ID A0A0D1E2V9_USTMA Unreviewed; 664 AA.
AC A0A0D1E2V9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Glycosyl hydrolase family 30 TIM-barrel domain-containing protein {ECO:0000259|Pfam:PF02055};
GN ORFNames=UMAG_05223 {ECO:0000313|EMBL:KIS70151.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS70151.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS70151.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family.
CC {ECO:0000256|ARBA:ARBA00005382, ECO:0000256|RuleBase:RU361188}.
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DR EMBL; CM003143; KIS70151.1; -; Genomic_DNA.
DR RefSeq; XP_011388260.1; XM_011389958.1.
DR AlphaFoldDB; A0A0D1E2V9; -.
DR EnsemblFungi; KIS70151; KIS70151; UMAG_05223.
DR GeneID; 23565170; -.
DR KEGG; uma:UMAG_05223; -.
DR VEuPathDB; FungiDB:UMAG_05223; -.
DR eggNOG; KOG2566; Eukaryota.
DR InParanoid; A0A0D1E2V9; -.
DR OrthoDB; 5487508at2759; -.
DR Proteomes; UP000000561; Chromosome 4.
DR GO; GO:0004348; F:glucosylceramidase activity; IBA:GO_Central.
DR GO; GO:0006680; P:glucosylceramide catabolic process; IBA:GO_Central.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001139; Glyco_hydro_30.
DR InterPro; IPR033453; Glyco_hydro_30_TIM-barrel.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11069; GLUCOSYLCERAMIDASE; 1.
DR PANTHER; PTHR11069:SF23; LYSOSOMAL ACID GLUCOSYLCERAMIDASE; 1.
DR Pfam; PF02055; Glyco_hydro_30; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361188};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361188};
KW Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..664
FT /note="Glycosyl hydrolase family 30 TIM-barrel domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002240639"
FT DOMAIN 100..358
FT /note="Glycosyl hydrolase family 30 TIM-barrel"
FT /evidence="ECO:0000259|Pfam:PF02055"
FT REGION 433..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 71884 MW; 44316CDC7591F3A2 CRC64;
MRSITSWLSI AAACTACLAD TVLSAATTTS QEVVIDKMWS TTWNYSKVQE LSNPGIKFSP
GPALAASVNV TAEQSSDSQS HDQIGIQVQD NQVHQLVDAL GGGITDSVAI TLQEFKSKHP
QDYDDLLHLL FAQDQAWFTR GGLGLNSVRV PLGACDFGVS PYTYDDTEDG SADPKLELFT
IKKAPKLWLT LKDILAINPT LKIFVAAWSA PGWMKENADA AQPLFGGNLK PGMEAVYAQY
LTKSIVEIKK QEGIEIYAMS PANEPQVPAV QYPSMHLSAN QSIQLGKLLR SGLDAAGFNR
VKLLAWDFNW DNTDYPLEVL NADPTPWAGI AWHGYAGEPI NQKVITDAFP NLDTYFTEKT
VVTQWFNEPY KNMKNAAREL IIGSIRYSSR SLILWNLVLR KDEDGFTTPH LPKVCENCNA
AILLLPESTD AHFDRGDPNH VKTVEEANGG AAAKKDTVAP AAGSRRKRSL GHRAETDPDS
RQLDAAGSDE TGSAQRSTAE SVAPSKVIDA KKTGSPSVYE SALFKRTSDL SVLSHLSTAI
RPEGASKSYS KRIGVTSTDE QTELGGRLLA QAFRQDGVKS GVTRFSIVLL NQNDHYETGV
FEPVTAVIAF RGMTANVTTV PGLYTLSWEA STIPPSDAST EADAQTVPAS QNADTDKSDA
PAPA
//
