ID   A0A1Q9EQX7_SYMMI        Unreviewed;      1179 AA.
AC   A0A1Q9EQX7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Putative alpha-tubulin polyglutamylase Ttll1 {ECO:0000313|EMBL:OLQ09787.1};
GN   Name=Ttll1 {ECO:0000313|EMBL:OLQ09787.1};
GN   ORFNames=AK812_SmicGene6568 {ECO:0000313|EMBL:OLQ09787.1};
OS   Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS   microadriatica).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC   Symbiodinium.
OX   NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ09787.1, ECO:0000313|Proteomes:UP000186817};
RN   [1] {ECO:0000313|EMBL:OLQ09787.1, ECO:0000313|Proteomes:UP000186817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ09787.1,
RC   ECO:0000313|Proteomes:UP000186817};
RA   Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA   Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA   Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT   "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT   adaptations to a symbiotic lifestyle.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000256|ARBA:ARBA00004120}.
CC   -!- SIMILARITY: Belongs to the tubulin polyglutamylase family.
CC       {ECO:0000256|ARBA:ARBA00006118}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLQ09787.1}.
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DR   EMBL; LSRX01000090; OLQ09787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q9EQX7; -.
DR   OrthoDB; 179787at2759; -.
DR   Proteomes; UP000186817; Unassembled WGS sequence.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   PANTHER; PTHR12241:SF31; POLYGLUTAMYLASE COMPLEX SUBUNIT TTLL1; 1.
DR   PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   Pfam; PF03133; TTL; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cilium {ECO:0000256|ARBA:ARBA00023069};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186817}.
FT   DOMAIN          425..548
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|Pfam:PF00293"
FT   REGION          630..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1179 AA;  131194 MW;  CFB88B104AADCA59 CRC64;
     MDVAVIFRLP GPAHRDIISP DASGATLEAG SESARRRGFM HMHDSWLEQS ISARAEESSD
     PAVKLFVISS AWPYKPTHSP LQPFVLLHGA TGPADFTGPE SACHQHIGLA RSVLRRDQND
     LLFVIDVSDV AECHDWQAEV VRPARSRRML ERWFAKFNPR EATVIAFGND AELWVPLVRL
     HDEPRISKLI VLGDPPCQKS VAQLAAGHVE VCILGAGFSM EALVDAMGSQ SSASRLDVED
     LHFTFVNFVQ TGHNVTLSTV ESFRSLTRSV LPQEGPPGPL VAGKSLGLRP PVSVDPDPIP
     ADVVALLNNK VERDILPSTF STQFLAPGTA FSGLIVNIQT CSYDEDASVL RALLADAHGS
     VEGLFPTTLA KMILPGKSVA VSGRTLSLQG RLLVLGQEAT PNQGLRDGYM PVSDGRRNVS
     DVSRKFGCLV LRGRKCVLAR DCDKQLYIPV DEARNSETAQ QAATRAVAES CDIYPEEFAL
     LGDVPPAVYY EKAGQAKPQV VSIFAAVATS PPPPGSAEDT DTIEDVEDMY DWFPFEQALS
     LLSVNERHAI ARLAHGALAS IIVRSPHVLA FARRLDAVEV SDGTRTNARA AHFRLVWAEA
     EEFGGCTAGN SADAMRFLCE FVEKEEARLG LGLSPPRPPP SGAPQSSLTT LRMDPGLEQL
     SAGKVALEKQ AMTKSEVDDV PRDLGNFLAK KELPPYDMGS YVPPEALFCW TESDFASYIN
     SGGFVKPKLK CQYYLSPENP QTIVDLLEPI LSELNWTCTV DSHSGREESL AQVTDYMGMP
     VPRLKKQDDG SLEVAPVFIW EASRNMIDHG PTLKLVNRLN GVNMFTKVGM LELIRERCIE
     RDIPINFPPP WYPLTFTLPD DLEQWKRHAE ANPHKKWIYK PSCEVRRWAE ASSLSPARML
     LELLPRTCCK LTVEVNKISD VDSKVFDPNE PPLKERNFAN VGIIQEYMVN PMLLENRKFA
     IRVYMLVART KPLLTFHYNF GYVKRLAPSR RHCAGVQGTE WQPAGCGEFY DENKFNREDL
     FRHITEQEFQ KKQDDFGGSA ASQLMSIEDL DKYLQENYGI PAFRLNFWQQ VKAICMEAFL
     PQKVHEIQSV GQFEIFGLDI IVDADQRLYL LEANRDPSWV LDTQVKKAII PDMIREMMEI
     VLWAHSDEGK NKEAMLHSPM RGFEVLIDEA FDFQAVDVE
//