ID J9VQS3_CRYNH Unreviewed; 2438 AA.
AC J9VQS3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000256|ARBA:ARBA00012009};
DE EC=2.7.1.150 {ECO:0000256|ARBA:ARBA00012009};
GN ORFNames=CNAG_01209 {ECO:0000313|EMBL:AFR94934.2};
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:0000313|EMBL:AFR94934.2, ECO:0000313|Proteomes:UP000010091};
RN [1] {ECO:0000313|EMBL:AFR94934.2, ECO:0000313|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC {ECO:0000313|Proteomes:UP000010091};
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., Bahn Y.S.,
RA Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA 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).
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DR EMBL; CP003824; AFR94934.2; -; Genomic_DNA.
DR RefSeq; XP_012049022.1; XM_012193632.1.
DR GeneID; 23884948; -.
DR KEGG; cng:CNAG_01209; -.
DR VEuPathDB; FungiDB:CNAG_01209; -.
DR HOGENOM; CLU_000480_3_0_1; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000010091; Chromosome 5.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd03334; Fab1_TCP; 1.
DR CDD; cd15725; FYVE_PIKfyve_Fab1; 1.
DR CDD; cd17300; PIPKc_PIKfyve; 1.
DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR Gene3D; 3.50.7.10; GroEL; 1.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR044769; PIKfyve_PIPKc.
DR InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45748; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR PANTHER; PTHR45748:SF7; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 367..427
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 2083..2409
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1492..1513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1546..1626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1644..1773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1786..1846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1880..1952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1560..1575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1576..1590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1644..1666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1668..1709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1715..1764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1786..1802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1831..1846
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1883..1899
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1909..1952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2438 AA; 270456 MW; 473BB2950FCBC06E CRC64;
MPSSFSEHSI PPSSHLTTFP NPFQDEPEQG ILPTFLSKVK QTFTSGISQP PTQNSHASSD
RLPHLIEGEN KIAHDGDSNL VAPPREGGQT EAQAIAEAVM RNRIQTAAQG ALPNSAAEQQ
QRMHGQSAGS IGAVVATSAE ALPPTQSTAH PSNLSIHTTH GQPLNQPIGP VNTFGSSNPH
LPVPASVASS QVSISGQKRA VAPGGPQWRP SGVAPAQVTV SPVTTTVQTA SKEPISSPAR
PIRFPSTKPP HRGNVNLQSS ISSSSRAPTP LPHHIHTNLL STGQNKRHRR SSVATLPDSP
SSLSISGMIA ANAELTQSHS YVPGFPLAQD DTRSVRSMGA VKRLNSVSRI IKRMKGDGLS
KQYWMADEHC KECYDCKSIF TAWRRKHHCR ICGQIFCSRC ASNIIGARRF GQEGVVRVCN
LCLKIMEEYK DDDDDDRRSI NSFSTSVHRY PTISDRAFLN TAMSPEMPYA KSPFAASQLF
SSHPNDSLMA IDEASVPIRW EDGRLDTERA FLLNEVGRSP TSDRDDHIWA GRPPTVAPFR
RPLELDQKVA ADQGEADGDG RVSTPVLETS GSALHATYRD ATSFPFPRTN TMSTDDDVER
VPLSREDSGH PLIGLKTRMN QAVLTALLDS EKSEGLWRAR SHSFAHQPEM LTGASLQHFK
LMLSQAIARA ELPKADEWHR ILTSLILKVP LNLQPNVRAG DDIDVRAYVK IKKVPGGKIS
DSEYVDGIVI TKNVAHKAMS RRLVNPRIMV VTFPLDYHRV DNQFMSLDPI LAQEKDYLRL
LTKRIVDARP HIVLAQSSVS RIALDYLLEA NVALARSVKT SAIQQVARCT QADVVASMDR
LVLEPRMGRC GEFRIQSFDH ELIPGRRKTL MRFEGASKEQ GCTIILRGAD LPTLRKVKVI
TDFMALVAYH LRNEMIMYND EHNIPPPKPV LPTEYRELLD LLDSDKPPAE GSPSCDTPSQ
LSHSTATLKP SLKPITPPDD IEFISESSST PTPNQNPIQS DDKQLEKRDA LEVTRQIAKS
LEPYLTVVLS SSAAIMFPPP AILAKMVELD RRLSELRVNR DEAEAAQILE EETKVAEVPK
DSAPNAGGTD SETVSLAPTS ISEATRSSSE VPISDAMSVY PTTSTSKPPI RDPYHILRKP
QEVSQESALA QVEHAHQEQI RLWRWYTRRF AEELRPENYQ GIVYLSSLGC EGAEKPCMEP
SLQRIDYYQP GDQTVGQFLE NLALVAPDQC TSKNCERLLL FHYHLLVHGQ RRLQIAVDQF
PCPSPGHEDQ IITWSYCRQC ATPSPTTIMR EETWKMSWGA YLQQCFYPPE IRAGFSCPHD
AFRDQIRYYA HRNLAIRIHN EQIDLFEPVR PSIKLQVRAE TKVVLKNREY DSALAKIYAF
FDSVASRLRT IDVEDVQSDK VSRLNTTVES MLVRAASDRE EITNLLNRTY KLTPVTDVLS
LNVVLRALQD KVVQWDVDFA DIEKAFMPTE KDLRKMTASH LKRLFANQDA PGSLERSALT
GTPSVVSEEH ETKDDVALTH VPSDKQTTII GLSSDTNTDG AEDIATTKFD GDDASITPTA
GILQPMSNPY SRSVRSGSKE TDDDSDSTVF ATHEDLVGKS GGGKTTIEPS TENDTSQFVS
RLPRRAAPAP SIADLVQRFN ESTQLALPKL TRSPERSRSA GGSYRQSPRQ HPRHDISDSD
HSSRNRPKLR RGKTEQPSHR QRDASRPGLM SDGDRSYATN ASRISSSSHL HRSVGESKNN
DYLTVRHSIG SRAPSYTSKV SPRSGRASPK LRYPVVTHVQ SLFDLEEGKP RVAGKGKSPR
RPESDTITPI AGKNAGRRSQ SGTSRVNSIA RHFDRLSREA EKERQKRISI VRGKRARPVS
VTKAKVQVFD NLRDAFRDEF DTDSSEADNE EDELGSDDSL GSADELVSRT KAESFSNKSP
LIRQTGTSSV PITTSPSLLP GPSLSNDDLV TTSPPIAYEA TTSILSDSKS EKSFTDRLKI
ELPSFETSAP LPSHPATPQV HTDTTTADEA LGAVSASQTS DVETSTANEK SSLLKSLSGL
WAFRAADFAP LEYPLSASEH IFADSKVIIR ETEPTSIIAF TLSSKTYRDN SKAWSASRQK
EGRFDTFMPE EAMGTNHPAA WDAVSLEDVD EAARLERGTH MKYDFESGAS TIFCRIFFAE
QFAALRKSCN CEDSFVESLA RCIQFDASGG KSGSAFLKSR DDRFIAKEIT RYEMDALTKF
APAYFDYTRK AFQGQRPTVL AKIYGFFKIG FNNAITGKAM KMNVLIMENL FYERRFAKIY
DLKGSTRNRL IQPTGRINEV LLDENLMEIV YKHPLYLREQ SKRILRTALF NDTLFLSNLN
VMDYSLVVGV DTDKHELVVG IVDYIRTFTW DKKLESWVKD LGAGGKGEPT IVTPKQYKLR
FRTAMERFYF PSVPDRWTIV GPDETQIEED GPGAGMTG
//
