ID A0A094HJA7_9PEZI Unreviewed; 2512 AA.
AC A0A094HJA7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=V502_06548 {ECO:0000313|EMBL:KFZ13544.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ13544.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ13544.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFZ13544.1}.
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DR EMBL; JPKE01002417; KFZ13544.1; -; Genomic_DNA.
DR STRING; 1420915.A0A094HJA7; -.
DR HOGENOM; CLU_000480_0_0_1; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000029308; Unassembled WGS sequence.
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; 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; 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; 2.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000029308};
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 446..505
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 2162..2493
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1672..1698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1774..1863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1965..1990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2003..2052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2064..2096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1774..1797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2011..2049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2066..2092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2512 AA; 278632 MW; 7CD482E97DDE568B CRC64;
MSSQDSPQNS SSSKMAANLP SGLRSRRDSL ASLGGSSQAD KEHLTQALDA IHNTASHSET
LTTFNEFASP PASSSSVESK GIAGELMQNG LSGLYSRFRG VVGGAKDKSH QPVAKNSLDS
RDRPLTQGQN FSTNTGNSSA PAIAREELNV NDSTGEVVSD SPLGHAPVVP ASTTPSGSSS
QLYQSSKPST QFTPTTAKAL LSSRPGMTSR SESTASPAAA PTTTPVNIVA SEDRESAADS
PKEPGESDSV NHHILRRTNH VPLRAHPFED SDGFDIKHPD DPNPELNHGP GGLPLSPGLI
TSLGGGHEIP IIEGPDDTSA TSSRRSAKSS LRPLDAHAAL SANHTSQKSN HPTAIDRFTQ
SHLPGYQPSR ASSTERSATE TSPVNTSNHN SVDHGLFYAD ESHHSRTAGA SRTPGSTLNE
GEPGVVNARL EQMRKQVLSK EFWMADEICK ECFLCGDPFT AFRRKHHCRT CGCIFDSKCT
SIISGERFGV QGTLRVCRTC LDIINRRHDS SGSDDESGDD TFLPASFFQS HQTRLNSMKD
DRASEEGPDG SFTGRSLNGD SVGPITTPMM AIPATRRIGD SENRRSAILE IDAPQLGRPS
SSRSLKALSL SRPLSSGQKA NQAKHNFLGR FRSTAAERPP FHSNPAADEI KKRSRLPALH
DDNIIDPDLA PYMSDDESSG DEQMSIFTAL NGNAGVSTSY ENEKSAFGSL LNTAKKHRSR
AGEKSISGMS FSGRPVEDNS WAGSVGHSRP NRRRNLSTSS NNVHIARGSP RQNKPGALTY
NYGELSEETI VPRDDPLEPS SHGASKVTRS ASMRNAKAPA VELNNASLHH VRRLLRQLLQ
DACVENVASW EKALIPILLQ CTDDVNPDVR RGDDIDIRHY VKLKKIPGGK PGDTSYVSGV
VFTKNLALKS MARSISQPRI VIISFPIEYQ RHQQHFMSLE PVIAQEKDFL RNMVNRIASL
RPHVVLIQSH ISGLALQYLA EANIAVAYNV KQSVIEAVSR FAQTEIISSI DMVALKPVHV
GKSAGFDVKT YVHKDIPGTR KTCIYISGCP KELGCTIVLR GASMAVLSTM KRITEFMVYV
VYNLKLETCL MRDEFVLIPE ITEDYGTLTL GSKSAPEKID SSNSSAEPIQ KPVQDARKDT
NSTKSVDGAT ARHNESQEPS GEPGEPGEPR DNDSQPSFPQ TTINTTAETP TQGSHLDMRP
KLISAHESHV HDTQVLPEDI PMPTFYSDMV AKHQTKILSA SPFVKFTQPY LLMNAREQER
RLVYLKRLRD QDTFEDQTDV EKADPQRFQL IHPEMVHETV RGAPRQIMEV LHAVHDAEYD
KALHNYQTQK RQWENYIQGN LNLFDPYSHQ NIVVLYTVVC TATTVPCAGP DLTAMAFYNE
HETSHDFFPD CTLGQYVEDL CLTVDAVCAS NGCERKMSEH HRTYVHGEAR ITVFVEASPC
KLNGLQDSIL MWSYCKICKK ETQVMPMSES TWKYSFGKYL ELSFWSTELR LRAGFCPHDL
HRNHLRYFGF RNVTMRIHYD PIDLLEIVVP RTRITWKVDN DLRLKNDLFT KTEDRWNRFM
ASVKSRIKGI NIDSVVSDKV EACIAEVETL SKRAQDEHAS LLNKLQEKYM ESKYYEIIPM
NRAIRAMQER VAEWDTAFTD FDRNFFPSEK DIRRLAALQL KNLFLDRDAS TTHLASSETP
DQSQGIYERQ PDEGQSNKVT NLVHDNNDLP PIEFRGTLAP LVEDVASIDD ATLEVPRSQS
TEELNVTKSQ DTVHHLDLAI PWVATADDAP AINSSADQAD SQLPSSESKT VANSDDVLAS
QPEPHIPEVD IAKNPQQVRK ESQADLREGA ATNLEPSGIP RPSDRNSGRR SGLAVSPPIL
RTQSQPAVTL RRTQPATLRA FNIAAKEKTN AVGIPLDSTI PLGAFPVPGE QTKDKRLSDR
LGLGSLKSSR KPGHSLIPRS IHSKGRETKV STLAKHFEQL SREFEKERLR DKKQRAAKVT
QSRAFPKASS KPIVEVYKDV NEAVEERGPS EEGSQPTNQS SSNIETTGPR DGISNANIKS
KQNAHNDPAQ IDTDVVGEDT VTEIETDDNQ QTLSQTASDD ETAASDTEQS FLEDMPSIKD
ITESLGVSET ISEVDLPKHE KTSLMKMLTN FWAERSASGW TQLEYPLHAT DHVFVDSDVI
VREDEPSSLI AFSLSSQDYI EKLHAIRQQG QTNMPEKTSG QERYNSAEAD VETSLLRATG
THLKYQFAEG SAKMLCKIFY AEQFDAVRRK CGASDRIVES LSRCLKWDSK GGKTKSVFLK
TLDERLVLKS LSPVETQAFL RFAPAYFNIM AEALFHELPS VIAKMLGFYQ IIIKNPVTGT
EIKWDVLVME NLFYDRAPTR IFDLKGSMRN RKIQSTGEQN EVLLDENMVE FIYESPLFAR
EHSKKLLKAS VWNDTLFLAR QDVMDYSLMV AVDEARKELV VGIIDCIRTY TWDKKLESWI
KDRGFAGGGR NRPTVTSPKE YKSRFREAMD RYVLQAPNCW HHFGGYDARV SK
//
