ID G5B001_HETGA Unreviewed; 343 AA.
AC G5B001;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=GW7_08918 {ECO:0000313|EMBL:EHB02612.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB02612.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB02612.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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; JH167710; EHB02612.1; -; Genomic_DNA.
DR AlphaFoldDB; G5B001; -.
DR STRING; 10181.G5B001; -.
DR eggNOG; KOG2157; Eukaryota.
DR InParanoid; G5B001; -.
DR OMA; CAQKLYS; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140096; F:catalytic activity, acting on a protein; IEA:UniProt.
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:EHB02612.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHB02612.1"
SQ SEQUENCE 343 AA; 39242 MW; 8D65785F323BF996 CRC64;
NPRFNLMLGE RNRLPFGRLG HEPGLLQLVN YYRGADKLCR KASLVKLIKT SPELAESCTW
FPESYVIYPT NLKTPVAPAQ NGIQPQVSNS RTDEREFFLA SYNKKKEDGE GNIWIAKSSA
GAKGEGILIS SEASELLDFI DNQGQVHVIQ KYLEHPLLLE PGHRKFDIRS WVLVDHQYNI
YLYREGVLRT ASEPYHVDDF QDKTCHLTNH CIQKEYSKNY GKYEEGNEMF FEEFNQYLMS
ALNITLEASI LQQIKHIIRS CLMSVEPAIS TRYLPYQSFQ LFGFDFMVDK ELKVWLIEVN
GAPACAQKLY AELCQGIVDL AISSVFPPPD VEQQPQSAAF IKL
//