ID   A0A0V1NIJ5_9BILA        Unreviewed;       306 AA.
AC   A0A0V1NIJ5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=AMP-activated protein kinase glycogen-binding domain-containing protein {ECO:0000259|Pfam:PF16561};
DE   Flags: Fragment;
GN   ORFNames=T08_12438 {ECO:0000313|EMBL:KRZ83821.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ83821.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ83821.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ83821.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Non-catalytic subunit of AMP-activated protein kinase (AMPK),
CC       an energy sensor protein kinase that plays a key role in regulating
CC       cellular energy metabolism. In response to reduction of intracellular
CC       ATP levels, AMPK activates energy-producing pathways and inhibits
CC       energy-consuming processes: inhibits protein, carbohydrate and lipid
CC       biosynthesis, as well as cell growth and proliferation. AMPK acts via
CC       direct phosphorylation of metabolic enzymes, and by longer-term effects
CC       via phosphorylation of transcription regulators. Also acts as a
CC       regulator of cellular polarity by remodeling the actin cytoskeleton;
CC       probably by indirectly activating myosin. Beta non-catalytic subunit
CC       acts as a scaffold on which the AMPK complex assembles, via its C-
CC       terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits
CC       (PRKAG1, PRKAG2 or PRKAG3). {ECO:0000256|ARBA:ARBA00025180}.
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:KRZ83821.1}.
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DR   EMBL; JYDM01000196; KRZ83821.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1NIJ5; -.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
DR   CDD; cd02859; E_set_AMPKbeta_like_N; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR032640; AMPK1_CBM.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF16561; AMPK1_CBM; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924}.
FT   DOMAIN          235..306
FT                   /note="AMP-activated protein kinase glycogen-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16561"
FT   REGION          66..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ83821.1"
SQ   SEQUENCE   306 AA;  36689 MW;  CCDC169720E120BD CRC64;
     LEAKVSMLEM ENYELKAKLR ENQHFIRRVT NSQMKQDVQK KYEELSSELY KAYLELQKVR
     SELAHSKSMQ NNDDGHQAEK RQTENMDNMV REIDALKASL DRETSRADWY HGEVEYFRRR
     VQELENEIQR RSSEHAQNDS VFRECERLQA QLHDMTNKAK WYEGEKEYFK REMENYSSRC
     AELDKYNCTI KNIINEALIV RKDPYYDRQK WNLAQVSSNE NKQFRHVIFK YACATAHQVY
     LTASFYNWEC AILMNKQDDG IWSIGIDVPL GRHEFRFLQL QNCDCSSQHP TCYNDYGSMN
     NWIMVE
//