ID A0A2A2JUY6_9BILA Unreviewed; 4878 AA.
AC A0A2A2JUY6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=WR25_12523 {ECO:0000313|EMBL:PAV65430.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV65430.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV65430.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV65430.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:PAV65430.1}.
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DR EMBL; LIAE01010208; PAV65430.1; -; Genomic_DNA.
DR STRING; 2018661.A0A2A2JUY6; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd21370; cwf21_SR140; 1.
DR CDD; cd00053; EGF; 1.
DR CDD; cd15725; FYVE_PIKfyve_Fab1; 1.
DR CDD; cd17300; PIPKc_PIKfyve; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR Gene3D; 3.50.7.10; GroEL; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR Gene3D; 1.10.10.790; Surp module; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR006582; MD_domain.
DR InterPro; IPR013170; mRNA_splic_Cwf21_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_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; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR047488; SR140_cwf21.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR035967; SWAP/Surp_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_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; PTHR47324:SF1; PROTEIN IRG-7; 1.
DR PANTHER; PTHR47324; PROTEIN IRG-7-RELATED; 1.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF01504; PIP5K; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF01805; Surp; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM01115; cwf21; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00604; MD; 3.
DR SMART; SM00330; PIPKc; 1.
DR SMART; SM00582; RPR; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00648; SWAP; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR SUPFAM; SSF109905; Surp module (SWAP domain); 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS51391; CID; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50128; SURP; 1.
DR PROSITE; PS50234; VWFA; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
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:UP000218231};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
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 177..237
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1286..1590
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT DOMAIN 1803..1884
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 1970..2013
FT /note="SURP motif"
FT /evidence="ECO:0000259|PROSITE:PS50128"
FT DOMAIN 2122..2282
FT /note="CID"
FT /evidence="ECO:0000259|PROSITE:PS51391"
FT DOMAIN 3011..3047
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3477..3511
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3829..3953
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 4142..4176
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 4679..4866
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 52..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1704..1734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2074..2124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2305..2350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2369..2479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2494..2608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4591..4672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1712..1726
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2369..2391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2392..2414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2419..2438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2439..2453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4609..4649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 3037..3046
