ID G3XPQ0_ASPNA Unreviewed; 907 AA.
AC G3XPQ0;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 13-SEP-2023, entry version 41.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHA27249.1};
DE Flags: Fragment;
GN ORFNames=ASPNIDRAFT_119606 {ECO:0000313|EMBL:EHA27249.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA27249.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA27249.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHA27249.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACJE01000003; EHA27249.1; -; Genomic_DNA.
DR AlphaFoldDB; G3XPQ0; -.
DR STRING; 380704.G3XPQ0; -.
DR HOGENOM; CLU_002351_2_2_1; -.
DR Proteomes; UP000009038; 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 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;
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHA27249.1"
FT NON_TER 907
FT /evidence="ECO:0000313|EMBL:EHA27249.1"
SQ SEQUENCE 907 AA; 101949 MW; 9AE4376CE4A787B5 CRC64;
FLPYTVNFHQ NGPQIRPAEG TSPQPTNPAE NSTPNPKATL SLFERNNGAP QVGLTPGATT
EHECIFSTDI SKAEQEHTGF PFPKTDGEVT LLTESEAHSP AWGSTLALNQ PRPRAAFPAS
PSILKHQEIG PSGTEAPKEK PRSVPKTPTS HIRDSWADHS RKSSFSYADW TIETAEQGNG
GLRNAVRSAT DAGQLEDKVW VGTLGMPTDA LPEHTKEAIA EKLEDEYGSV TVYVSDGDFD
GHYTHFCKTI LWPVFHYQIP DNPKSKAYED HSWVYYVKTN QAFAERIAKN WKRGDSIWVQ
DYHLLLVPAM LRKLLPDAQI GFFLHIAFPS SEVFRCLAPR KELLEGILGA NLVGFQTDEY
CRHFLQTCSR ILCVEATNDG LQLEDRFVNV GKFSIGIDPT SWDQRRRAAD VERWIKTISE
RYEGKRLIVS RDKIDQVRGI RQKLLSYELF LNTYPEWRDQ VVLIQVATST TEQPELEATI
SDIAMRINST HSTLAHQPLV FLKQDLAFPQ YLALISVADA LIITSLREGM NLTSHEFVYC
QDGKWGNKKY GSLILSEFTG SASVFGDHAL LVNPWDYRQC AEAIHTALSR DEQERQEVWT
KLHQAVLQNS THNWVKSFSE TLSRVWNEQS SREIMAVPRL QINKLEEMYH RSSRRLIIVD
YEGTLASWGS PKSIIVTTPQ RAITTLAELT EDPRNVVYVM SARMPEEMER LFRLVTGLGL
IAENGCFVRE PNSETWLKLT DKVQTDAWKA AVSHILEYYQ ERAEGSWVEQ RHCSLMFHYE
SAEDQVAASR LASECAGHIN DACLSQGVHA VPVERALVVE PAGINKASAA EVAWRSCLKQ
SQRDESVPRP EFLLAIGDGR DDESVFRWAN KLDSARAVNY AMTVTLGSRS TEAKATLTQG
VTGKLLS
//
