ID G2XEN6_VERDV Unreviewed; 712 AA.
AC G2XEN6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Carbon catabolite-derepressing protein kinase {ECO:0000313|EMBL:EGY18287.1};
GN ORFNames=VDAG_08621 {ECO:0000313|EMBL:EGY18287.1};
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:EGY18287.1};
RN [1] {ECO:0000313|EMBL:EGY18287.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY18287.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
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DR EMBL; DS572715; EGY18287.1; -; Genomic_DNA.
DR RefSeq; XP_009651225.1; XM_009652930.1.
DR AlphaFoldDB; G2XEN6; -.
DR STRING; 498257.G2XEN6; -.
DR EnsemblFungi; EGY18287; EGY18287; VDAG_08621.
DR GeneID; 20710084; -.
DR KEGG; vda:VDAG_08621; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_3_1; -.
DR InParanoid; G2XEN6; -.
DR OMA; QNGRMKE; -.
DR OrthoDB; 5475340at2759; -.
DR GO; GO:0000144; C:cellular bud neck septin ring; IEA:EnsemblFungi.
DR GO; GO:0005641; C:nuclear envelope lumen; IEA:EnsemblFungi.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IEA:EnsemblFungi.
DR GO; GO:0005774; C:vacuolar membrane; IEA:EnsemblFungi.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:EnsemblFungi.
DR GO; GO:0071940; P:fungal-type cell wall assembly; IEA:EnsemblFungi.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR GO; GO:0017148; P:negative regulation of translation; IEA:EnsemblFungi.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IEA:EnsemblFungi.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:EnsemblFungi.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IEA:EnsemblFungi.
DR GO; GO:2000222; P:positive regulation of pseudohyphal growth; IEA:EnsemblFungi.
DR GO; GO:2000217; P:regulation of invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:EnsemblFungi.
DR GO; GO:0006986; P:response to unfolded protein; IEA:EnsemblFungi.
DR GO; GO:0090606; P:single-species surface biofilm formation; IEA:EnsemblFungi.
DR CDD; cd12122; AMPKA_C; 1.
DR CDD; cd14334; UBA_SNF1_fungi; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR032270; AMPK_C.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR013896; SNF1_UBA.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF82; SERINE_THREONINE-PROTEIN KINASE MARK-A-RELATED; 1.
DR Pfam; PF16579; AdenylateSensor; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08587; UBA_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; KA1-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:EGY18287.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:EGY18287.1}.
FT DOMAIN 91..313
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 712 AA; 78869 MW; 407C06060C5D719C CRC64;
MAPPRGFEDE ELTISLSPSQ IRRRANEGWK ASPSESNPAA NTNTTTTPAM ASAARADQQA
AAAAAGRGPI PTGIGAGVRE RIKTEQRIGA YKVIKTLGEG SFGKVKLAIH NGTGQHVALK
IIARKKLISR DMAGRVEREI EYLQLLRHPH IIKLYTVIKT QNEIIMVLEY AGGELFDYII
VHRDLKPENL LLDDQLNVKI ADFGLSNIMT DGNFLKTSCG SPNYAAPEVI GGKLYAGPEV
DVWSCGVILY VLLVGRLPFD DEHIPSLFAK IARGTYSIPQ WINTGAANLI KKLLVVNPVQ
RASIDDIRAD PWFQIDLPPY LQPAVEEFYN TGVDPNQAIK KSDIAPNAPT KVQEKLHDEV
TEKISKTMGY GKKDVQEALE AEEPSAIKDA YMIVRENKLM QVNDGLASLT VDPETSNSPM
ISASSARSGT SGVGAVPRPY ISKIGILPSS LPDYHKEYVE REKAGIEDTP TPSIVVDEHG
SSSRTDAERE ELARHLKPHN KTQQRYADES GQRPQGMTPV TVPAKKVKPV RWQFGIRSRN
APWEALLCIH KALNKLGATY VPDEDYEKLH AQDESEHGGS GDGSFVDEYG SGTQQSEGAN
TSTSSIDPLK KYKLPADPWH IKVRWETKTM SRRAYDHPDS YHVHEENMKR DFVALHVDIQ
IYEMEHGVYL VDFKCSGYET ADRRLLEEKD VTSPFPFLDM AAKLIMQLAE AD
//
