HSL1_CANAL
ID HSL1_CANAL Reviewed; 1462 AA.
AC Q5AG71; A0A1D8PNJ3;
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=Serine/threonine-protein kinase HSL1;
DE EC=2.7.11.1;
GN Name=HSL1; OrderedLocusNames=CAALFM_C502840CA;
GN ORFNames=CaO19.11784, CaO19.4308;
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 DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, 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).
CC -!- FUNCTION: Protein kinase involved in determination of morphology during
CC the cell cycle of both yeast-form and hyphal cells via regulation of
CC SWE1 and CDC28. Regulates pseudohypha formation, but is not required
CC for septin ring organization or septum formation. Plays an essential
CC role in virulence in a mouse model. {ECO:0000269|PubMed:14769857,
CC ECO:0000269|PubMed:15659158}.
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:0000269|PubMed:15659158}. Note=In
CC the hyphal cells, localizes at a potent septation site before the
CC completion of septum formation.
CC -!- PTM: Phosphorylated throughout the cell cycle, except for the G1 phase.
CC {ECO:0000269|PubMed:15659158}.
CC -!- DISRUPTION PHENOTYPE: Leads to elongated cell phenotype.
CC {ECO:0000269|PubMed:15659158}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. NIM1 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 EMBL; CP017627; AOW29709.1; -; Genomic_DNA.
DR RefSeq; XP_720615.2; XM_715522.2.
DR AlphaFoldDB; Q5AG71; -.
DR SMR; Q5AG71; -.
DR BioGRID; 1220785; 2.
DR STRING; 237561.Q5AG71; -.
DR PRIDE; Q5AG71; -.
DR GeneID; 3637810; -.
DR KEGG; cal:CAALFM_C502840CA; -.
DR CGD; CAL0000190859; HSL1.
DR VEuPathDB; FungiDB:C5_02840C_A; -.
DR eggNOG; KOG0588; Eukaryota.
DR HOGENOM; CLU_003363_0_0_1; -.
DR InParanoid; Q5AG71; -.
DR OrthoDB; 1127668at2759; -.
DR PRO; PR:Q5AG71; -.
DR Proteomes; UP000000559; Chromosome 5.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR031850; Fungal_KA1_dom.
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; PF16797; Fungal_KA1; 1.
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; Coiled coil; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Virulence.
FT CHAIN 1..1462
FT /note="Serine/threonine-protein kinase HSL1"
FT /id="PRO_0000424369"
FT DOMAIN 65..330
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1269..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 636..715
FT /evidence="ECO:0000255"
FT COMPBIAS 41..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..622
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1154
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 71..79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1462 AA; 163674 MW; 8D52BF6D941643D0 CRC64;
MSTVVNRRSS HQFDSPSNHL DHSSSMNVDK VVQSVTNATK RLSQISTNTN NSNKKRKTQN
KIGPWKLGRT LGRGSTGRVR LAKNTTTGQL AAVKIVPKSN FKKLENPKYK RSKEDATRLP
YGIEREIIIM KLISHPNIMG LYDVWENKND LYLILEYIEG GELFDYLIKR GKLQEYEAIN
YFKQIINGIN YLHQFNICHR DLKPENLLLD FNKNIKIADF GMAALEVKEK LLETSCGSPH
YASPEIVAGK NYHGAPSDIW SCGIILFALL TGHLPFDDEN IRKLLLKVQS GKFNMPPELS
FEAKDLITKM LKVNPRERIT IDAILTHPLL AKYPEPTVSY SSTTTLDINS INIKQIESVD
KIDKEILKNL SVLFHNCDEK TIISRLLSPN RCPEKMFYYL LMKYRNEHLS NSNSFNSSND
VDSARSLPRS TSYVKTTVTD HATGEKHTTV KKIQQSSSIY SNRSLLKKST SAKGNVLSNI
TNRPNTPKQF SASSSFNKKK ALHSKTQIYA SRSRNASSRS LKSNSSTGRN GNNASVTSVN
KIPEITGATV LQPIPSMAMN RGDEQQNKTK KNLTGTFGNK SLLNFQLICE EVFENDKENS
KPVSKTPVSQ LPPPPPPPIE TPTSRTNSVK RGKTWSLARR ERELAEQVRQ RNEARENKLK
AEELARKELE QEKKRIAEEK KRLEQQEREL DEKQKLQEKQ KAALEKLQKH QSAHDFEGLF
ASNRRSVTDM APSSGMSSLD PRAHMVSRAN TIGSPNLSSS SVNIDENASK VLHKFGIDVA
PSPKRFSRAS KTSTSKNLSS FLAPTVSRNL SSQLKTSSSK NLAGYLHGTT DTNGSAIAAK
KKDNSTNKAL TIEEFNAKER TSMSPSISKA SVNKRNSNQS SYYRSMFSDN GNDDNVTKVR
TRESHLSVQE EEEMDMENAI DEDISLIPNP RFSRFSFGGL LGSNTVANEE GDWTIMNSTL
NHSNTVVRRT HNKSSTMLGL GIKMRDTTTI KEDEEFEDEK PFISVPSSED DEGNTHKNKR
GGLRDSGNYD FDEEHSVAST ANTEYSDVAS QGQQRPGSHT IHQLETELSN FDLLSYRVAD
IGKVNKHKPS IVDSKETLLK NHSSDEATIE VKEDNNEHDF NDKIKQHYDD NGDSEEDDED
EDEEEEDDDD DDDARSSFEA RPHSHNYSLA EITSESPVGG GYESPSIAND FKKSRHSTGI
FSTTQFPRSP YVVNNNGDSN KDENSQQQTK HMLNDGHKGL ITSPVQDTFG SKKPVESNSL
FRRLSLNPNR AAPKAPAPPP PSAPTSSAAK ANISQPLSSP TKGHNRFSRI SIGSKNMLQK
EDKSTKSNWF KKFFHSLTTP STKEQSGNSS SKVASKDIKI IDTSLTAAQL IRVIKYQLEL
KKIEGSISKV DIDEEFGLIS GVIPSKFANG RKLKFKIEVI DLINSSSLHV IKMKGNDKGF
QSLVNIVTFI IKKEEQDKIC RR
