SNF1_FUSVI
ID SNF1_FUSVI Reviewed; 698 AA.
AC P0DP15;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Sucrose non-fermenting protein kinase 1 {ECO:0000303|PubMed:28132080};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P06782};
GN Name=SNF1 {ECO:0000303|PubMed:28132080}; ORFNames=g3696;
OS Fusarium virguliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=232082;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mont-1;
RX PubMed=24454689; DOI=10.1371/journal.pone.0081832;
RA Srivastava S.K., Huang X., Brar H.K., Fakhoury A.M., Bluhm B.H.,
RA Bhattacharyya M.K.;
RT "The genome sequence of the fungal pathogen Fusarium virguliforme that
RT causes sudden death syndrome in soybean.";
RL PLoS ONE 9:E81832-E81832(2014).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Mont-1;
RX PubMed=28132080; DOI=10.1007/s00294-017-0676-9;
RA Islam K.T., Bond J.P., Fakhoury A.M.;
RT "FvSNF1, the sucrose non-fermenting protein kinase gene of Fusarium
RT virguliforme, is required for cell-wall-degrading enzymes expression and
RT sudden death syndrome development in soybean.";
RL Curr. Genet. 63:723-738(2017).
CC -!- FUNCTION: Catalytic subunit of the AMP-activated protein kinase complex
CC also known as the SNF1 kinase complex (Snf1c), a central regulator of
CC cellular energy homeostasis, which, in response to a fall in
CC intracellular ATP levels, activates energy-producing pathways and
CC inhibits energy-consuming processes (By similarity). The complex
CC phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac
CC formation, leading to transcriptional activation through TBP
CC recruitment to the promoters (By similarity). Activates the expression
CC of the galactose oxidase (GOA) gene and of several cell wall-degrading
CC enzymes (CWDEs) such as pectate lyase, xylanase and glucanase
CC (PubMed:28132080). Plays an important role in sudden death syndrome
CC (SDS) by controlling the colonization of the infected roots
CC (PubMed:28132080). {ECO:0000250|UniProtKB:P06782,
CC ECO:0000269|PubMed:28132080}.
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:0000250|UniProtKB:P06782};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P06782};
CC -!- SUBUNIT: Component of the AMP-activated protein kinase complex also
CC known as the SNF1 kinase complex (Snf1c), a heterotrimeric complex
CC composed of a catalytic subunit alpha and 2 regulatory subunits beta
CC and gamma (By similarity). {ECO:0000250|UniProtKB:P06782}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06782}. Nucleus
CC {ECO:0000250|UniProtKB:P06782}. Note=Nuclear translocation occurs under
CC nitrogen and glucose starvation conditions (By similarity).
CC {ECO:0000250|UniProtKB:P06782}.
CC -!- DOMAIN: The regulatory domain (RS) also called auto-inhibitory domain
CC (AID) inhibits kinase activity of the protein kinase domain (KD) (By
CC similarity). {ECO:0000250|UniProtKB:P06782}.
CC -!- DOMAIN: The ubiquitin-associated domain (UBA) localized within the AID
CC dampens kinase activation, probably by restraining alpha-gamma
CC associations (By similarity). {ECO:0000250|UniProtKB:P06782}.
CC -!- DISRUPTION PHENOTYPE: Impairs the expression of the galactose oxidase
CC gene which abolishes galactose utilization and causes poor growth on
CC xylose, arabinose and sucrose (PubMed:28132080). Impairs severely the
CC ability to cause sudden death syndrome (SDS) on challenged soybean
CC plants through preventing to colonize the xylem vessels and phloem
CC tissue during infection (PubMed:28132080).
CC {ECO:0000269|PubMed:28132080}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0DP15; -.
DR SMR; P0DP15; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd14334; UBA_SNF1_fungi; 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 Pfam; PF16579; AdenylateSensor; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08587; UBA_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; SSF103243; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Carbohydrate metabolism; Cytoplasm; Kinase;
KW Nucleotide-binding; Nucleus; Serine/threonine-protein kinase; Transferase;
KW Virulence.
FT CHAIN 1..698
FT /note="Sucrose non-fermenting protein kinase 1"
FT /id="PRO_0000439650"
FT DOMAIN 62..313
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 360..397
FT /note="UBA"
FT /evidence="ECO:0000250|UniProtKB:P06782"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..417
FT /note="Auto-inhibitory domain (AID)"
FT /evidence="ECO:0000250|UniProtKB:P06782"
FT REGION 410..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 68..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 698 AA; 78591 MW; 7C38FA000079FA7A CRC64;
MAPRGFEDEE LTISLSSSHV RRPQQQQPPP PTQQQHAHQP GSRPADAPLK ERIKTEQRIG
AYKVLRTLGE GSFGKVKLAI HNGTGQQVAL KIIARKKLIS RDMAGRVERE IEYLQLLRHP
HIIKLYTVIK TPNEIIMVLE YAGGELFDYI VQHGRMKEAE ARRFFQQMLC AVEYCHRHKI
VHRDLKPENL LLDENLNVKI ADFGLSNIMT DGNFLKTSCG SPNYAAPEVI GGKLYAGPEV
DVWSCGVILY VLLVGRLPFD DEHIPSLFAK IAKGTYSIPQ WMPLGAANLI KKMLVVNPVH
RATIEDIRAD PWFTTELPVY LQLPVEEFFN TGVDPNKAIQ KNDIAPNAPE KVQERLHNEV
TEKISKTMGY GKNDVEEALQ ASEPSAIKDA YMIVRENKMM QVNQHPEALL EPEGSSPMLS
MSSARSATST TTTTAPRPYV SKVGILPSSL PAYHKDYVER EKAGSVNNSP PQVLINDELP
VTRTDAEKEE TSRRLRPHSR SQLRLDEANT RPQGMTPINP PKKTKPVRWQ FGIRSRNSPW
EALLCIHKAL HKLGATYIPD EDYESRHAEE RAEASGNGSF ADSYDGSRGS TTSIDPMKRY
RLPADPWHIN VRWDTSAIKK KLQGSADTPD KRQAHEPFVA LHLDIQIYEM EHGVYLVDFK
CSGYETATGR LLEEKEVTSP FPFLDMAAKL IMQLAEAD
