SNF1_CANAX
ID SNF1_CANAX Reviewed; 620 AA.
AC P52497; Q00309;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Carbon catabolite-derepressing protein kinase;
DE EC=2.7.11.1;
GN Name=SNF1;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 32354 / B-311;
RX PubMed=9393775; DOI=10.1128/iai.65.12.4909-4917.1997;
RA Petter R., Chang Y.C., Kwon-Chung K.J.;
RT "A gene homologous to Saccharomyces cerevisiae SNF1 appears to be essential
RT for the viability of Candida albicans.";
RL Infect. Immun. 65:4909-4917(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-620.
RC STRAIN=ATCC 32354 / B-311;
RA Petter R., Kwon-Chung K.J.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential for release from glucose repression. It interacts
CC and has functional relationship to the regulatory protein SNF4. Could
CC phosphorylate CAT8 (By similarity). {ECO:0000250}.
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 -!- 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;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; L78129; AAB48643.1; -; Genomic_DNA.
DR EMBL; L39263; AAA92456.1; -; mRNA.
DR AlphaFoldDB; P52497; -.
DR SMR; P52497; -.
DR VEuPathDB; FungiDB:C5_01320W_A; -.
DR VEuPathDB; FungiDB:CAWG_04520; -.
DR BRENDA; 2.7.11.1; 1096.
DR PHI-base; PHI:7073; -.
DR GO; GO:0031965; C:nuclear membrane; 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 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 2: Evidence at transcript level;
KW ATP-binding; Carbohydrate metabolism; Kinase; Membrane; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..620
FT /note="Carbon catabolite-derepressing protein kinase"
FT /id="PRO_0000086666"
FT DOMAIN 53..305
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 59..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 208
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 7..8
FT /note="PQ -> AR (in Ref. 2; AAA92456)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..234
FT /note="AGPEVDV -> SSVQKLMI (in Ref. 2; AAA92456)"
FT /evidence="ECO:0000305"
FT CONFLICT 242..255
FT /note="YVMLCGRLPFDDEF -> GMSCCVVDYHSMTSS (in Ref. 2;
FT AAA92456)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="A -> R (in Ref. 2; AAA92456)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="R -> A (in Ref. 2; AAA92456)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="S -> L (in Ref. 2; AAA92456)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 620 AA; 70006 MW; 1806C652B5061D2B CRC64;
MSEQAQPQAS ADQQQHQHNH HHHHHHHHHN ENQSQQQVPI DPAANPANRI GRYQILKTLG
EGSFGKVKLA QHLGTGQKVA LKIINRKTLA KSDMQGRVER EISYLRLLRH PHIIKLYDVI
KSKDEIIMVI EFAGKELFDY IVQRGKMPED EARRFFQQII AAVEYCHRHK IVHRDLKPEN
LLLDDQLNVK IADFGLSNIM TDGNFLKTSC GSPNYMPAPE VISGKLYAGP EVDVWSAGVI
LYVMLCGRLP FDDEFIPALF KKISNGVYTL PNYLSAGAKH LLTRMLVVNP LNRITIHEIM
EDDWFKQDMP DYLLPPDLSK NKNSKIDVDE DVIRALSVTM GYDRDCKIVN VIEKANKQVA
AGNSSSQQSK SSNEILDAYL LMKENHALVK DLKKSKSENI ESFLSQSPPP SPFPNRGSTS
SAPGVQQSLT YQTLATVPDL STLPNSTIAI LPTSLPSIHR AYMAETKQNG DPSQQHAPPP
TKKSKTRWHF GIRSRSYPLD VMGEIYRALK NLGAEWAKPT EEELWTIRVR WKYDTSAQFE
CGSAPNLMKM QIQLFQLEPN NYLVSFKFSG WESAHGNAGT DSPQSHRQQD LDEVGSFSAY
PFLHLATRLI MELAVNSQSG
