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Database: UniProt
Entry: A0A452E7K7_CAPHI
LinkDB: A0A452E7K7_CAPHI
Original site: A0A452E7K7_CAPHI 
ID   A0A452E7K7_CAPHI        Unreviewed;       377 AA.
AC   A0A452E7K7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Tubulin--tyrosine ligase {ECO:0000256|ARBA:ARBA00041021};
DE            EC=6.3.2.25 {ECO:0000256|ARBA:ARBA00038960};
GN   Name=TTL {ECO:0000313|Ensembl:ENSCHIP00000008054.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000008054.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000008054.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000008054.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the post-translational addition of a tyrosine to
CC       the C-terminal end of detyrosinated alpha-tubulin.
CC       {ECO:0000256|ARBA:ARBA00037791}.
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:0000256|ARBA:ARBA00036187};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|ARBA:ARBA00001958};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC       {ECO:0000256|ARBA:ARBA00006820}.
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DR   EMBL; LWLT01000009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005686802.2; XM_005686745.3.
DR   AlphaFoldDB; A0A452E7K7; -.
DR   STRING; 9925.ENSCHIP00000008054; -.
DR   Ensembl; ENSCHIT00000015806.1; ENSCHIP00000008054.1; ENSCHIG00000011356.1.
DR   GeneID; 102180860; -.
DR   KEGG; chx:102180860; -.
DR   CTD; 150465; -.
DR   GeneTree; ENSGT00940000161907; -.
DR   OMA; CAQKLYS; -.
DR   OrthoDB; 160834at2759; -.
DR   Proteomes; UP000291000; Chromosome 11.
DR   Bgee; ENSCHIG00000011356; Expressed in frontal cortex and 17 other cell types or tissues.
DR   GO; GO:0005876; C:spindle microtubule; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004835; F:tubulin-tyrosine ligase activity; IEA:Ensembl.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:Ensembl.
DR   GO; GO:0090235; P:regulation of metaphase plate congression; IEA:Ensembl.
DR   Gene3D; 3.40.50.11480; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   PANTHER; PTHR46570; TUBULIN--TYROSINE LIGASE; 1.
DR   PANTHER; PTHR46570:SF1; TUBULIN--TYROSINE LIGASE; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291000}.
SQ   SEQUENCE   377 AA;  43286 MW;  6ED407E88CA94107 CRC64;
     MYTFVVRDEN SSVYAEVSRL LLATGHWKRL RRDNPRFNLM LGERNRLPFG RLGHEPGLMQ
     LVNYYRGADK LCRKASLVKL IKTSPELAES CTWFPESYVI YPTNLKTPVA PAQNGIHPPL
     HSSRTDEREF FLASYNRKKE EGEGNVWIAK SSAGAKGEGI LISSDATELL DFIDNQGQVH
     VIQKYLERPL LLEPGHRKFD IRSWVLVDHQ FNIYLYREGV LRTASEPYHM DNFQDKTCHL
     TNHCIQKEYS KNYGKYEEGN EMFFEAFNQY LTSALNITLE SSILLQIKHI IRSCLMSIEP
     AISTKHLPYQ SFQLFGFDFM VDEELKVWLI EVNGAPACAQ KLYAELCQGI VDIAIASVFP
     PPDTEQQPPQ PATFIKL
//
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