HAD1_CRYNH
ID HAD1_CRYNH Reviewed; 411 AA.
AC J9VX38;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Probable phosphatase HAD1 {ECO:0000303|PubMed:29233914};
DE EC=3.1.3.- {ECO:0000305};
GN Name=HAD1 {ECO:0000303|PubMed:29233914};
GN ORFNames=CNAG_01744 {ECO:0000312|EMBL:AFR97946.1};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000312|Proteomes:UP000010091};
RN [1] {ECO:0000312|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
RN [2] {ECO:0000305}
RP PHOSPHORYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=27611567; DOI=10.1371/journal.ppat.1005873;
RA Park H.S., Chow E.W., Fu C., Soderblom E.J., Moseley M.A., Heitman J.,
RA Cardenas M.E.;
RT "Calcineurin Targets Involved in Stress Survival and Fungal Virulence.";
RL PLoS Pathog. 12:e1005873-e1005873(2016).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29233914; DOI=10.1534/g3.117.300444;
RA Jung W.H., Son Y.E., Oh S.H., Fu C., Kim H.S., Kwak J.H., Cardenas M.E.,
RA Heitman J., Park H.S.;
RT "Had1 Is Required for Cell Wall Integrity and Fungal Virulence in
RT Cryptococcus neoformans.";
RL G3 (Bethesda) 8:643-652(2018).
CC -!- FUNCTION: Probable phosphatase (Probable). Required for cell wall
CC integrity and virulence (PubMed:29233914).
CC {ECO:0000269|PubMed:29233914, ECO:0000305}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:27611567}.
CC -!- DISRUPTION PHENOTYPE: Decreases virulence in mouse intranasal and
CC intravenous model for infection (PubMed:29233914). Sensitive to: high
CC temperature; sodium dodecyl sulfate (cell wall stress inducer); Congo
CC Red (cell wall stress inducer); dithiothreitol; Calcofluor White; salt
CC stress (induced by KCl) (PubMed:29233914). Simultaneous disruption of
CC CRZ1 results in phenotypic enhancement (PubMed:29233914).
CC {ECO:0000269|PubMed:29233914}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; CP003830; AFR97946.1; -; Genomic_DNA.
DR RefSeq; XP_012052729.1; XM_012197339.1.
DR AlphaFoldDB; J9VX38; -.
DR SMR; J9VX38; -.
DR EnsemblFungi; AFR97946; AFR97946; CNAG_01744.
DR GeneID; 23885433; -.
DR VEuPathDB; FungiDB:CNAG_01744; -.
DR HOGENOM; CLU_669051_0_0_1; -.
DR PHI-base; PHI:7867; -.
DR Proteomes; UP000010091; Chromosome 11.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Phosphoprotein; Virulence.
FT CHAIN 1..411
FT /note="Probable phosphatase HAD1"
FT /id="PRO_0000451403"
FT REGION 14..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 61
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT ACT_SITE 63
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P60487"
FT BINDING 63
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P60487"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P60487"
SQ SEQUENCE 411 AA; 43933 MW; 5BB5EE5C534E4C2F CRC64;
MSVFTKSAFT MSALPSPNTS QPPSAAPSRR GSFANGLASG QLTPVTDPHI VSINVESVLF
DMDGTLINSS PAVVKAWELF AEKYPLDLDD ILRSAHGMRT IDVLKKWCKI TDPELLASEV
IRFETAILNS AEDIAKHSGK AGIEVLPGVA KLLADLGEEA DKRDGEEKWA ICTSSTYFYA
GKAIPIAGLP TPKVFVTADS VTRGKPFPDP YLLGASGCNA SPFESLVVED APTGIRSGKA
SGALVLATCT SHEREELERE RPDFLVDDLS HVKASWDAAT NTFNLIIEQP IDRYTPRPTP
DVTPVITPAM SRSNSFSGVG QDRPSVRNTQ TIMKGSDDLT GNDSVVGSPA ASRPGSPGAD
DSVEKRAEME FHRRASQSGQ AGVTLDAFRR ALAGNAAKRR AQSQGEMSQD E
