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Entry: Q7SFT8_NEUCR
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ID   Q7SFT8_NEUCR            Unreviewed;       929 AA.
AC   Q7SFT8;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 2.
DT   24-JAN-2024, entry version 96.
DE   SubName: Full=Trehalose phosphate synthase {ECO:0000313|EMBL:EAA35713.2};
GN   ORFNames=NCU00793 {ECO:0000313|EMBL:EAA35713.2};
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA35713.2, ECO:0000313|Proteomes:UP000001805};
RN   [1] {ECO:0000313|EMBL:EAA35713.2, ECO:0000313|Proteomes:UP000001805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC   {ECO:0000313|Proteomes:UP000001805};
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA   FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA   Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA   Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA   Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA   Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA   Lander E.S., Nusbaum C., Birren B.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- SIMILARITY: In the C-terminal section; belongs to the trehalose
CC       phosphatase family. {ECO:0000256|ARBA:ARBA00006330}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 20 family. {ECO:0000256|ARBA:ARBA00005409}.
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DR   EMBL; CM002236; EAA35713.2; -; Genomic_DNA.
DR   RefSeq; XP_964949.2; XM_959856.3.
DR   AlphaFoldDB; Q7SFT8; -.
DR   STRING; 367110.Q7SFT8; -.
DR   PaxDb; 5141-EFNCRP00000000557; -.
DR   EnsemblFungi; EAA35713; EAA35713; NCU00793.
DR   GeneID; 3881098; -.
DR   KEGG; ncr:NCU00793; -.
DR   VEuPathDB; FungiDB:NCU00793; -.
DR   HOGENOM; CLU_002351_2_2_1; -.
DR   InParanoid; Q7SFT8; -.
DR   OrthoDB; 1023at2759; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR003337; Trehalose_PPase.
DR   NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR   NCBIfam; TIGR00685; T6PP; 1.
DR   PANTHER; PTHR10788:SF15; TREHALOSE SYNTHASE COMPLEX REGULATORY SUBUNIT TPS3-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:UP000001805}.
FT   REGION          18..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   929 AA;  105164 MW;  5254DE5CE655113D CRC64;
     MTVFIASLFL PKTVHFNLPG ARPRGASASQ KPASKAKKLA PNTPPSLFQP APSHITPPHT
     PTEDRKHHDP WANEDGLKVQ IPQMPFSPDG SYRAPIDRSS PTWGGRPDQP MSRANSPPPP
     SLINSSRALN QKAREMGRQG ITQPRSLVRS ESHDRVFAHA DWKIVSADQG NGGLRNAAEA
     AARDGKLGEY TWIGTLGMPT DALRGTQQLQ DIDDRLATEH DMLAVFCSDK DFDGHYSHFC
     KQILWPVFHY QIPDNPKSKA YEDHSWKYYV NVNQAFADKI VKNWKKGDTV WIHDYHLLLV
     PGMIRKKIPE AKIGFFLHVA FPSSEVFRCL AVRKELLEGM LGANLIGFQI REYARHFLQT
     CSRILSVEAT PDGLQLEDRF VDVINLPIGI DPVSLSRHRG ESEVKRWLDI MRERYAGKKL
     IVARDKLDHV RGVRQKLLSY EMFLNMNPEW RDKVVLIQVA LSTSEKSELD ATVSDIVTRV
     NSSWANLAYQ PVVYLKQDID YAQYLALLSI ADALMITSQR EGMNLTSHEY LFCQDGKFSE
     KKHGSLILSE FTGTSSLFNG NELSVNPWDY RACADAIKKA LEMEGEEKER RWKNLYEAVN
     VHTGSHWFSE FMLRLDKVYE EQHSRDQTAV PRLSMTTLLQ QYERTNRRLF IIDFEGTLVS
     WGPVNQIIPV SPQRTLDVLN DLLLDERNTI YVMSGRRPEE LDRIFRRVTN LGLIAESGCY
     LKDCGSNTWT EMADANKIRS WKSSLRDIMT YYLERTPGAA IEERRCSLVF HYKSADDYET
     AATQASDLAS HINDACEDQR VHAIPMDGCV LVEPIDWTKS TAAQTIFDDL QQRMGPDEKH
     KSPVDFLMVV GDGRDDEKVF KWANQLGTDG TVQEVVTVSL GNRNTEAKAT VTQGVSGVLA
     ALQKLSQVVV PAEHQRRRSS ITIPSLVNM
//
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