ID A0A091EUQ0_CORBR Unreviewed; 332 AA.
AC A0A091EUQ0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=N302_15182 {ECO:0000313|EMBL:KFO60726.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO60726.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO60726.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO60726.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK718983; KFO60726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091EUQ0; -.
DR STRING; 85066.A0A091EUQ0; -.
DR Proteomes; UP000052976; 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; 3.30.470.20; 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:KFO60726.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000052976}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO60726.1"
FT NON_TER 332
FT /evidence="ECO:0000313|EMBL:KFO60726.1"
SQ SEQUENCE 332 AA; 37992 MW; 6DECFD87720DB261 CRC64;
LCFPFLGHEP GLVQLVNYYR GADKLCRKAS LVKLIKTSPE LSESCTWFPE SYVIYPTNLK
TPVAPAQNGI HHLINNSRTD EREVFLAAYN RRREGKEGNV WIAKSSAGAK GEGILISSEA
AELLDFIDEQ GQVHVIQKYL ENPLLLEPGH RKFDIRSWVL VDHQYNIYLY REGVLRTSSE
PYNSANFQDK TCHLTNHCIQ KEYSKNYGRY EEGNEMFFEE FNQYLMDALN TTLENSILLQ
IKHIIRSCLM CIEPAISTKH LHYQSFQLFG FDFMVDEELK VWLIEVNGAP ACAQKLYAEL
CQGIVDVAIS SVFPLNDTGQ KMSQSSSIFI KL
//
