ID   D4AXJ6_ARTBC            Unreviewed;      1005 AA.
AC   D4AXJ6;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   03-MAY-2023, entry version 54.
DE   SubName: Full=Alpha,alpha-trehalose phosphate synthase subunit, putative {ECO:0000313|EMBL:EFE32024.1};
GN   ORFNames=ARB_00915 {ECO:0000313|EMBL:EFE32024.1};
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE32024.1, ECO:0000313|Proteomes:UP000008866};
RN   [1] {ECO:0000313|Proteomes:UP000008866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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:EFE32024.1}.
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DR   EMBL; ABSU01000017; EFE32024.1; -; Genomic_DNA.
DR   RefSeq; XP_003012664.1; XM_003012618.1.
DR   AlphaFoldDB; D4AXJ6; -.
DR   STRING; 663331.D4AXJ6; -.
DR   GeneID; 9522742; -.
DR   KEGG; abe:ARB_00915; -.
DR   eggNOG; KOG1050; Eukaryota.
DR   HOGENOM; CLU_002351_2_2_1; -.
DR   OMA; TSWDKRR; -.
DR   OrthoDB; 1023at2759; -.
DR   Proteomes; UP000008866; 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; IPR023214; HAD_sf.
DR   InterPro; IPR003337; Trehalose_PPase.
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:UP000008866};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..1005
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003053743"
FT   REGION          33..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1005 AA;  112027 MW;  5EF7321492C1A4DB CRC64;
     MTIFIVSLAL FADRASFLPH TIDFALPEGY QRKASHHHRR KSSGQRATLF GRLPGSQTAT
     PTSASASTSA STSTATTATT SAAASNHASG STVAGRRPSS LRDQGRIFSC PDYSSSGIEV
     TSQQPRLLAP SDPHSPRWGS PGAFNQPKAQ ALAPPSSSIL NHALGQESAS ELSRTEPTVL
     PPSPVRPSIE PGSQPNQESV FESAEWTVQP SEQGNGGLLN AIRSAVDWPY MKDKLWVGTL
     GMPTDALHEK QKEAIAEKLA ADYEALTIFV SDNDFDSHYL HFCKMILWPV FHYQIPDNPK
     SKAYEDHSWI FYRRVNYNFA KELIKNWKRG DVIWVHDYHL LLVPAMVRKE IPDAQIGIFL
     HVAFPSSEVF RCLSVRVELL KGMLGANLIG FQTQEYCHHF LQTCSRLLNV EATKDGVQLE
     DRFVNVGTFP IGIDPVSLDI RRQCGEVKSW INILQEKFKG KRLIVARDKL DNVRGVRQKL
     LAYELFLNKY PHWRDSVVLI QVASTTTEQP ELEASVSDIA TRINSVHSNL AHQPLIFHKQ
     DLLFDQYLAL ISVADVFMVT SLREGMNLTS HEFIHCQDGL LSSSKHGPLI LSEFTGSASI
     FNYHPLLVNP WNYQECADAI NTALEMSPET RLAQWTRLNT TAKDHVTTRW VNNFTEALDR
     AYRQHSTRET VAVPRLSIPN LCNAYRTSSR RLLILDYEGT LVSWGQPTST VLTTPQRAID
     TLTDLLEDPL NTVYVMSSRM PEDMERLFSR VPGLGLIAEN GCFVRPPPML SPTPSPPTTG
     TFVTSNWIRL IDMTKMNDWK LSLSPMLRYF QERTEGSWIE ETHASLIFHY ERAEDSQSAE
     RHASECANNV NDSCGNHSLR AIQMDGCVVA GPVEPNKGTA ANVVFSTYTR RESRRSSSAG
     SASSAKQGMA IEWKSETEDN DEDVPDFILV IGDGRDDEPA FRWANELGEE KKVKNVMTVT
     LGFKNTEAMA TLNQGVTGKL VDISQRRDSA SLAQKLSYIP ASNGE
//