133; TTL; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 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
//
