ID G2X7Q1_VERDV Unreviewed; 537 AA.
AC G2X7Q1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=AMP-activated protein kinase glycogen-binding domain-containing protein {ECO:0000259|Pfam:PF16561};
GN ORFNames=VDAG_06509 {ECO:0000313|EMBL:EGY15019.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY15019.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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DR EMBL; DS572706; EGY15019.1; -; Genomic_DNA.
DR RefSeq; XP_009657182.1; XM_009658887.1.
DR AlphaFoldDB; G2X7Q1; -.
DR EnsemblFungi; EGY15019; EGY15019; VDAG_06509.
DR GeneID; 20707972; -.
DR KEGG; vda:VDAG_06509; -.
DR eggNOG; ENOG502STER; Eukaryota.
DR HOGENOM; CLU_486603_0_0_1; -.
DR InParanoid; G2X7Q1; -.
DR OMA; IGIGWWQ; -.
DR OrthoDB; 1969424at2759; -.
DR Proteomes; UP000001611; Chromosome 8.
DR CDD; cd02859; E_set_AMPKbeta_like_N; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR SUPFAM; SSF81296; E set domains; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001611}.
FT DOMAIN 6..94
FT /note="AMP-activated protein kinase glycogen-binding"
FT /evidence="ECO:0000259|Pfam:PF16561"
FT REGION 80..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 58553 MW; 929FEDD41341EC64 CRC64;
MAASKVPITL TYRKPGTQPP LFVAGTFSNP QWEAQEMQVT TGDDGEHTFS KPLHLPPGSK
IQYKIRIGPG DWWVLNDDAP TVTDEAGNRN NVLIAPERDE AHADDEARNN DSIDERSNTS
HAGVNMNGST HSEVLPAPKP RGVDKLRERS EEELQHLTAT PPEEVAETAA EVADTAENLD
ADKDGKDTND RENSTVCLID SFPDEEEDLD AQSELPPLFA HECLGGSDPV PEVVSPPVRR
SSEARSGSVD YNIDKYDLND PTLERWPSDR NAIMDAVRRV ESSRDEDQTY VLGSPISPII
TSRRASKIEE DIALSPEFPS LVTAAKLDVP TRKQSHGSMV SNRSLTSLAS IVEEDNRRIE
EEGDDEEAVE DLRPSPVVRL PSPAVKVTPD LLRSPASDDD EGVVLKSSRS DLDLKSDTNT
PAAALELPEH ATSESQPSPP VQQDQPSARA PPPDEMDELD DDGADGSIGQ RAAPQGEDSA
DGQLRRRNLS NDGSVASSSA QGAKDADSSN WLQAFFRVLF VDWIGGFVRQ LFHGNRK
//
