ID A0A2G7G308_9EURO Unreviewed; 460 AA.
AC A0A2G7G308;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Snf1 kinase complex beta-subunit Gal83 {ECO:0000313|EMBL:PIG87193.1};
GN ORFNames=AARAC_004185 {ECO:0000313|EMBL:PIG87193.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG87193.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG87193.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG87193.1,
RC ECO:0000313|Proteomes:UP000231358};
RA Moore G., Beltz S.B., Mack B.M.;
RT "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT Aspergillus arachidicola.";
RL Submitted (MAY-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:PIG87193.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NEXV01000186; PIG87193.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G7G308; -.
DR STRING; 656916.A0A2G7G308; -.
DR OrthoDB; 120305at2759; -.
DR Proteomes; UP000231358; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Kinase {ECO:0000313|EMBL:PIG87193.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000231358};
KW Transferase {ECO:0000313|EMBL:PIG87193.1}.
FT DOMAIN 345..455
FT /note="Association with the SNF1 complex (ASC)"
FT /evidence="ECO:0000259|SMART:SM01010"
FT REGION 1..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 49373 MW; 08005515AD922B51 CRC64;
MGNNPSKGPA GDVPSTSGHS THVGSAGDRK VTRRPSLNAP SGTAKATAAD PSASKETATG
HSVSQNQASV QQRLQSRNAP DSATRHAPDT KKADTHYKEI PSPDPSNPVQ VPASRISARH
DHYTPVAPSG PPHNAYYSAS AHLQRPPRLP LPIGDATATP GSPYMGSPPS ERLLDEQAGQ
GDPNLGDAAV EDEEVLEELE PYTSSGVGRP VPTIIEWTAP GDKVYVTGTF VNWEKKFRLH
RSESNPGVMS TRLNLRPGTH HLKFIVDGEM RAADSLPTAV DFTNHLVNYI EISADDTNRS
RSGSDKTSQS NVPPGVHPPQ VLPTRVGSEQ VGSGSAVEDQ LDEWEEIPQG DFRRIIPQFL
VDLDREDETQ ESPAYQRAVN VIGDAPTPPS LPLFLGKSIL NGTTPMKDDS SVLNYPNHTV
LNHLATSSIK NGVLATSATT RYKRKYVTTI LYKPTGDITG
//
