ID A5DS93_LODEL Unreviewed; 506 AA.
AC A5DS93;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 03-MAY-2023, entry version 70.
DE RecName: Full=Glucosidase 2 subunit beta {ECO:0000256|ARBA:ARBA00022387};
GN ORFNames=LELG_00229 {ECO:0000313|EMBL:EDK42051.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK42051.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK42051.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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DR EMBL; CH981524; EDK42051.1; -; Genomic_DNA.
DR RefSeq; XP_001527709.1; XM_001527659.1.
DR AlphaFoldDB; A5DS93; -.
DR STRING; 379508.A5DS93; -.
DR GeneID; 5235924; -.
DR KEGG; lel:LELG_00229; -.
DR VEuPathDB; FungiDB:LELG_00229; -.
DR eggNOG; KOG2397; Eukaryota.
DR HOGENOM; CLU_016834_2_1_1; -.
DR InParanoid; A5DS93; -.
DR OMA; KHESASH; -.
DR OrthoDB; 103990at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR Gene3D; 1.10.287.1490; -; 1.
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:UP000001996};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..506
FT /note="Glucosidase 2 subunit beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002679792"
FT DOMAIN 383..489
FT /note="MRH"
FT /evidence="ECO:0000259|PROSITE:PS51914"
FT COILED 158..247
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 357..384
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 506 AA; 58288 MW; 2954EF1E33762CF8 CRC64;
MQLGKLAIFL PLWLLCLSQA HVIGVSPEDQ HLYSAKIDED GNQYWTCLND SSIKLQLSQI
NDDICDCPDG SDEPGTNACP DSAIKFYCAN QGHFPAYIEQ FKLNDGVCDY DICCDGSDEY
QLGTCENKCD EIHRQFETYK AEQLQILNKA LKKKQHVVDL SQRNRKSLIN NLEHLERQVP
EKKMKLNKLK IQMEDVELQE DTPDLYDILD EHFANLANRI EAYKRDILKQ DEQLQKLEKI
LEELSKGYNP NYNDHAVKES IHKFQEYISN KEDGVQKDFH DITEFVKKIV ENAKEHSINI
ELTGNGNINN DKSKSKSKSK HYDGVPSLKN MIHYYFNLFA QNFLIKTPET YVSKLSSNQL
APEIDKLEEE LEKIEKTITV IKKDLSSDYG PDDILRAYEK LPISNNLGGY YYRVDFLNSI
YQNDVLIGVF KEYKEGKLIF ANGARCWNGP KRSATVEFIC GEGPAIVSVA EPEKCHYNFV
IRGEAWCHPV SEQELLQSFE IDYNLL
//
