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Database: UniProt
Entry: A0A5N5X3I6_9EURO
LinkDB: A0A5N5X3I6_9EURO
Original site: A0A5N5X3I6_9EURO 
ID   A0A5N5X3I6_9EURO        Unreviewed;       569 AA.
AC   A0A5N5X3I6;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   22-FEB-2023, entry version 9.
DE   RecName: Full=Glucosidase 2 subunit beta {ECO:0000256|ARBA:ARBA00022387};
GN   ORFNames=BDV29DRAFT_109732 {ECO:0000313|EMBL:KAB8075321.1};
OS   Aspergillus leporis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=41062 {ECO:0000313|EMBL:KAB8075321.1, ECO:0000313|Proteomes:UP000326565};
RN   [1] {ECO:0000313|EMBL:KAB8075321.1, ECO:0000313|Proteomes:UP000326565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 151.66 {ECO:0000313|EMBL:KAB8075321.1,
RC   ECO:0000313|Proteomes:UP000326565};
RG   DOE Joint Genome Institute;
RA   Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA   Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA   Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA   Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA   Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA   Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA   Baker S.E., Andersen M.R.;
RT   "Friends and foes A comparative genomics study of 23 Aspergillus species
RT   from section Flavi.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; ML732196; KAB8075321.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N5X3I6; -.
DR   Proteomes; UP000326565; Unassembled WGS sequence.
DR   Gene3D; 2.70.130.10; Mannose-6-phosphate receptor binding domain; 1.
DR   InterPro; IPR039794; Gtb1-like.
DR   InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR   InterPro; IPR044865; MRH_dom.
DR   InterPro; IPR036607; PRKCSH.
DR   InterPro; IPR028146; PRKCSH_N.
DR   PANTHER; PTHR12630:SF1; GLUCOSIDASE 2 SUBUNIT BETA; 1.
DR   PANTHER; PTHR12630; N-LINKED OLIGOSACCHARIDE PROCESSING; 1.
DR   Pfam; PF12999; PRKCSH-like; 1.
DR   Pfam; PF13015; PRKCSH_1; 1.
DR   SUPFAM; SSF50911; Mannose 6-phosphate receptor domain; 1.
DR   PROSITE; PS51914; MRH; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Reference proteome {ECO:0000313|Proteomes:UP000326565};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..569
FT                   /note="Glucosidase 2 subunit beta"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025041794"
FT   DOMAIN          443..555
FT                   /note="MRH"
FT                   /evidence="ECO:0000259|PROSITE:PS51914"
FT   COILED          186..286
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          400..431
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   569 AA;  63134 MW;  102DE5C8FC405490 CRC64;
     MILPQGSLFF VSLAACSTAV AAASKDGSAR PRGVGPEFAK FYKDTETFSC ISHPAIKISF
     SAVNDDYCDC PDGSDEPGTS ACAHLCRNSP LTVADRPGNN DIDLTLSLPG FYCKNKGHKP
     AYVPFQRVND GICDYDLCCD GSDEWARVGG KKCEDKCKEI GKEWRKNEEK KQKSMTAALK
     KKKELLADAG RQEQEVVDNI KRLEIEIQGQ DIKLKALEAD LEEVEKQERS KVVKGKKAGR
     VNVLSQLAKG RVEELRTALT EVRKERDETR SRVKELEEIL SKFKVEYNPN FNDEGVKRAV
     RSWEEYAAKG TSEGLENAAR DRDLDEIAKP DDDKSGINWE QWENEDDACE ADTVYQLAAY
     LPPSLVSFIE DKVLAIRGFL EKNGVLPTKD EGSSSESKVV TEARDAVNEA RKSIEDLNKQ
     VKDHKADLER DYGVGSIFRA LKGVCIQKDA GEYTYEHCFL DQAKQIPKKG GSTARMGNFV
     RIGSITVDEL NDSGEIVPEE RVALEYANGQ TCWNGPARST TVVLQCGEED EILKIAEDEK
     CVYSMLVNTP AVCPGGEEEI RAPAHKDEL
//
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