ID   TTLL1_TETTS             Reviewed;         413 AA.
AC   Q23SI8;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2016, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Probable alpha-tubulin polyglutamylase Ttll1;
DE            EC=6.-.-.-;
DE   AltName: Full=Tubulin-tyrosine ligase family protein 1;
GN   Name=Ttll1; ORFNames=TTHERM_00136210;
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, AND SUBCELLULAR LOCATION.
RX   PubMed=15890843; DOI=10.1126/science.1113010;
RA   Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA   Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S.,
RA   Gaertig J., Edde B.;
RT   "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT   family.";
RL   Science 308:1758-1762(2005).
CC   -!- FUNCTION: Probable tubulin polyglutamylase with a strong preference for
CC       alpha-tubulin. Modifies alpha-tubulin, generating side chains of
CC       glutamate on the gamma-carboxyl groups of specific glutamate residues
CC       within the C-terminal tail of alpha-tubulin.
CC       {ECO:0000269|PubMed:15890843}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:15890843}. Cytoplasm, cytoskeleton, cilium basal
CC       body {ECO:0000269|PubMed:15890843}. Contractile vacuole
CC       {ECO:0000269|PubMed:15890843}. Note=Associated with microtubules from
CC       basal bodies, contractile vacuole pore and oral deep fiber.
CC   -!- SIMILARITY: Belongs to the tubulin polyglutamylase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GG662639; EAR99457.2; -; Genomic_DNA.
DR   RefSeq; XP_001019702.2; XM_001019702.3.
DR   AlphaFoldDB; Q23SI8; -.
DR   SMR; Q23SI8; -.
DR   PRIDE; Q23SI8; -.
DR   EnsemblProtists; EAR99457; EAR99457; TTHERM_00136210.
DR   GeneID; 7823011; -.
DR   KEGG; tet:TTHERM_00136210; -.
DR   eggNOG; KOG2157; Eukaryota.
DR   HOGENOM; CLU_010131_0_0_1; -.
DR   InParanoid; Q23SI8; -.
DR   OrthoDB; 584228at2759; -.
DR   BRENDA; 6.3.2.B3; 6245.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR   GO; GO:0000331; C:contractile vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IDA:UniProtKB.
DR   GO; GO:0018095; P:protein polyglutamylation; IDA:UniProtKB.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   InterPro; IPR027750; TTLL1.
DR   PANTHER; PTHR12241:SF31; PTHR12241:SF31; 1.
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   Microtubule; Nucleotide-binding; Reference proteome; Vacuole.
FT   CHAIN           1..413
FT                   /note="Probable alpha-tubulin polyglutamylase Ttll1"
FT                   /id="PRO_0000249319"
FT   DOMAIN          2..370
FT                   /note="TTL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT   BINDING         184..187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         199
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
SQ   SEQUENCE   413 AA;  48267 MW;  3CD71F739E3509DA CRC64;
     MASKKLKYKT DFDKCVLTDN FAARGWTRCG DKDDDDWNIY WATVWNVRNI FNPKSGIRLN
     DMQIINHFPN HYELTRKDLM VKNFKRYKKE LEKENSPYCQ KDENGNYLYL DFIPQTFTLP
     GEYSLFVEEF HRNPNATWIV KPASRSQGKG IFLLRKIQQL KKIGGGTNSN PLQAFSLKEA
     YVVSRYIDNP LLVGGRKFDL RIYALVTSYR PLKVYLYAMG FGRFCNEQYT QDIAEMDNMF
     IHLTNVAIQK FSDKYSEKHG GKWSLQSLRY YLEMVYGTDM ANKCFDDINN IIIMSLKSVQ
     SIIINDKHCF EMYGYDILID ENCKPWLIEI NASPSLTVTG KIDKELKTEL IKNVYQIVIP
     DDWNDDSSKT GANTSTQTKV GDFNILYDEA QEKKISQQQQ QQKKNINSKT IWK