ID A0A212EI97_DANPL Unreviewed; 774 AA.
AC A0A212EI97;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=SNF4/AMP-activated protein kinase gamma subunit {ECO:0000313|EMBL:OWR41233.1};
GN ORFNames=KGM_212579 {ECO:0000313|EMBL:OWR41233.1};
OS Danaus plexippus plexippus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR41233.1, ECO:0000313|Proteomes:UP000007151};
RN [1] {ECO:0000313|EMBL:OWR41233.1, ECO:0000313|Proteomes:UP000007151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR41233.1};
RX PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT "The monarch butterfly genome yields insights into long-distance
RT migration.";
RL Cell 147:1171-1185(2011).
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:OWR41233.1}.
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DR EMBL; AGBW02014676; OWR41233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212EI97; -.
DR STRING; 278856.A0A212EI97; -.
DR KEGG; dpl:KGM_212579; -.
DR eggNOG; KOG1764; Eukaryota.
DR InParanoid; A0A212EI97; -.
DR Proteomes; UP000007151; 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:OWR41233.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Reference proteome {ECO:0000313|Proteomes:UP000007151};
KW Transferase {ECO:0000313|EMBL:OWR41233.1}.
FT DOMAIN 442..507
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 519..581
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 596..658
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 667..728
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 774 AA; 88689 MW; 9560E8036A19E85C CRC64;
MHGISHFLHK HNSRESTPPL IKDNSSESWC STLSSTDSRS SVQNDTASKA IPINRRGCSA
QRSFRGSPLE FASSPRDRYP NFTSYYRDVM EGHGSPSPHH YNASNWDVRQ RRTDEERYQS
NMNAYHVSRQ DYRHFVSPLY NEVMDDIQEN EYSKCEKYGE ISSTKLSHGS YKNRFDNKSF
AHKLSESANS PKDFQSHTTE RRGSGSSTSG HRHKHSIQDL IRTFSKKVGN WRHESGEGRR
GSCAVPAANS ERTVQTEEFR SRSKSLDADN LQKGMKISIL DDCGATYQIF EKILQEGAYL
RRAASQEAEK RRSSLGNVPS GRHRMSDAFL DPHHAAMLFR DSRGLPVADP FLEKVSLSDL
AVGGGGRCAA VRMLRLHYYS DNPALVVECE EESVYAIELI KEFEEVGRAW KAFLADWLIK
EEDESQIFVK FFKFHKCYDL IPTSAKLVVF DTQLLVKKAF FALVYNGVRA APLWDSQRQR
FVGMLTITDF IKILQMYYTS PNVTMDELEE HRLETWRQVL KGSVMPLVSI GPDSSLYDAI
KMLITNRIHR LPVIDPDTGN VLYILTHKRI LRFLFLYINE LPKPSYLQCK LRDLRIGTLN
DIETATEDTS IIQALRKFVN RRVSALPLID SEGRLKDIYA KFDVINLAAE KTYNNLDVSL
KKANEHRNEW FEGVQKCNLD ETLYEVMERI VRAEVHRLVV VNEDDKVTGI ISLSDLLMYL
VLRPTGDCEG ASLRNEHGPI EEKDETTNTE DKPTDEDKKL ITTDTETTQQ ECQH
//
