ID   A0A0V0Y9N7_TRIPS        Unreviewed;      1261 AA.
AC   A0A0V0Y9N7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=AMP-activated protein kinase glycogen-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=T4E_4622 {ECO:0000313|EMBL:KRX96690.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX96690.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX96690.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX96690.1};
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:KRX96690.1}.
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DR   EMBL; JYDU01000040; KRX96690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0Y9N7; -.
DR   Proteomes; UP000054815; 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   InterPro; IPR041105; TDP43_N.
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; PF18694; TDP43_N; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815}.
FT   DOMAIN          57..108
FT                   /note="TAR DNA-binding protein 43 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18694"
FT   DOMAIN          1191..1261
FT                   /note="AMP-activated protein kinase glycogen-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16561"
FT   REGION          810..833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          223..257
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          486..548
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          573..672
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          848..875
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          904..1051
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        811..825
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX96690.1"
SQ   SEQUENCE   1261 AA;  145595 MW;  B2ED6DFBD02F7BD8 CRC64;
     LHNFQLSNSN TYDSSPCLFS APDTEVVGSK KPSFPKRQFG NFPKFIQMET PTSENIVQVS
     TGVLECPLEK DGTLSLATLR SLLPGARGLW YKPSEFKPIQ LMENQRNLCP RVKDGVIEYI
     TSVFCPEMHR EFQRFMTTFK RSASNCSEKD FHDSGITESA SDVIANLHSF NNFSLFFVIC
     FFLFPQYCSS SFHDLSEADL SSDSIPYDVY FRQKRCSDPA IECAEKSVRL VKQSQRLLEL
     ENEIAELKKL INESNSTSIR TKQGERKASI ECCDSCKSIC KNYQMLLDQK AQDIELLLEG
     YTRNRRLIGE LSKVGTGNQD ELKEQKEKIL QQMKDICKQC TEKFEYFDTD KTTNDKDDQI
     EVTMIPGSNA EQLGESQKKM RLESDFKSSE RALFASEPVK WSGNIVNTWV MTENAERLKS
     TDQEDVAKLR YRRSLSVERD QDPSRTDINT TTNATTATTA TAAIERKMVP DQFSAMITDT
     SAEDECNKWK AMCENLQDHL DKQNKQIAEF TRLMDWIEDE SEMLQEGLRK LEKKMASSAE
     TVGQLENQKA GDADYNKSID ELKSDSKPTA EACNKLQDEL NELKSKCKNL SQKLHNGNLN
     LEESAPVVDV DEFKKKYKEK KQRCIELESA LEDKEAQLDR IKRENDKLQM DIQFIQQQFN
     EMNESLANVE EESKMKLPDS TEVHEEEQFS LEQQPYEECF GENLDNPYKA RDAEYQLKRI
     GESETASSRK KWSKDKLNII ADLQNQLNDQ RQQLRNLEEE RSEISEQLNQ AKARCEQLES
     ERENVSQIEQ LQKCIQNLKM ENEKLKLQTI EQSQRKSSNA GAEIPSTTAK KEAVDELSSE
     LYQTYQRKYT LEMELETAKQ QAAKASAELA SQQQARRVEQ DELLAWQKKV EDLKTAFAKV
     DKDRLDLQQM YDEKNSALAT VENELESVKR QLSALQGSSA TLGEGENQNA AEEERHRLNE
     EIITLQAQLS EASDKANWYA GEVGYFKQKL EEAYNEISRL EDHLKNLQIA SAGQNLSSAD
     ANEVANLKEQ LNRLNVELGT VRKELQKETD RANWYHGEVE YFRSMQKNIE EKLCNLIKKI
     TNNSDANVNA EAALQQLSNV YECIQVDIST LMDKAKWYEG EKEYFKKEME KFSEKCIELQ
     DQNICNASQF EDAFIVNKEP YVDRQKWILS MLKLKKENMR RVQFEITAPH SHQVYLVGSF
     YNWECALLMH QRPNEKWELG LYVPVGRHEF RFIQNGQWCT DEHYATCPND YGTLNNWLIV
     E
//