GenomeNet

Database: UniProt
Entry: G5B001_HETGA
LinkDB: G5B001_HETGA
Original site: G5B001_HETGA 
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}.
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; 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
//
DBGET integrated database retrieval system