ID   TTL_BOVIN               Reviewed;         377 AA.
AC   P38584;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Tubulin--tyrosine ligase;
DE            Short=TTL;
DE            EC=6.3.2.25 {ECO:0000250|UniProtKB:Q9QXJ0};
GN   Name=TTL;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], COFACTOR, AND SUBUNIT.
RC   TISSUE=Brain;
RX   PubMed=8093886; DOI=10.1083/jcb.120.3.725;
RA   Ersfeld K., Wehland J., Plessmann U., Dodemont H., Gerke V., Weber K.;
RT   "Characterization of the tubulin-tyrosine ligase.";
RL   J. Cell Biol. 120:725-732(1993).
CC   -!- FUNCTION: Catalyzes the post-translational addition of a tyrosine to
CC       the C-terminal end of detyrosinated alpha-tubulin.
CC       {ECO:0000250|UniProtKB:Q9QXJ0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-
CC         [tubulin] + L-tyrosine = ADP + C-terminal L-alpha-aminoacyl-L-
CC         glutamyl-L-glutamyl-L-tyrosyl-[tubulin] + H(+) + phosphate;
CC         Xref=Rhea:RHEA:17605, Rhea:RHEA-COMP:16434, Rhea:RHEA-COMP:16435,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58315, ChEBI:CHEBI:149554, ChEBI:CHEBI:149555,
CC         ChEBI:CHEBI:456216; EC=6.3.2.25;
CC         Evidence={ECO:0000250|UniProtKB:Q9QXJ0};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:8093886};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000269|PubMed:8093886};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8093886}.
CC   -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase 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   PDB; 5J2U; X-ray; 2.50 A; F=1-375.
DR   PDBsum; 5J2U; -.
DR   AlphaFoldDB; P38584; -.
DR   SMR; P38584; -.
DR   STRING; 9913.ENSBTAP00000018815; -.
DR   PaxDb; P38584; -.
DR   eggNOG; KOG2157; Eukaryota.
DR   InParanoid; P38584; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004835; F:tubulin-tyrosine ligase activity; EXP:Reactome.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   Pfam; PF03133; TTL; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Ligase; Magnesium; Nucleotide-binding;
KW   Potassium; Reference proteome.
FT   CHAIN           1..377
FT                   /note="Tubulin--tyrosine ligase"
FT                   /id="PRO_0000212433"
FT   DOMAIN          3..370
FT                   /note="TTL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT   HELIX           50..52
FT                   /evidence="ECO:0007829|PDB:5J2U"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:5J2U"
FT   HELIX           69..72
FT                   /evidence="ECO:0007829|PDB:5J2U"
FT   HELIX           74..83
FT                   /evidence="ECO:0007829|PDB:5J2U"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:5J2U"
FT   STRAND          97..100
FT                   /evidence="ECO:0007829|PDB:5J2U"
FT   HELIX           130..136
FT                   /evidence="ECO:0007829|PDB:5J2U"
FT   TURN            137..139
FT                   /evidence="ECO:0007829|PDB:5J2U"
FT   STRAND          163..165
FT                   /evidence="ECO:0007829|PDB:5J2U"
FT   HELIX           167..175
FT                   /evidence="ECO:0007829|PDB:5J2U"
FT   STRAND          176..178
FT                   /evidence="ECO:0007829|PDB:5J2U"
FT   STRAND          180..184
FT                   /evidence="ECO:0007829|PDB:5J2U"
FT   STRAND          187..189
FT                   /evidence="ECO:0007829|PDB:5J2U"
FT   TURN            193..196
FT                   /evidence="ECO:0007829|PDB:5J2U"
FT   STRAND          197..207
FT                   /evidence="ECO:0007829|PDB:5J2U"
SQ   SEQUENCE   377 AA;  43270 MW;  FB7418B36CF97CEF CRC64;
     MYTFVVRDEN SSVYAEVSRL LLATGHWKRL RRDNPRFNLM LGERNRLPFG RLGHEPGLMQ
     LVNYYRGADK LCRKASLVKL IKTSPELAES CTWFPESYVI YPTNLKTPVA PAQDGIHPPL
     HSSRTDEREF FLASYNRKKE EGEGNVWIAK SSAGAKGEGI LISSDATELL DFIDNQGQVH
     VIQKYLERPL LLEPGHRKFD IRSWVLVDHQ FNIYLYREGV LRTASEPYHM DNFQDKTCHL
     TNHCIQKEYS KNYGKYEEGN EMFFEAFNRY LTSALNITLE SSILLQIKHI IRSCLMSVEP
     AISTKHLPYQ SFQLFGFDFM VDEELKVWLI EVNGAPACAQ KLYAELCQGI VDIAIASVFP
     PPDAEQQPPQ PATFIKL