ID A0A319CTN3_9EURO Unreviewed; 462 AA.
AC A0A319CTN3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Snf1 kinase complex beta-subunit Gal83 {ECO:0000313|EMBL:PYH88544.1};
GN ORFNames=BO71DRAFT_132900 {ECO:0000313|EMBL:PYH88544.1};
OS Aspergillus ellipticus CBS 707.79.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH88544.1, ECO:0000313|Proteomes:UP000247810};
RN [1] {ECO:0000313|EMBL:PYH88544.1, ECO:0000313|Proteomes:UP000247810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH88544.1,
RC ECO:0000313|Proteomes:UP000247810};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000256|ARBA:ARBA00010926}.
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DR EMBL; KZ826083; PYH88544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319CTN3; -.
DR STRING; 1448320.A0A319CTN3; -.
DR Proteomes; UP000247810; 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:PYH88544.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000247810};
KW Transferase {ECO:0000313|EMBL:PYH88544.1}.
FT DOMAIN 350..450
FT /note="Association with the SNF1 complex (ASC)"
FT /evidence="ECO:0000259|SMART:SM01010"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 49902 MW; 068AFCC7EA5D754C CRC64;
MGNNPSKGPA PDAQLPSGIA ASTGERKVAR RPSINAPSGA AKATAADPSA TKETATGHST
SQNQPSVQQR LQSRNAADSP TRNLDRPDRR KPDAHARDIP SPDPSNPVQV PVSRAAAKRD
PVATSGHPPN AYYSASVHLQ RPPRMPLPIG DATVTPGSPI IGPEDSYMET LPTDQLLDEH
VDPSHTNAGG TTIEDEEALD ELQPYTPSSV GRAVPTTIEW TETGDKIYVT GTFVNWEKKF
RLHRSENNPG TQSTTLNLRP GTHHLKFIVD GEMRASNNLP TAVDFTNHLV NYIEISADDV
NRSRRESDRV SRGGVPDGVR PPQVLPDPVG ADDTKDGSTV EEQSDKEEPE EIPLGDFRGI
IPQFLLDLDR EEETPEYQQA VNIVGDAPTP PSLPLFLGKS ILNGTTPMKD DSSVLNYPNH
TVLNHLATSS IKNGVLATSV TTRYKRKVSA TSRVEVPPPD YV
//
