ID G4U8U6_NEUT9 Unreviewed; 1030 AA.
AC G4U8U6;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 13-SEP-2023, entry version 40.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGZ76825.1};
GN ORFNames=NEUTE2DRAFT_161682 {ECO:0000313|EMBL:EGZ76825.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ76825.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ76825.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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; GL890999; EGZ76825.1; -; Genomic_DNA.
DR AlphaFoldDB; G4U8U6; -.
DR STRING; 510952.G4U8U6; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_2_2_1; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
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:UP000008513}.
FT REGION 131..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1030 AA; 115790 MW; A4CFB0F129BA7D59 CRC64;
MSLCSGPQIL VKLRPLTSVL IHIPRPAEAR PSPTSSTSAE SRILDSSCLT HVHSLDALEL
GDAFTAISDE HNRRPIADIS VAVTSIKSIY HLADYTVFSS FDKALTAAHH DCVHCLAATL
SDPSTPSDGF LPKTVHFNLP GARPRGASAS QKPASKAKKL APNTPPSLFQ PAPSHITPPH
TPTEDRKHHD PWANEDGLKV QIPQMPFSPD GSYRAPIDRS SPTWGGRPDQ PMSRANSPPP
PSLSNSSRAL NQKAREMGRQ GITQPRSLVR SESHDRVFAH ADWKIVSADQ GNGGLRNAAE
AAARDGKLGE YTWIGTLGMP TDALQGTQQL QDIDDRLATE HDMLAVFCSD KDFDGHYSHF
CKQILWPVFH YQIPDNPKSK AYEDHSWKYY VNVNQAFADK IVKNWKKGDT VWIHDYHLLL
VPGMIRKKIP EAKIGFFLHV AFPSSEVFRC LAVRKELLEG MLGANLIGFQ IREYARHFLQ
TCSRILSVEA TPDGLQLEDR FVDVINLPIG IDPVSLSRHR GESEVKRWLD IMRERYAGKK
LIVARDKLDH VRGVRQKLLS YEMFLNMNPE WRDKVVLIQV ALSTSEKSEL DATVSDIVTR
VNSSWANLAY QPVVYLKQDI DYAQYLALLS IADALMITSQ REGMNLTSHE YLFCQDGKFS
EKKHGSLILS EFTGTSSLFN GNELSVNPWD YRACADAIKK ALEMEGEEKE RRWKNLYEAV
NVHTGSHWFS EFMLRLDKVY EEQHSRDQTA VPRLSMTTLL QQYERTKRRL FIIDFEGTLV
SWGPVNQIIP VSPQRTLDVL NDLLLDERNT IYVMSGRRPE ELDRIFRRVT NLGLIAESGC
YLKDCGSNTW TEMADSNKIR SWKSSLQDIM TYYLERTPGA AIEERRCSLV FHYKSADDYE
TAATQASDLA SHINDACEDQ RVHAIPMDGC VLVEPIDWTK STAAQKIFDD LQKRMGPDEK
HKSPVDFLMV VGDGRDDEKV FKWANQLATD GTVQEVVTVS LGNRNTEAKT TLTQGVSGVL
AALQKLSQVV
//