ID A0A067RX71_ZOONE Unreviewed; 341 AA.
AC A0A067RX71;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=5'-AMP-activated protein kinase subunit gamma-2 {ECO:0000313|EMBL:KDR24494.1};
DE Flags: Fragment;
GN ORFNames=L798_02905 {ECO:0000313|EMBL:KDR24494.1};
OS Zootermopsis nevadensis (Dampwood termite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Termopsidae; Zootermopsis.
OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR24494.1, ECO:0000313|Proteomes:UP000027135};
RN [1] {ECO:0000313|EMBL:KDR24494.1, ECO:0000313|Proteomes:UP000027135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR24494.1};
RX PubMed=24845553; DOI=10.1038/ncomms4636;
RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA Liebig J.;
RT "Molecular traces of alternative social organization in a termite genome.";
RL Nat. Commun. 5:3636-3636(2014).
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}.
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DR EMBL; KK852409; KDR24494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067RX71; -.
DR STRING; 136037.A0A067RX71; -.
DR EnsemblMetazoa; KDR24494; KDR24494; L798_02905.
DR eggNOG; KOG1764; Eukaryota.
DR InParanoid; A0A067RX71; -.
DR OMA; XHETLET; -.
DR Proteomes; UP000027135; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04618; CBS_euAMPK_gamma-like_repeat1; 1.
DR CDD; cd04641; CBS_euAMPK_gamma-like_repeat2; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR PANTHER; PTHR13780; AMP-ACTIVATED PROTEIN KINASE, GAMMA REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR13780:SF35; LD22662P; 1.
DR Pfam; PF00571; CBS; 2.
DR SMART; SM00116; CBS; 3.
DR SUPFAM; SSF54631; CBS-domain pair; 2.
DR PROSITE; PS51371; CBS; 3.
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:KDR24494.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Reference proteome {ECO:0000313|Proteomes:UP000027135};
KW Transferase {ECO:0000313|EMBL:KDR24494.1}.
FT DOMAIN 88..148
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 165..227
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 242..304
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KDR24494.1"
FT NON_TER 341
FT /evidence="ECO:0000313|EMBL:KDR24494.1"
SQ SEQUENCE 341 AA; 39247 MW; 05FF922F3BDA8070 CRC64;
SVLTGALLRR SSLEPDRRCF SLGTTTTHHR ASDVSLDPHH AAILFRDSRG LPVADPFLEK
VSISDLVEDE SQIFVKFFKF HKCYDLIPTS AKLVVFDTQL LVKKAFFALV YNGVRAAPLW
DSKRQQFVGM LTITDFIKIL QMYYTSPSVT MEELEEHKLD TWRNVLKNQV MPLVSISPDA
SLFDAIRTLI HNRIHRLPVI DHKTGNVLYI LTHKRILRFL FLYISDLPKP SYMNKTLSEL
KIGSYDNIET ANEDTSIILA LKKFVERRVS ALPIIDPEGR LVDIYAKFDV INLAAEKTYN
NLDVSLKKAN EHRNEWFEGV HKCKLEETLQ TIMERIVRAE V
//
