ID K2MLM0_TRYCR Unreviewed; 416 AA.
AC K2MLM0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Tubulin--tyrosine ligase {ECO:0000256|ARBA:ARBA00041021};
DE EC=6.3.2.25 {ECO:0000256|ARBA:ARBA00038960};
GN ORFNames=MOQ_009735 {ECO:0000313|EMBL:EKF26569.1};
OS Trypanosoma cruzi marinkellei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF26569.1, ECO:0000313|Proteomes:UP000007350};
RN [1] {ECO:0000313|EMBL:EKF26569.1, ECO:0000313|Proteomes:UP000007350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|EMBL:EKF26569.1,
RC ECO:0000313|Proteomes:UP000007350};
RX PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA Andersson B.;
RT "Comparative genomic analysis of human infective Trypanosoma cruzi lineages
RT with the bat-restricted subspecies T. cruzi marinkellei.";
RL BMC Genomics 13:531-531(2012).
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:EKF26569.1}.
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DR EMBL; AHKC01020357; EKF26569.1; -; Genomic_DNA.
DR AlphaFoldDB; K2MLM0; -.
DR EnsemblProtists; EKF26569; EKF26569; MOQ_009735.
DR OrthoDB; 160834at2759; -.
DR Proteomes; UP000007350; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000313|EMBL:EKF26569.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007350}.
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 47371 MW; D1E8F9E4CA226D4A CRC64;
MDAQLFATAD ADPTVPRPKE ESERQQRHCQ DTEQSETQGD ESSLFFLGES AFSVYEEMAA
QLRQSGWREA RSKGLIVQCD LVLGDRFTIP YSLLRCERLP ATSRYGGYRW INYFRGSHRL
TLKASMARIL SGSDATYDAW MPRSFVLGGE QKKRPDDRET FLRWVEQHPE GTWIIKPSSG
SKGKDILLTR GLARIETFIQ ELDPSSRSIF VAQQYVDRPL LYCGRKFDVR VWAFLKTPYD
IYAFSQGSCR TSSVLYDADN FGNTLVHLTN HCLQEGSPQF GQYETGNELW FPQLSAYLRE
VYKEDVFGKK ILPQIGNIIL RTLLVMKGEL EVLPDMPYKC FQLFGYDLIV DEQLNVFLLE
INGSPGVATK YLHPVVKETL AIVSGDDASR VWDVDTVRFV KLWGVGDALP DGAARM
//
