ATAT1_TRYCC
ID ATAT1_TRYCC Reviewed; 329 AA.
AC Q4CQJ5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Alpha-tubulin N-acetyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=Alpha-TAT 1 {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=TAT 1 {ECO:0000255|HAMAP-Rule:MF_03130};
DE EC=2.3.1.108 {ECO:0000255|HAMAP-Rule:MF_03130};
DE AltName: Full=Acetyltransferase mec-17 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03130};
GN ORFNames=Tc00.1047053467287.10;
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener;
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
CC -!- FUNCTION: Specifically acetylates 'Lys-40' in alpha-tubulin on the
CC lumenal side of microtubules. Promotes microtubule destabilization and
CC accelerates microtubule dynamics; this activity may be independent of
CC acetylation activity. Acetylates alpha-tubulin with a slow enzymatic
CC rate, due to a catalytic site that is not optimized for acetyl
CC transfer. Enters the microtubule through each end and diffuses quickly
CC throughout the lumen of microtubules. Acetylates only long/old
CC microtubules because of its slow acetylation rate since it does not
CC have time to act on dynamically unstable microtubules before the enzyme
CC is released. {ECO:0000255|HAMAP-Rule:MF_03130}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[alpha-tubulin] = CoA + H(+) + N(6)-
CC acetyl-L-lysyl-[alpha-tubulin]; Xref=Rhea:RHEA:15277, Rhea:RHEA-
CC COMP:11278, Rhea:RHEA-COMP:11279, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:61930; EC=2.3.1.108; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03130};
CC -!- SIMILARITY: Belongs to the acetyltransferase ATAT1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03130}.
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DR EMBL; AAHK01002446; EAN82545.1; -; Genomic_DNA.
DR RefSeq; XP_804396.1; XM_799303.1.
DR AlphaFoldDB; Q4CQJ5; -.
DR SMR; Q4CQJ5; -.
DR STRING; 5693.XP_804396.1; -.
DR PaxDb; Q4CQJ5; -.
DR EnsemblProtists; EAN82545; EAN82545; Tc00.1047053467287.10.
DR GeneID; 3533827; -.
DR KEGG; tcr:467287.10; -.
DR eggNOG; KOG4601; Eukaryota.
DR OrthoDB; 1312675at2759; -.
DR Proteomes; UP000002296; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0019799; F:tubulin N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071929; P:alpha-tubulin acetylation; IEA:UniProtKB-UniRule.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03130; mec17; 1.
DR InterPro; IPR038746; Atat.
DR InterPro; IPR007965; GNAT_ATAT.
DR InterPro; IPR003657; WRKY_dom.
DR PANTHER; PTHR12327; PTHR12327; 1.
DR Pfam; PF05301; Acetyltransf_16; 1.
DR PROSITE; PS51730; GNAT_ATAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..329
FT /note="Alpha-tubulin N-acetyltransferase 1"
FT /id="PRO_0000402086"
FT DOMAIN 5..185
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT REGION 218..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 119..132
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT BINDING 155..164
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT SITE 58
FT /note="Crucial for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
SQ SEQUENCE 329 AA; 36884 MW; A57BCEF71D02322C CRC64;
MSSTSQVALL PKLSLPDGVT VWDGTALEYE RRCNNVDEHA VHLMQTINIL GIRSKEAQCL
NTVLTSVARL RENRQARVYL LCQDGYGVGI LKMGVKKLFV THPSYSSLVE IDPLCVLDFF
VDTSFQRKGF GKTLFDAMLL NEGLNPGEVA IDRPSVKFLA FLQKYYGLVE YTPQSNNFVV
FHRYFDKWQP QRGKGHWGGN AVPTRSLVRP QNCLRVYPKY QSTTGPNNNF EEDATHRTPP
PPPLPPPLVP QGSVTSPGVG KKTAYELQYE EYLREQAYRR RQGGDPRLQP VPNPVSSSEI
VAASCGARRR MSPTRSGVQY NIISGTPEH
