ID A0A0V1NFX2_9BILA Unreviewed; 915 AA.
AC A0A0V1NFX2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=5'-AMP-activated protein kinase subunit gamma-2 {ECO:0000313|EMBL:KRZ82723.1};
DE Flags: Fragment;
GN Name=Prkag1 {ECO:0000313|EMBL:KRZ82723.1};
GN ORFNames=T08_8876 {ECO:0000313|EMBL:KRZ82723.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ82723.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ82723.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ82723.1};
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 -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1
CC or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic
CC subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2.
CC {ECO:0000256|ARBA:ARBA00025878}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma
CC subunit family. {ECO:0000256|ARBA:ARBA00006750}.
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:KRZ82723.1}.
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DR EMBL; JYDM01000255; KRZ82723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1NFX2; -.
DR STRING; 92180.A0A0V1NFX2; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR023340; UMA.
DR PANTHER; PTHR13780:SF157; AMP-ACTIVATED PROTEIN KINASE GAMMA SUBUNIT; 1.
DR PANTHER; PTHR13780; AMP-ACTIVATED PROTEIN KINASE, GAMMA REGULATORY SUBUNIT; 1.
DR Pfam; PF00571; CBS; 3.
DR SMART; SM00116; CBS; 4.
DR SUPFAM; SSF54631; CBS-domain pair; 2.
DR PROSITE; PS51371; CBS; 3.
DR PROSITE; PS51497; UMA; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Kinase {ECO:0000313|EMBL:KRZ82723.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Transferase {ECO:0000313|EMBL:KRZ82723.1}.
FT DOMAIN 365..425
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 443..508
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 520..576
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 672..718
FT /note="UMA"
FT /evidence="ECO:0000259|PROSITE:PS51497"
FT REGION 39..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ82723.1"
SQ SEQUENCE 915 AA; 103346 MW; 450949D1214A0B96 CRC64;
LIDEHVHHVF LIISYFLQST AMNNFVKLKS DSALLNKMNS NGDNNKHNHS NLMEKIKPKK
RTFSGQNDEK LAEADGSEQT LKSSSPRHSS CKNPDKSPEE TSQRSNHFLW RFRSKDATPE
KEDLNKAGTN ANALRNTSPV DATENSHMGS NQVETLRSPS SNFGGFFHRF RQRTRSESTP
TEDHSIASVV DASTNLMHKM SIVDEDSVME PSMKSQHSAV QEAEGGGGDI LPQLRRRSRS
EASASQYLVL RKMSRPNVTE VVGRLNTDER PLTKILSMFS CFDLMPKQGL IVSLDTNLTI
HQTLVAMLGS GALSALIWDS DRHSNVGVMT LTNLLGVMLN NNDDYRCWLD RSLKSWMSDP
VKSAYCPNLD AMVTLHSNAK LIEAITLLNS SRLHRIPITD THSGNFMYML SIWSILKFLH
QYLSTLPLPQ DMYKPLDHFK FGTWENVHRA KGEDTVSDVL HVLLNNRISC LPVVQVNEAE
EETVLNIITK VDIVNYLVKF GWKNLRELTV NDIVNCRSST VEGMVTCHRS VPLLLVIDLF
VRQSAHRLII VDSMKHLVGV ISIADLLFSL IYSLLFSFLF HLPPFLSLPV FQVTCLHAAF
TVREKSEKRL KKNKTTTTSS NELMMDDMVK LNMRTENLYF DRHQLKPSCM RSKFPNSAFA
LGRCLTFPLN YLNDIPFKLN DRFAPIPSLP LGDCEPEVKL KTELLERDVN FELEKRILCS
ELAAEGTGYV CPALLQQQNG PGCSDSAFSS EMTRCRSLPD FKGLHVPFPS YSKVLEPTRS
NDLKSSVVER SPECQLDVDA IEEFEPVEST PFDAIQLNTI DDLEELRLVL ECAKQNEKQE
NILARSSHHN VMHGNAQTIF RYSPIVRPWF GQNENSSNDL SYMNINAPAG FNPLTSSFSY
LEEADRMNES NGKNA
//
