ID B2WAV1_PYRTR Unreviewed; 2578 AA.
AC B2WAV1;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Phosphatidylinositol-4-phosphate 5-kinase fab1 (PtdIns(4)P-5-kinase) {ECO:0000313|EMBL:EDU50333.1};
GN ORFNames=PTRG_07414 {ECO:0000313|EMBL:EDU50333.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU50333.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(6)-D-ribulosyl-L-lysyl-[protein] = ADP + H(+) + N(6)-
CC (3-O-phospho-D-ribulosyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:48432,
CC Rhea:RHEA-COMP:12103, Rhea:RHEA-COMP:12104, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:90418, ChEBI:CHEBI:90420,
CC ChEBI:CHEBI:456216; EC=2.7.1.172;
CC Evidence={ECO:0000256|ARBA:ARBA00001616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48433;
CC Evidence={ECO:0000256|ARBA:ARBA00001616};
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DR EMBL; DS231621; EDU50333.1; -; Genomic_DNA.
DR RefSeq; XP_001937746.1; XM_001937711.1.
DR STRING; 426418.B2WAV1; -.
DR EnsemblFungi; EDU50333; EDU50333; PTRG_07414.
DR GeneID; 6345687; -.
DR eggNOG; KOG0230; Eukaryota.
DR eggNOG; KOG3021; Eukaryota.
DR HOGENOM; CLU_000480_0_0_1; -.
DR InParanoid; B2WAV1; -.
DR OMA; QEKVVEW; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102193; F:protein-ribulosamine 3-kinase activity; IEA:UniProtKB-EC.
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; 3.90.1200.10; -; 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; IPR016477; Fructo-/Ketosamine-3-kinase.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR011009; Kinase-like_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; PF03881; Fructosamin_kin; 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; SSF56112; Protein kinase-like (PK-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:UP000001471};
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 386..440
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1975..2293
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 25..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1600..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1736..1760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1818..1839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1873..1908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..549
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1548..1580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1653..1670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1739..1756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1873..1894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2578 AA; 288002 MW; F9703968C3AF5017 CRC64;
MARDSRRGSL QPSLHQMHAV ASRSDTLTTF DDFTVPPAPS VVGEPKGIEL VQGGFSGLYS
RLRASVGGGS REQAQDGSGN GVSRTGTPPA AGNRNSPGGT STSSPQLVAL PPSRLQSPAT
