ID V8P7C9_OPHHA Unreviewed; 320 AA.
AC V8P7C9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Tubulin--tyrosine ligase {ECO:0000256|ARBA:ARBA00041021};
DE EC=6.3.2.25 {ECO:0000256|ARBA:ARBA00038960};
DE Flags: Fragment;
GN Name=TTL {ECO:0000313|EMBL:ETE69787.1};
GN ORFNames=L345_04400 {ECO:0000313|EMBL:ETE69787.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE69787.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE69787.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE69787.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE69787.1}.
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DR EMBL; AZIM01000694; ETE69787.1; -; Genomic_DNA.
DR AlphaFoldDB; V8P7C9; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:ETE69787.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE69787.1"
FT NON_TER 320
FT /evidence="ECO:0000313|EMBL:ETE69787.1"
SQ SEQUENCE 320 AA; 36961 MW; B629ED9DDF4D016A CRC64;
MYTFVVRDEN SSIYAEVSKI LLCTGQWKRL KRDNPRFNLM LGERNRLPFG RLGHEPGLTQ
LIKTSPELVE ACTWFPESYV IYPTDLKTPV APAENGLHHL INNTRTDERE VFLSSYQKRK
ESGEGNVWIA KSSAGAKGEG ILISSEATEL LDFIDNQGQV HVIQKYLEKP MLLEPGHRKF
DIRSWVLVDH QYSIYLYREG VLRTSSEPYN SANFLDKTCH LTNHCIQKEY SKNYGRYEEG
NEMFFEEFNQ YLVNTLNVTL ENTILLQVKN IIRSCLTCIE PAISTKHLHY QSFQLFGFDF
MVDEDLKVWL IEVNGAPACA
//
