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Database: UniProt
Entry: L8IYR0_9CETA
LinkDB: L8IYR0_9CETA
Original site: L8IYR0_9CETA 
ID   L8IYR0_9CETA            Unreviewed;       357 AA.
AC   L8IYR0;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Tubulin--tyrosine ligase {ECO:0000256|ARBA:ARBA00041021};
DE            EC=6.3.2.25 {ECO:0000256|ARBA:ARBA00038960};
DE   Flags: Fragment;
GN   ORFNames=M91_19266 {ECO:0000313|EMBL:ELR60534.1};
OS   Bos mutus (wild yak).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR60534.1, ECO:0000313|Proteomes:UP000011080};
RN   [1] {ECO:0000313|EMBL:ELR60534.1, ECO:0000313|Proteomes:UP000011080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080};
RX   PubMed=22751099; DOI=10.1038/ng.2343;
RA   Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA   Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA   Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA   Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA   Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA   Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA   Wang J., Liu J.;
RT   "The yak genome and adaptation to life at high altitude.";
RL   Nat. Genet. 44:946-949(2012).
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; JH880577; ELR60534.1; -; Genomic_DNA.
DR   AlphaFoldDB; L8IYR0; -.
DR   STRING; 72004.ENSBMUP00000010065; -.
DR   Proteomes; UP000011080; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
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   Ligase {ECO:0000313|EMBL:ELR60534.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011080}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ELR60534.1"
SQ   SEQUENCE   357 AA;  40931 MW;  02BF602D11D0ED3D CRC64;
     LLPPGHWKRL RRDNPRFNLM LGERNRLPFG RLGHEPGLMQ LVNYYRGADK LCRKASLVKL
     IKTSPELAES CTWFPESYVI YPTNLKTPVA PAQNGIHPPF HSSRTDEREF FLASYNRKKE
     EGEGNVWIAK SSAGAKGEGI LISSDATELL DFIDNQGQVH VIQKYLEHPL LLEPGHRKFD
     IRSWVLVDHQ FNIYLYREGV LRTASEPYHM DNFQDKTCHL TNHCIQKEYS KNYGKYEEGN
     EMFFEAFNQY LTSALNITLE SSILLQIKHI IRSCLMSVEP AISTKHLPYQ SFQLFGFDFM
     VDEELKVWLI EVNGAPACAQ KLYAELCQGI VDIAIASVFP PPDAEQQPPQ PATFIKL
//
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