ID A0A3B3S208_9TELE Unreviewed; 403 AA.
AC A0A3B3S208;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Tubulin--tyrosine ligase {ECO:0000256|ARBA:ARBA00041021};
DE EC=6.3.2.25 {ECO:0000256|ARBA:ARBA00038960};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000024091.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000024091.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3B3S208; -.
DR Ensembl; ENSPKIT00000004792.1; ENSPKIP00000024091.1; ENSPKIG00000007468.1.
DR GeneTree; ENSGT00940000161907; -.
DR OrthoDB; 160834at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005524; F:ATP binding; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT REGION 369..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 403 AA; 45484 MW; 5F7FE825BFD00146 CRC64;
MSMPLYTFVT RDENSSVYAE VSKILISTGQ WKRLKKDNPR FNLMLGERNR LPFGRLGHEP
GLVQLVNYYR GADKLCRKAS LVKLIKTSPE LSDSCNWFPE SYIIYPTNLN TPVAPAKNGM
SHMKNNPKTD EREVFLASYH LKKMNGEGTV WIAKSSAGAK GAGILISSDA NQLLEFIDNQ
GQVHVIQKYL ENPLLLQPGN RKFDIRSWVL VDHQYNIYLY REGVLRTSSE PYNSSDFEDK
TSHLTNHCIQ KEHSQNYGRY EEGNEMFFDE FRQYLLNTHS VSLEAAILPQ IKQIIRSCLV
SIEPAISTKH LSYQSFQLFG FDFMVDENLK VWLIEINGAP ACAQKLYSEL CHGIVDMAIS
SVFTLNSSDS SASSSASSSL SSSSSCSSPK SRPPNHHGPF IKL
//
