ID A0A0B7N0S1_9FUNG Unreviewed; 482 AA.
AC A0A0B7N0S1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Association with the SNF1 complex (ASC) domain-containing protein {ECO:0000259|SMART:SM01010};
GN Name=PARPA_04806.1 scaffold 15639 {ECO:0000313|EMBL:CEP11007.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP11007.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP11007.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP11007.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) 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; LN725615; CEP11007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7N0S1; -.
DR STRING; 35722.A0A0B7N0S1; -.
DR OrthoDB; 120305at2759; -.
DR Proteomes; UP000054107; 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:UP000054107}.
FT DOMAIN 361..478
FT /note="Association with the SNF1 complex (ASC)"
FT /evidence="ECO:0000259|SMART:SM01010"
FT REGION 1..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 482 AA; 52440 MW; 16DF89A3C1E99268 CRC64;
MGNTNSTQGN NLGPSYQQGK EQQTQEQIGA EQDQLLQQGE RRRSTSSTAS NKPKPDSASS
STSSSTSSIS RKPQSFEFTV TEPTTHSVSK PEPIPPSTHH WSPTEPSIQE DNATKLNIMK
EESEPEPPAN TPAKAVPVST NAKSGWVSST GAASPWYSSL SSSTSSSHHR ASISGPYYRT
RGMSVTRDSE NDEDLTNIIT STTTAATNST TTAAVVNSNA SPTNSVPAPA PAAVATETPA
STAAPSSIPS AANQGVPTII TWTLGGNNVY ITGTFNGWKH KIKLIKSTHD FSAVLELPPG
THRLKFIVDD EWKCSNDMET ATDPDGNLVN YLQVLDEDDE ENNDEFADND LSTVSSSGSL
SMDENKKYSN VIPPELLQLA SLMSNSEQKD DEKTQQQKKT MLEWEKKQPQ PPGLPPHLEK
VLLNSHTVSE EDNSVLHEPN HVTLNHLYAC SIKDNVMALA TTSRYRKKYV TTMYYRPVFP
KN
//
