SWE1_CANAL
ID SWE1_CANAL Reviewed; 1178 AA.
AC Q5AP97; A0A1D8PER4;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Mitosis inhibitor protein kinase SWE1;
DE EC=2.7.11.1;
DE AltName: Full=Wee1 homolog;
GN Name=SWE1; OrderedLocusNames=CAALFM_C110010CA;
GN ORFNames=CaO19.12331, CaO19.4867;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION.
RX PubMed=14769857; DOI=10.1083/jcb.200307176;
RA Wightman R., Bates S., Amornrrattanapan P., Sudbery P.;
RT "In Candida albicans, the Nim1 kinases Gin4 and Hsl1 negatively regulate
RT pseudohypha formation and Gin4 also controls septin organization.";
RL J. Cell Biol. 164:581-591(2004).
RN [5]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=15659158; DOI=10.1111/j.1365-2958.2004.04405.x;
RA Umeyama T., Kaneko A., Nagai Y., Hanaoka N., Tanabe K., Takano Y.,
RA Niimi M., Uehara Y.;
RT "Candida albicans protein kinase CaHsl1p regulates cell elongation and
RT virulence.";
RL Mol. Microbiol. 55:381-395(2005).
RN [6]
RP FUNCTION.
RX PubMed=16468988; DOI=10.1111/j.1365-2958.2005.05038.x;
RA Andaluz E., Ciudad T., Gomez-Raja J., Calderone R., Larriba G.;
RT "Rad52 depletion in Candida albicans triggers both the DNA-damage
RT checkpoint and filamentation accompanied by but independent of expression
RT of hypha-specific genes.";
RL Mol. Microbiol. 59:1452-1472(2006).
RN [7]
RP FUNCTION.
RX PubMed=17093060; DOI=10.1091/mbc.e06-05-0411;
RA Court H., Sudbery P.;
RT "Regulation of Cdc42 GTPase activity in the formation of hyphae in Candida
RT albicans.";
RL Mol. Biol. Cell 18:265-281(2007).
RN [8]
RP FUNCTION.
RX PubMed=19778960; DOI=10.1099/mic.0.033233-0;
RA Gale C.A., Leonard M.D., Finley K.R., Christensen L., McClellan M.,
RA Abbey D., Kurischko C., Bensen E., Tzafrir I., Kauffman S., Becker J.,
RA Berman J.;
RT "SLA2 mutations cause SWE1-mediated cell cycle phenotypes in Candida
RT albicans and Saccharomyces cerevisiae.";
RL Microbiology 155:3847-3859(2009).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=20140194; DOI=10.1371/journal.ppat.1000752;
RA Blankenship J.R., Fanning S., Hamaker J.J., Mitchell A.P.;
RT "An extensive circuitry for cell wall regulation in Candida albicans.";
RL PLoS Pathog. 6:E1000752-E1000752(2010).
CC -!- FUNCTION: Protein kinase that acts as a negative regulator of entry
CC into mitosis (G2 to M transition) by phosphorylating and inhibiting the
CC mitosis-promoting cyclin B-bound CDC28 at 'Tyr-18'. SWE1-mediated
CC inhibition of CDC28 acts in a cell size or morphogenesis checkpoint to
CC delay mitosis in response to defects in growth, actin organization or
CC bud formation. Plays an important role in filamentous growth.
CC {ECO:0000269|PubMed:14769857, ECO:0000269|PubMed:15659158,
CC ECO:0000269|PubMed:16468988, ECO:0000269|PubMed:17093060,
CC ECO:0000269|PubMed:19778960}.
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: Bud neck {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15659158}.
CC -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to caspofungin.
CC {ECO:0000269|PubMed:20140194}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. WEE1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; CP017623; AOW26632.1; -; Genomic_DNA.
DR RefSeq; XP_723552.2; XM_718459.2.
DR AlphaFoldDB; Q5AP97; -.
DR SMR; Q5AP97; -.
DR STRING; 237561.Q5AP97; -.
DR PRIDE; Q5AP97; -.
DR GeneID; 3634866; -.
DR KEGG; cal:CAALFM_C110010CA; -.
DR CGD; CAL0000197159; SWE1.
DR VEuPathDB; FungiDB:C1_10010C_A; -.
DR eggNOG; KOG0601; Eukaryota.
DR HOGENOM; CLU_009087_0_0_1; -.
DR InParanoid; Q5AP97; -.
DR OMA; KMFKNAN; -.
DR OrthoDB; 718303at2759; -.
DR PRO; PR:Q5AP97; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 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 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1178
FT /note="Mitosis inhibitor protein kinase SWE1"
FT /id="PRO_0000424371"
FT DOMAIN 791..1154
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 929
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 797..805
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 818
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 934
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 947
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1178 AA; 130733 MW; F9662B10E7805023 CRC64;
MDSNPCQDVS GDTSSTPMAN NNPTNDSTIS SQNHSKIGLR KHQQQHYHQH SHSQMHSHSQ
QSPYINQLEY FTNNQFSRSF NSLILEDAND ANTNNSSTTT LNKKTINKSP PFNIKQDLLN
DSIDTFLDNS NTETIEDGDV TTTDDDHDFD DEDIEDPEAV QYTPTLNILK SKKVDSFDII
SSKHRKSNSQ ITYNSHVRKP SEEDTSSSMA TIRLSNNSQS SIKRSSKYLN LSIDSNLKTV
DGGKIPDEID DISLNEIDVA VAPNDFSSPL SARKPDIFAA ITAANGNSNN QFKRPHKLVS
QSPSPSSKNK FRISSSTTSS PQSNLHSPSK LGSKGFKMFK NANRDAIMSS SRVMTPEKPK
MVSKIFGKSA KIRRAYTPTH TSTPMAVSSL NPPSSSTSNS TTAAITSTSP PANEHYDIDN
DFDSPSKNRK SSNISASSII IYQDENHIKS NHARKSSNPI PYPPTEPLPT NISASVAETG
KGSTTTKSNL SKGCPLFDDK ENKASYQFVK PLQTAFNSSG LVKKNSISGS SDRKLPPETP
IKRNPLMILN TNKVVPPYSS GFAEGKDVMG DQHDIYSHIP CQNQRFPGSV NPNTTTNNNN
TQQHHDSDLS IEVGRNNSYD ASSSTINNTS YIKIFPSSEL KKEQVLQRPQ EDLELVFNSD
IELDDNIIPE TPTKKSLLPN QHHQHHLPLY TQSKSPLLKF DTEKDGRRNL SIVLDKSNAT
KREISEPPST PINMSFAKNS FKKPMNNAER GDDPDSIIAQ RIDIMPSLDE ADSVSVYPSK
IDEHLIEKFG MKNIKYIGSG AFSIAFECLF NNEKFAIKRT KKPLIGKLEK QTIKREIEAL
RVLTSIKEDE ATNMQEQEEG KEYLVYFIEA WDFNNYYYIM TEFCEGGTLF DFLEENKHYK
IDEFRIWKIL IEILNGLKFI HSKNYLHLDL KPANIFITFE GSLKIGDFGL ATKLPILEKD
FDLEGDRNYI APELINDKIY TPFADIFSLG LIILEIAANI ILPDNGTPWR KLRSGDLSDA
GRLSSDNISM FLQHNPNTNS NISGSGSRSG SGSTGGNGSA GDGSTNSTNF SYNSLSGNSL
TLNPPVKAVH GTSDTNNTLA SELSKNIEGL IPSWAPDFLV HGDSMNLDKL VNKMLRPNPF
DRPSACNILE MPECLIVENR RKCGATIFEG EFGSPPDE
