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
//