ID D4AIJ1_ARTBC Unreviewed; 412 AA.
AC D4AIJ1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Glycosyl transferase, putative {ECO:0000313|EMBL:EFE36564.1};
GN ORFNames=ARB_04086 {ECO:0000313|EMBL:EFE36564.1};
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:EFE36564.1, 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: Belongs to the glycosyltransferase 32 family.
CC {ECO:0000256|ARBA:ARBA00009003}.
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:EFE36564.1}.
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DR EMBL; ABSU01000001; EFE36564.1; -; Genomic_DNA.
DR RefSeq; XP_003017209.1; XM_003017163.1.
DR AlphaFoldDB; D4AIJ1; -.
DR GeneID; 9522293; -.
DR KEGG; abe:ARB_04086; -.
DR eggNOG; ENOG502QS3D; Eukaryota.
DR HOGENOM; CLU_036369_3_0_1; -.
DR OMA; NRHSWSF; -.
DR OrthoDB; 1658384at2759; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IEA:UniProt.
DR GO; GO:0006673; P:inositol phosphoceramide metabolic process; IEA:UniProt.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
DR Gene3D; 3.90.550.20; -; 1.
DR InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR32385; MANNOSYL PHOSPHORYLINOSITOL CERAMIDE SYNTHASE; 1.
DR PANTHER; PTHR32385:SF15; MANNOSYL PHOSPHORYLINOSITOL CERAMIDE SYNTHASE CSH1-RELATED; 1.
DR Pfam; PF04488; Gly_transf_sug; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008866};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFE36564.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 390..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 47735 MW; 758CE90354B77057 CRC64;
MRRGLLIFLL INTVIILFLV RSVFTLLTLL VEDATDDAIQ NVELPGVNSS LIDLRPQLIP
KIIHQTYKNE SIPEIWVGPR NGCIEMHPDY EYILWTDKKS RDFIAEHYPW FLTTFDNYPF
PIQRADSIRY FILAHYGGTY IDLDDPPHLP LLPPIYLYTN EKKRKKKKKK KKKKATKTNN
IKKKNAIGAN AVRYMQGCNR RLDPLLSYPA WVRRTAPTGI SNDAMGSVPN HPFFLRVIKS
LQAYDRAWVL PYITVMYSTG PLFLSVIWKE YKNTDPDGVN RVRVLLQDAY NRHSWSFFTH
HPGSSWHGED AQLIFWTLVM QMGSHWMLIT FSGFLAAGIV GLALWRIYRR VLSLGSKHAR
YTPLASGTSS PRRSLSPSRR KMRILPLFFQ RSHAKKEDEE IGPDSPYELG NR
//
