ID   W5NDA3_LEPOC            Unreviewed;       643 AA.
AC   W5NDA3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Tubulin tyrosine ligase-like family, member 6 {ECO:0000313|Ensembl:ENSLOCP00000018612.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000018612.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000018612.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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; AHAT01004844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5NDA3; -.
DR   STRING; 7918.ENSLOCP00000018612; -.
DR   Ensembl; ENSLOCT00000018644.1; ENSLOCP00000018612.1; ENSLOCG00000015123.1.
DR   eggNOG; KOG2158; Eukaryota.
DR   GeneTree; ENSGT00940000165637; -.
DR   HOGENOM; CLU_010131_7_2_1; -.
DR   InParanoid; W5NDA3; -.
DR   OMA; KRRLWIN; -.
DR   Proteomes; UP000018468; Linkage group LG3.
DR   Bgee; ENSLOCG00000015123; Expressed in testis and 5 other cell types or tissues.
DR   GO; GO:0005929; C:cilium; IBA:GO_Central.
DR   GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR   GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR   PANTHER; PTHR12241:SF161; TUBULIN POLYGLUTAMYLASE TTLL6; 1.
DR   Pfam; PF03133; TTL; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT   REGION          1..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   643 AA;  73576 MW;  5247A38908568D72 CRC64;
     MNSGSGAESE AGEESGKEEE EEDGDSLVQG SGGERSGVPE EERPQRSLGA GAEAQEDPRT
     GERGEESPRD EQGQTPVKRP GGDHSSPTSD SHRKIKKRKK SRSLGINLSN CKYESVRRAA
     QAVGLREASE KEDWIVCWTD FSVSMERVKD MKRYQKINHF PGMSEICRKD LLARNMNRML
     KLFPKDYNIF PKTWCLPSDY VDFQAYCRAK RNKTFICKPD SGCQGKGIYI TRNLRDINPD
     EHIVCQSYIS KPFIIDGYKF DLRLYVLVTS CDPLRVFLYQ EGLVRFATSR YSHPHSSNLD
     DICMHLTNYA INKHNDNFIR DEETGSKRKL STLKEWLELH CYDIQALWSN MEDVIIKTLI
     SAHPILKHNY CTGFPNQLGP SSCFEILGFD ILLDSKLKPW LLEVNHSPSF TTDSELDRQV
     KEALLTDTLR LLNLGVNDRR RLLEEDKRRA KERLLQKHQP PCRSRRELFL STQASWLAEQ
     EKHEEQHSGA FCRIYPRIDS EKYDKFLQHS VSLFQETVAS KAREECARKM LEELQVKQEL
     GGRIPLPGKR GGRGQQGESS GERAINRRIT QHTAPSISCN LLTKLPHILP KGSNSIRLVV
     EEEEAERLQG LEQRESLLRG LGVVELVYCL LQAGNMYSIP REI
//