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Database: UniProt
Entry: A0A3A2ZIY1_9EURO
LinkDB: A0A3A2ZIY1_9EURO
Original site: A0A3A2ZIY1_9EURO 
ID   A0A3A2ZIY1_9EURO        Unreviewed;       450 AA.
AC   A0A3A2ZIY1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Association with the SNF1 complex (ASC) domain-containing protein {ECO:0000259|SMART:SM01010};
GN   ORFNames=PHISCL_05401 {ECO:0000313|EMBL:RJE22263.1};
OS   Aspergillus sclerotialis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Polypaecilum.
OX   NCBI_TaxID=2070753 {ECO:0000313|EMBL:RJE22263.1, ECO:0000313|Proteomes:UP000266188};
RN   [1] {ECO:0000313|Proteomes:UP000266188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 366.77 {ECO:0000313|Proteomes:UP000266188};
RA   Tafer H., Lopandic K.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC       family. {ECO:0000256|ARBA:ARBA00010926}.
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:RJE22263.1}.
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DR   EMBL; MVGC01000177; RJE22263.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A2ZIY1; -.
DR   STRING; 2070753.A0A3A2ZIY1; -.
DR   Proteomes; UP000266188; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   CDD; cd02859; E_set_AMPKbeta_like_N; 1.
DR   Gene3D; 6.20.250.60; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR032640; AMPK1_CBM.
DR   InterPro; IPR006828; ASC_dom.
DR   InterPro; IPR037256; ASC_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR10343; 5'-AMP-ACTIVATED PROTEIN KINASE , BETA SUBUNIT; 1.
DR   PANTHER; PTHR10343:SF84; ALICORN, ISOFORM A; 1.
DR   Pfam; PF16561; AMPK1_CBM; 1.
DR   Pfam; PF04739; AMPKBI; 1.
DR   SMART; SM01010; AMPKBI; 1.
DR   SUPFAM; SSF160219; AMPKBI-like; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000266188}.
FT   DOMAIN          351..449
FT                   /note="Association with the SNF1 complex (ASC)"
FT                   /evidence="ECO:0000259|SMART:SM01010"
FT   REGION          1..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   450 AA;  48382 MW;  8F5F3C7D12AD761C CRC64;
     MGNNPSKSLS GDAPSTSGPS NINASLNEKR VARRPSLNAL SGTAKATAAD PSASKETATG
     YSAAQNPASV QQHIQSRNIA DSPTRNLDRS SRRDVRKTDS QFNDIPDPSN PVQVPASRAA
     ARHDPFPPVT PSAPPSSAYY NASTHLQRPP RMPLPIGDAT ATPGSPIIGP PDGHTDSLPQ
     ERLLDEQGDM SNIGNATVDE DEFVDELQPY TVSGVGKAVP TVIQWTGPGH KVYVTGTFVN
     WEKKFRLHRS ENDKGVMATT LNLRPGTHHM KFIVDGEMRA SDNLPTAVDF TNHLVNYIEI
     SADDANRTRR VSDKDAKTSV PGVYPPQVIP DLYGPDQMGA AVDEAEKGEP EEIPIGDFRS
     IIPQFLSDLD KEEEGEAYQK AASLIGDTPA PPSLPLFLGK SILNGTTPMK DDSSVLNYPN
     HTVLNHLATS SIKNGVLATS VTTRYKRKVS
//
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