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Database: UniProt
Entry: A0A6G0WP48_9STRA
LinkDB: A0A6G0WP48_9STRA
Original site: A0A6G0WP48_9STRA 
ID   A0A6G0WP48_9STRA        Unreviewed;       493 AA.
AC   A0A6G0WP48;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   13-SEP-2023, entry version 10.
DE   RecName: Full=Glucosidase 2 subunit beta {ECO:0000256|ARBA:ARBA00022387};
GN   ORFNames=Ae201684_013129 {ECO:0000313|EMBL:KAF0729151.1};
OS   Aphanomyces euteiches.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=100861 {ECO:0000313|EMBL:KAF0729151.1, ECO:0000313|Proteomes:UP000481153};
RN   [1] {ECO:0000313|EMBL:KAF0729151.1, ECO:0000313|Proteomes:UP000481153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 201684 {ECO:0000313|EMBL:KAF0729151.1,
RC   ECO:0000313|Proteomes:UP000481153};
RA   Gaulin E.;
RT   "Genomics analysis of Aphanomyces spp. identifies a new class of oomycete
RT   effector associated with host adaptation.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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:KAF0729151.1}.
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DR   EMBL; VJMJ01000167; KAF0729151.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6G0WP48; -.
DR   VEuPathDB; FungiDB:AeMF1_004288; -.
DR   Proteomes; UP000481153; Unassembled WGS sequence.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 2.70.130.10; Mannose-6-phosphate receptor binding domain; 1.
DR   InterPro; IPR039794; Gtb1-like.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
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; PS50068; LDLRA_2; 1.
DR   PROSITE; PS51914; MRH; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Reference proteome {ECO:0000313|Proteomes:UP000481153};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..493
FT                   /note="Glucosidase 2 subunit beta"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5026070584"
FT   DOMAIN          377..478
FT                   /note="MRH"
FT                   /evidence="ECO:0000259|PROSITE:PS51914"
FT   REGION          290..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..360
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  53976 MW;  DF70861284E799E1 CRC64;
     MRDLNRKMKL SILAACLAGC AASVPQLHGL KPEFQAQVAA AASLNCDSGT KNIPIASVND
     DYCDCRDGSD EPGTAACSHT QVQFYCENKG FFPSEIPTSR VNDGICDCCD GSDEYNSGAS
     CPQTCATLRA DHDKEKAAQD AVLEAGREAR LKIVTTSKLQ KEEQYRRRTD LEVEKARLDK
     AVEDARALKV SEEAIEVQEQ KAAAVATRKK VAVHLGLHDL SSEQLIELVL DLSVKVPLRS
     DVLSAIRGVQ TSDASVIDQQ EQAYELTLAA HKKEVERVNQ VNDDLKKAKE DARKLKEDAG
     ETFEEENDDK YKPLEVPTPP ERPIDQLFGK LTSDQSVPRP EAKAAREALD SAESKARETQ
     SELDAIEKKL QLQYGPDDVL FSLRDTCVEV KSGEYTYKMC WFGQAHQDHT SLGKMEPIGP
     SPRLNRIKFS GGAKCWNGPE RSLTVTLTCG ETQELGGIEE PSTCVYVATL QTPIACSPEA
     TTAPTSTPSH DEL
//
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