ATFPETLPPS RDSNISSTTF SSKASRSRPS ISASIEPGPA KQDEVYIKSP VSIHSKNHST
STIDLPRSNT PRDSALGSQK VDSPRFSREN AAPRQQGDFD LVGQESDDTD DDDDLGGAIG
QASTGDSKTG SDTPRESLSR VSSRTDSQYQ PNRSVPNREL PENSAEGTQP NRVAVNQSTT
HAPEPQRPPL VHVGPSHLPG FRPSRASSSD GLSSVVTAST IRMPTVPPIE EIQRQVQAAP
AANTMSRSTF TQMRRKILDR EFWMRDENAK ACFNCGDAFT TFRRKHHCRT CGQIFDSKCT
SIVSGKMFGQ QSNLKVCKPC EGIIYGHDDD SSDYTDDGDQ GSIYDPGDTA QYSDQEEADH
VESDHTKIGT PTISIPMSRK IGNEKKRRPH VIEVGPQTLA RPSSSRSLRS LGGRPRSSSH
KRHPSKHQHM RNVKHDDRAP FHQYHDNSRS QPSLSAFHHD NIIDPDLAPF MSDDGSSEEE
HPSIFATLKD DPTATANLES ERGGLGGLLA AMRKGKSRPG DRSVFGTSHA RDADNVSIAS
RNGNRPSRRR NLSVSSMTHR ASPRRSKSNS LLRPYTGYGA SGPGTPQLQP SPSPTPSGSR
ITRSASMQGM TPKVELNKAS LDHARKLLIQ MLHDAGVSHA SNWERALIPI LRQCTDDVNP
DVDRGDDIDV RNYIKLKKIP GGKPKDTAYV SGVVFTKNVA LRSMPRSIPN PRIVIITFAI
EYARHQAHFM SLEPVIAQER EYLRNLVSRI AALEPHVLLV QRNVAGLALE FLEKEGIAVV
YNVKPTVLNA VARCTNSKMI SSVDKLATDP SHLGSCGSFD VKTYVHKNAR KTYIFLSGCQ
KELGCTIVLR GAESQELVKL KRVTEFMTYV VYNLRLETCL MRDEFIDTPT TSIIGTLASS
QNEQDAAQPQ NTADAVQRTA DGDDTQTNDA APSYYSDMVE NHRTKILSSS PFVKFMQPYL
LEQARQYEAK LGHLKKLKNQ YTADDQEDEK PGEVGQKFEL VQPEMVHTVV EKASKQVREF
LSAVHASEYD KAMHQYMTQK RQWEQYLSGN TDLYDPFNHQ KIAVLYSVVN TTTSTPCIGP
EIIALGFYQE HDYDDGFTPD CTLGQYVEDL CTSAGVACEV GNCDRRMLDH SRQYVHGEGQ
MTVIVQKHPP KLKGMYQTIL MWSCCRVCGQ ETQTFPMSEW SWRYSFAKYL ELTFWSTKLH
PRAGICPHDI HKDHVRYFGY NNVALRIQYD PVPMYEVIAP KPNVTWKVDS DLRLKNSQYL
MIEEKLDCFM NSLRARIQGI HVEDVIPEKV DLCRKEVDIL LKRTNEEHEW LKAKLQDKYM
SSKYYEIIPM NRAIRAIQEK AIAWDVTFME FEQQFFPSER DIRRYANMQL KRFLERDEST
SSLASVDEGT ESGADDSYLD EKDDSIALSP RPSNMSPEMA RDMLSSVVKE ESSASDQPAD
GSTTSPEHKT PTSPRFSSEL PIQTPREALE RDDIRHLDLA IPSNFPDSPT VTTEDSETPT
GASDPNKFDE GSPTPTSYPK VNPIDKSLAE AIENMPTSPS TLQSGPNPNV ESKIPRLVDN
ARREPVQRPA TLVRTQSQPG NIAKHISPSV FNSGPAALKP NTGDTSRAFE RMTERLGLGL
STPKQSKNSS RIPRSIPYKS PNKVSKIAQH FEQLSREFQN QRMRERRNDR ARQVRAFPLA
SSKPVVEVYK NVHDAVQENE DSDEDLPGGS PTHESLDHSM LDDSTLTEQT DDMTIASQSP
VEERQTKDLT AELPCSDQSP EIPSQFQPDN DNDISDADIT PEDIPLPDSL ASSQLLNLSD
SQLENSLELP KHEKNTLLKI LTSFWSERSA SGWTPLEYPF SQIEHVWENS DIIIREDEPS
SIIALALSCP DYVAKRHSFR EDNSASGHLE TFEESIERNL LHEENHNIRY SFTNRGVKAH
CKIFYAQSFD ALRRKCGVAE RFVESLSRCS KWDSKGGKSK SIFLKTLDDR FVLKSLSPVE
VQAFFKFGPN YFAFTHQNLF KSLPSVIAKM FGLFQVQIKT PTGRDFDWYM LVMENLFYDR
EPNRRYDLKG SMRNRKIQAT GERDEVLLDE NLVDIIYSET PIFVREHTKK LLKASVFNDT
LFLSQNNVMD YSLMAGFDDT NREIIVGIID CIRTYTWDKK LESWIKDRGK NKPTITSPRD
YRNRFRIAME KYILQAPNCW HQFSGRMTNI SSVGGGSSFA STSKIVSQLD DGTQKAFFMK
TGSGKEAEVM FEGRSGSKSG KAQSLAAKLA KLHTTPAPNP EGYDKPMFGF PATTCCGDTP
QDNSYKESWA DFYAENRLRF IVRYAEQRGR RDGEVRKLVE RTASEVVPRL IGDAHLNNGK
GVTPVVVHGD LWSGNASVGV IGSDKGEPED VVYDSSACYA HSEFELGIMK MFGGFGGSFL
KEYHEICPKT EPVEEYADRV KLYELYHHLN HYAMFGGSYR SGAVGIMNNL IRKYGGDG
//
