ID B6JXW5_SCHJY Unreviewed; 904 AA.
AC B6JXW5;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Alpha,alpha-trehalose-phosphate synthase {ECO:0000313|EMBL:EEB06383.1};
GN Name=tps3 {ECO:0000313|JaponicusDB:SJAG_01427};
GN ORFNames=SJAG_01427 {ECO:0000313|EMBL:EEB06383.1};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB06383.1, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB06383.1, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000256|ARBA:ARBA00005409}.
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DR EMBL; KE651168; EEB06383.1; -; Genomic_DNA.
DR RefSeq; XP_002172676.1; XM_002172640.2.
DR AlphaFoldDB; B6JXW5; -.
DR STRING; 402676.B6JXW5; -.
DR EnsemblFungi; EEB06383; EEB06383; SJAG_01427.
DR GeneID; 7051382; -.
DR JaponicusDB; SJAG_01427; tps3.
DR VEuPathDB; FungiDB:SJAG_01427; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_3_3_1; -.
DR OMA; KFRCVPA; -.
DR OrthoDB; 1023at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IBA:GO_Central.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IBA:GO_Central.
DR GO; GO:0005992; P:trehalose biosynthetic process; IBA:GO_Central.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IBA:GO_Central.
DR CDD; cd03788; GT20_TPS; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR003337; Trehalose_PPase.
DR PANTHER; PTHR10788:SF129; ALPHA,ALPHA-TREHALOSE-PHOSPHATE SYNTHASE [UDP-FORMING] 106 KDA SUBUNIT-RELATED; 1.
DR PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR Pfam; PF02358; Trehalose_PPase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001744};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..904
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002844979"
FT REGION 55..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 101965 MW; 78F0AB50DE87B637 CRC64;
MGRLLLANLF LPSSVGISYD SVGSSELASR FLPSEQAAKW LTDGPLNETL LVSDSEDSVA
EMSPCTITRN NSEDKHNSDS TDTYLSDGAN DPASISKIFN HKHLSSIREQ VNLTEPVSRH
HSPPPVSVLA PQYETPQTAA RTRRRSSVYS QRRPSIDLAA WTEVQFKIRP SSSGNVCVVN
AINAAKRENP DFDEHIYFGT CGVPTDALPQ ALRERIDKVY QDEHNSKVVY VSDTDFVGHY
NHYCKHILWP TFHYQIPDNP KSKAYEDHSW HNYVSVNQAF ADSLVENYKD EDCIWVNDYH
LLLVPQMVRE KIPEAKIGLF VHIPFPSSEV FRCLPTRKEL LTGMLGANVI TFQIHEFAHH
FMQSCSRLMD LDVSGNVITI DNRIIIINSL PISVDPVALN RHLSSATVNH WTHVLMKRFK
GKRLIVSRDK LDPIKGVRQK LLSFEKFLAK YPEFRENTIF VQVSPSSVDD GEYLPAISDI
CTRINSAYSN IASQHVPVML LQLELSYSQY LALLKVADAM IVNSLREGMN LTSLEYIFAQ
QERHRPLILS EFVGSASLLG DFAIIINPWD YQQTADAFHK ALTLSDEECD KRYEKLLRVS
NAFEAGKWAQ AFLNSIKESW KLQIKYLLRR TPRFSASSLR SSYQRAKKRF IFLNYEGTLA
SWGNQKHIVM SSLQRANDLL VELTSDPKNC VYVSSTLSPQ ELDQLFHRVP NLGIVSENGC
YTHLPDPESS GKLKWTCNVP NCDLSWQKTV FDIFSYYAER TPGTYVSRKN ISIIFHFGSA
EDADTAAWAV KECCASVNGF KKLNCHVFVS TEAVICTTLD VSCREAAERA YKTSGESEFD
FVFAASDDPV DDAIFEWVRE LGHQGAGAPF TQTVSVGERA FSNADYTSAG VFGFLNDFQK
AVSK
//
