ID A0A151X918_9HYME Unreviewed; 1162 AA.
AC A0A151X918;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=5'-AMP-activated protein kinase subunit gamma-2 {ECO:0000313|EMBL:KYQ56824.1};
GN ORFNames=ALC60_04424 {ECO:0000313|EMBL:KYQ56824.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ56824.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ56824.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ56824.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ56824.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ982409; KYQ56824.1; -; Genomic_DNA.
DR RefSeq; XP_018301613.1; XM_018446111.1.
DR RefSeq; XP_018301614.1; XM_018446112.1.
DR RefSeq; XP_018301615.1; XM_018446113.1.
DR RefSeq; XP_018301616.1; XM_018446114.1.
DR RefSeq; XP_018301617.1; XM_018446115.1.
DR AlphaFoldDB; A0A151X918; -.
DR STRING; 64791.A0A151X918; -.
DR GeneID; 108721527; -.
DR OrthoDB; 880743at2759; -.
DR Proteomes; UP000075809; 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; 3.
DR SMART; SM00116; CBS; 4.
DR SUPFAM; SSF54631; CBS-domain pair; 2.
DR PROSITE; PS51371; CBS; 4.
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:KYQ56824.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW Transferase {ECO:0000313|EMBL:KYQ56824.1}.
FT DOMAIN 778..838
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 859..917
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 932..994
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 1003..1065
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1162 AA; 128170 MW; 980F1294D1C67F51 CRC64;
MEGTGNDKQN ESDECDVNGD NRKRNDDDST GQEDVDRKMK AEDKRESLEN MNLKNEMKTL
KKTLSADDEE ADEEDEGSKE SADEEERKET QPGGEKKEQE SSSDSTSTST TDDESETSSE
DKTEPSKPET VQTTQTEATS REESKESTSK NEDTTDDSDI EDDLVSAINY NTITSLAALK
DMLQSSGEDS DGVDSFFHHY FLSHVNRLPS RNQTHSPYPW GRRLSECREE DEYETEEGKN
VDSPSVDSKK DTSKTQVEKT DSVSSKTSKP SSPSSSENSS SEKIDEKSLA TSSVSDAKPP
SPSLITTTTT TMTTTMTTMT MAMTTTMTTT TTTTTTTTTT TTSTTTIITP TTGATMATTT
VATSVSGRFT TSTVTSPTSS TKPPLRRRHT TGPGMTFPAT DPPSYSTSMT FSRTSPLPSP
HFDKRFFDSS LIEMKSQASS TSTLDYDSTE EVWVRRMDLV QERKRRELGS QPLPTIVTED
TDNSGHVSQG HRPRADTWGS HSKPIRKSSY GSAPSSGKST PLPQPAEPSS SSSSGKGGRK
TSGTRSGSTS RSNSRSNSAE RRRSGGGTDD TASPTRKPAL FDAFRPRSKS DASKRKPSII
ANMKSAVQHS LHRGSHGSSS VDVHTEKEHH RESQKEQKEN RDQGSGRPRA GSESSRNPVS
KVMDLIRHRS HSALSAEDKR KARAAVQHQS QVASQSAHRR SSLDPTARRL SLGTPAIPHR
ASDACLDPVH AAILFRDARG LPVVDPFLEK VSLSDLEEDE SQIFVKFFKF HKCYDLIPTS
AKLVVFDTHL LVKKAFFALV YNGVRAAPLW DSSRQQFVGM LTITDFIKIL QMYYTSPSVT
MDELEEHELD TWRKVLKDQV HPLVSIGPDA SLYEAIRTLI QNRIHRLPVI DPDTGNVLYI
LTHKRILRFL FLYIHELPKP SFTNKTLREL RIGTFENIET ATEETSIILA LKKFVERRVS
ALPIVDSEGK LVNIYSKFDV INLAAEKTYN NLDVSLREAN EHRNEWFEGV QSCKLDETLF
TIMERIVRAE VHRLVVIDDD DKVIGIISLS DLLFYLVLRP CGEDGSSNKG SSISLRAQDS
LLSKAPSSAQ SEASLVDGEA EQDAAETADR NQSEEAPATP SPPLSPVTSD ISEPQSTLVN
QTQEATWRDV INICVSGVSG GE
//
