ID A0A1I8IW49_9PLAT Unreviewed; 391 AA.
AC A0A1I8IW49;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=5'-AMP-activated protein kinase subunit gamma-1-like {ECO:0000313|WBParaSite:maker-uti_cns_0018489-snap-gene-0.1-mRNA-1};
GN ORFNames=BOX15_Mlig024209g1 {ECO:0000313|EMBL:PAA60553.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0018489-snap-gene-0.1-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0018489-snap-gene-0.1-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:PAA60553.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA60553.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA60553.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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}.
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DR EMBL; NIVC01002138; PAA60553.1; -; Genomic_DNA.
DR STRING; 282301.A0A1I8IW49; -.
DR WBParaSite; maker-uti_cns_0018489-snap-gene-0.1-mRNA-1; maker-uti_cns_0018489-snap-gene-0.1-mRNA-1; maker-uti_cns_0018489-snap-gene-0.1.
DR Proteomes; UP000095280; Unplaced.
DR Proteomes; UP000215902; Unassembled WGS sequence.
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 Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Reference proteome {ECO:0000313|Proteomes:UP000215902}.
FT DOMAIN 82..142
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 163..221
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 236..298
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 308..367
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 43803 MW; 9DA9A694EE3C600A CRC64;
MSQGQPPLVS PSASSGLPAR QRSQSGAEVQ VTENEKYIIF RSRCQNDCSS VDMEEVRTES
LGDPSRVFAI FVQKHRCYDL IPTSNKLLVF DNSLNVRKAF FALVYNGLRA APLWDAQQQR
FVGMLTISDF IHILQNYYRS ALVPMEELET HRISTWRAEL SNRLKPLIWI SPEASLHDAV
RLLLQARVHR LPVIDPATGN ALFIVTHKRI LKYIFLYIHQ LPMPAWLARP VKQLGIGTYS
DIVTIGETTP LVRVLSLFVQ NRVSALPVVN GDGRLVDIYS KFDVINLAAT KTYNNLDISV
KEALQYRRDR FEGVSSCRGE DSLKSVIEKL VTAEVHRLVV TDSDNRVAGL LSLSDVLKAL
IVDCDKFGCC EAGDGDTMDS AFAPVESMDM S
//
