ID A0A0V0V7T2_9BILA Unreviewed; 703 AA.
AC A0A0V0V7T2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=5'-AMP-activated protein kinase subunit gamma-1 {ECO:0000313|EMBL:KRX59381.1};
GN ORFNames=T09_14737 {ECO:0000313|EMBL:KRX59381.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX59381.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX59381.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX59381.1};
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:KRX59381.1}.
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DR EMBL; JYDN01000073; KRX59381.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0V7T2; -.
DR Proteomes; UP000054681; 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 CDD; cd00754; Ubl_MoaD; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
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 SUPFAM; SSF54285; MoaD/ThiS; 1.
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:KRX59381.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transferase {ECO:0000313|EMBL:KRX59381.1}.
FT DOMAIN 416..476
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 549..611
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 620..680
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 136..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 77872 MW; 8183861B8CDE4A04 CRC64;
MEADDCWNNG KEGFSVQNSN DITDSGTKLI VQILFFAQAR ELTGLSSCSL ELEKPLFHQS
VRPMYGADLK ALIVEKFPSL RPIASTLLIA VNSDYVRFDD EVHLFQGVEV AVIPPSADLV
SSGGAIDCAT AEQRFEKRSS TKSQGNGQVV TGRRRGKGES STKKFGQFLC DQFRPRSKSD
IASRGQEPTA KGGGDDEQQR CYATVTSNAV NYHRTDCRQQ WNLAGMKLKA AVERRRNSSS
CTVPCPPPVP LVRLADQQPL YVDTNLANDV TSPCLLDSCF SDALSTTGRR FTGVDGHLKC
RAKKLFPCSC PSSGPPTLGS SRAVQGNRRL SESSAAAEQL RGRNLSLFSA LSADYSEMNQ
LAGYASIFST MHDKAGNAVP YGNSAVGHRH LFLSENQDLI YSQFIKSHHC YDLIPTSTKL
VVFDTKLPVK KAFFALVYNS VRAAPLWDDA TQQFVGMLTI TDFIRILQKY YKSGEENIKE
LEEHPTASLL DAVNILCNKK VHRLPVIDPC SGNILYILTH KRILKFLFLY MPDLPMPSFM
KKSPKELGIG TWSNIHTVTK VTPLIEVLRK LLELRVSALP VVDENDRVID IYSKFDVINL
AAEKAYNNLD ITVQDSLKHR TAWFEGVHNC KVTDSLSTYV DTLVRSEVHR LVAVDNDGRV
QGVVSLSDIL LFIVLRPEVT GSVSNVQTAE VSSSMERSED MEM
//
