TTL_YEAST
ID TTL_YEAST Reviewed; 753 AA.
AC P38254; D6VQ95;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Probable tubulin--tyrosine ligase PBY1;
DE EC=6.3.2.25;
DE AltName: Full=P-body-associated protein 1;
GN Name=PBY1; OrderedLocusNames=YBR094W; ORFNames=YBR0821;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 450.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-753.
RC STRAIN=ATCC 26109 / X2180;
RA Dekker P.J.T., Hoekert W., van Oosterum K., Grivell L.A.;
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17307817; DOI=10.1261/rna.355807;
RA Sweet T.J., Boyer B., Hu W., Baker K.E., Coller J.;
RT "Microtubule disruption stimulates P-body formation.";
RL RNA 13:493-502(2007).
CC -!- FUNCTION: Probable P-body-associated tubulin--tyrosine ligase.
CC {ECO:0000250, ECO:0000269|PubMed:17307817}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC Cytoplasm, P-body {ECO:0000269|PubMed:17307817}.
CC -!- MISCELLANEOUS: Present with 1770 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC {ECO:0000305}.
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DR EMBL; X78993; CAA55599.1; -; Genomic_DNA.
DR EMBL; Z35963; CAA85047.1; -; Genomic_DNA.
DR EMBL; X69881; CAA49508.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07215.2; -; Genomic_DNA.
DR PIR; S48261; S48261.
DR RefSeq; NP_009652.2; NM_001178442.2.
DR PDB; 6Y3Z; X-ray; 3.49 A; P=330-753.
DR PDBsum; 6Y3Z; -.
DR AlphaFoldDB; P38254; -.
DR SMR; P38254; -.
DR BioGRID; 32800; 85.
DR DIP; DIP-1585N; -.
DR IntAct; P38254; 7.
DR MINT; P38254; -.
DR STRING; 4932.YBR094W; -.
DR iPTMnet; P38254; -.
DR MaxQB; P38254; -.
DR PaxDb; P38254; -.
DR PRIDE; P38254; -.
DR EnsemblFungi; YBR094W_mRNA; YBR094W; YBR094W.
DR GeneID; 852391; -.
DR KEGG; sce:YBR094W; -.
DR SGD; S000000298; PBY1.
DR VEuPathDB; FungiDB:YBR094W; -.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000164409; -.
DR HOGENOM; CLU_007204_0_0_1; -.
DR InParanoid; P38254; -.
DR OMA; HTHKHFK; -.
DR BioCyc; YEAST:G3O-29058-MON; -.
DR PRO; PR:P38254; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38254; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0004835; F:tubulin-tyrosine ligase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.1210.10; -; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR002828; SurE-like_Pase/nucleotidase.
DR InterPro; IPR036523; SurE-like_sf.
DR InterPro; IPR027746; TTL.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR PANTHER; PTHR47551; PTHR47551; 1.
DR Pfam; PF01975; SurE; 1.
DR Pfam; PF03133; TTL; 1.
DR SUPFAM; SSF64167; SSF64167; 1.
DR TIGRFAMs; TIGR00087; surE; 1.
DR PROSITE; PS51221; TTL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Ligase; Magnesium; Potassium; Reference proteome.
FT CHAIN 1..753
FT /note="Probable tubulin--tyrosine ligase PBY1"
FT /id="PRO_0000212448"
FT DOMAIN 343..734
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT CONFLICT 352..355
FT /note="HALK -> TPE (in Ref. 4; CAA49508)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="A -> R (in Ref. 1; CAA55599 and 2; CAA85047)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="H -> R (in Ref. 4; CAA49508)"
FT /evidence="ECO:0000305"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 393..397
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 416..427
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 435..438
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 454..457
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 461..468
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 490..494
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 495..507
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 541..546
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 562..571
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT TURN 572..574
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 575..580
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 583..586
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 626..629
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 630..632
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 634..636
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 638..660
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT TURN 664..666
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 673..684
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 689..697
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 700..702
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 709..722
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 724..726
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT HELIX 732..735
FT /evidence="ECO:0007829|PDB:6Y3Z"
FT STRAND 742..746
FT /evidence="ECO:0007829|PDB:6Y3Z"
SQ SEQUENCE 753 AA; 86353 MW; 925C4E4CAB6679E9 CRC64;
MRVLITNDDG PLSDQFSPYI RPFIQHIKRN YPEWKITVCV PHVQKSWVGK AHLAGKNLTA
QFIYSKVDAE DNTFWGPFIQ PQIRSENSKL PYVLNAEIPK DTIEWILIDG TPASCANIGL
HLLSNEPFDL VLSGPNVGRN TSAAYITSSG TVGGAMESVI TGNTKAIAIS WAYFNGLKNV
SPLLMEKASK RSLDVIKHLV KNWDPKTDLY SINIPLVESL SDDTKVYYAP IWENRWIPIF
NGPHINLENS FAEIEDGNES SSISFNWAPK FGAHKDSIHY MDEYKDRTVL TDAEVIESEM
ISVTPMKATF KGVNHLLGEL KLTEEENNLS KTNNLIVVSI DPMEYIYKPL THALKKYLPQ
VEIVSNLPEF DNGGCEKEMK VFHYGDYEQL DMDKLMELPN NYFTNSYIYR KALIRKHFLS
HTIQTYTAKN PESILKKAYL ESFTIDLDYA EFLDDALDEN WELRQELENE SQDKWWIVKP
SMSDKGQGIR VFKTIEDLQA IFDSFDDEDS EAEESGNDDD ADDVNGEFMD NNKVNISQLR
HFIIQEYLTN PLLLASMDNR KFHIRCYVVC RGDLQVFVYD RMLALFAAKP FVPLDPYAYS
VTDLKDLECH LTNTCLQSKK KDKDSSVLEF DSIEEIPNER KSNIKEQIHS ITNDVFLAAV
NVNRLNFQPL PNAFETYGVD FLIDSNYEVK LLEINAFPDF KQTGKDLKNL IDELFDDTVK
YCVTPIFNEN RNKTDDETDP NFVKVIDYTS NGW