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3501..3510
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 4166..4175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 4878 AA; 546125 MW; 55C8B24D00CEFD37 CRC64;
MTDDPGGSTQ NSTRNGIIFF DRLQDEALDE ASQQTSGVLN GLFGRFWKSD VSTPTTPTAN
QNIPTETTSQ PEFSNPAGPS TIRGGISTIL SVNTESSAPS DAASNSSGSA EFPLNIRKNR
GNSNQNLDSP SNLSIDSNPD NSNSRRFSDK LTTLLKGNKP RLQDYNRSNF RQYWMPDSTG
KECYQCEERF TTFRRRHHCR VCGQIFCSKC CNIHFPGSAL GYLGDLRLCH YCAKMMSQYL
PADELSTAWR KTSNDESTSG GVTSSMNLTS SDSGAATLTS SGTEGIPPIY TPIPPIATVS
AGNLMWAPTD RDNGFNSPQL LRGGRDTGIG SVPGTPKASI PSSGNFGTIP ESQNRRASFS
LAPPTNRLPA MLSVEELLLV QAERTSSSGD SSSDKHLHAH NALQEDDESG PDWLRGIDSG
TQSLGIDGTD KVSLTSEVIE ANEKMTFDEN GLVISEITTI SPSTIVISRN APIDVDTNAA
FAKTAERLLD YLFEREQISD KRWKEIVLNL ADKIANRLTV DVQKRDSMNI LDYVHIKKLH
VDVEEPKSET IWGVVCSKNL QHKEAHLEEP RQASIMIVAG SIEYERIQGK LSSIEPIMFQ
EAEYLAKQVD RILARRPTLL LVEGGVSRIA AELLKRNSVK LAVNVKSTVL QRVARCTGAD
ILPSSDAQLI QQSIGFCPQF CQKSIKLADG SDKILLILDK CPDDRNCSVI LKGNDAVELK
SIKKILQMLI LSSYSSRLEK EFLNLFGVKL AYSESPCAAC TDRLANIENK EEKSPFEEAL
HRCVLSSSPF IEYEPPFLET PRGRACSLLP YFKQPLYRFG TKEDFEQAKA EAKLQIDRQM
ETTKAGKLPS EPREPFAKSS CVAPTDFKEV ASFRALSGLF FKRRMKAAQE EKERIRKKQN
EENMSSGDGT KRQDVLDPSC HQRVAVLFGS FSPKSPNAPY FCVRPWVVSM QFYGDHDMTL
GEFLTRFCFN KSYECPSSNC EVPMLDHSRK LVFGRVCIEV TTQTVVQSGE ENNQSVNGPI
LTWYYCPSCK LSSNVMTMSP DIWHLSFGRY LDYLSNSSYS TGSLINTAVH SQQQQCTHCF
FHETTHFFSM NNFVTTFKVS PIRPYHVQFS PILCTILPTR KAKQDYLNDL LRLSDLFESL
AATASERLQK LSDDHDEYVE KFHSELVNLV EKTRQIVGEK KPFIDYLQAS ENEELLTNDA
LAIKSVETRL QLREVIYDLI SAWNEQCGVL SAHMRALKNS KDETQPGAEM PEISIEKLDD
PFPAYLHLGL RLKARCGVTV RDIVDYRGNY KPDIGSIIAY ALSSADYEEN RRKQREAAGG
EDIALNLNSA SVNTENEASQ AAEHIEVEFQ DTQASYYVKA YYGERFRLLR KLLFPEGEEA
FIRSLSETQF WTPQGGKSGS FFYKTCDHRF IIKTMSNFEV RSFVKFAPNY FEYVKTAVTE
HKLTTLCKVF GVFKVGFKNK TSTYKGDILV MEYLFYNQNV NQVWDLKGSL RNRHQLYVYP
HAKAALNQAI SNDSHFLSAQ YVMDYSLLVG LDEKNGQLIF GIVDYMRTYT LDKKLESWVK
IVAIPGAHLP TILSPEMYCT RFSEAIDNYF PVVPDQWTGK LRTQHAMSRN KKKEQEEEAM
LKEQLSNFER DFGGSAPLPT VGKTFIRVDI VNANQSVGKD VKPELYKPTP TISLPKDKLP
VSASSFEDAK KLAAERARRY MEEAMKGKGG PAPTVIPPPT KAPAVRPPKP GSAAAVKDTK
KISQLESFKM ELQKIQEERD KRKGIRDQLV KGGIDAASVD RIAPILDKPY LGGGEFDDDP
FTTNLYVGNL AKDVTMNDIY DTFGSYGPLA SAKILYPRNE EENCRQFLCG FVAYMSRVDV
DRAMTHLPGV VINDETLKMS FAKPVPIPVQ PFYIPPPLQE LTIPDPPTGL PFNAMPLLKD
LNSFVDKYGE LPPLMKPLPD DKDLVHDYYQ MLKNATVRVV IPTDSHLLTI IHRTVEFVVK
EGPLFEAIIM SHEAQNPMFR FLYDNFHPAH VYYRWRIYSI MNGDTLTEWR MNKFRIFENG
SWWQPPVPMT DLLRQMPESL YYFACHNMNQ DKYFPNRRDQ RYDSRKRSRS ASDDEGQRRQ
DQKRLSSKEG AEAEQRKKKK YLSSSEREAF EDMLRGLTPE KDRVGDAMVW CCEHATCAKE
ICECIYESLT IDETPLHKKI ARLYLISDIL ANCAQRGVRD VFYFRQYFGD LLEQAIFCYF
ILIFSSFQIF EALGKAMDRI EARLKKEQFK QRIMACFSAW EDETIYPNDV LIKCQNIFLG
LVMPSKSESE DISLLKKDLL TSKSDSEDED IDGAPIEEDD VPMASLTSSA SKSKSKEATV
ESEDDDDIDG VPLESAHLLE ERKEKALKAN IFEDESDSDD ENAKRQVGDS KRNSNKLTFK
PAFENTSKKS ALSQEPLIRS KWDEPDDKSM EISGRRKDDG ATASSSQNSK ANDSDTDGEI
DDLNDPASIL ANASAEEERR KMMREIEIKV MALQDELEAS NDKDIKKKVA DYRKKEMDKI
DEKLVKKIKK REEKKKDKEK DNKEKEKKKD KEKESSNKER SRRDDERRRS RSRDRDRASR
TSRDGDRDRD RRRERKTDPG ESALARRIGE EDNWRGELPV TPSYFNKMRP VILLLWGFFI
SGFANQQYSH QNDVTTNPMA TIKAILKTWD PSKPIKFVPD HVAMEYEHQE AVYHRRKREA
GFEEEPANAI PHVRAALPTS RACQIPGYTG EYCEFPICSE QNMYIPDDPA NSADGASIDA
AVLLNCSQKY VTMVDNTMYW ITYEIESDPA LNPSFYVMGE DGTVYSPDQV ERTASYYRGF
FNNLDPGQYT IVPSADLPQS VCILTQKART DMTFVGGFVS GQNAERNDFP IKDYAYFETN
SVVTVHANRL RIPGDLRAIS IHGGDNFLIR PKLLRPRYNC SYEYIYESFW CPNDRGGSTQ
SYYLQVEGTT HMGYHFRRIQ PFRCVLPPVT SPTPTQPPTP SPTPVSSCDN NGILINPLEG
DPYCYCIGLY GGPTCSTPLC QNNGWLPNPA TDTRCQCPDG FSGIHCQNVY CSDNAGNEFN
AENPSFILVI RTRSQLSDVI GQVLNSTDAL MNFMNFAPTY IADYILVLFN NDKLLVNERY
SNYGDMQTRL TQAMHSEPSD GGCTDSVFGA IATALSQYPN NKSPLYVFTD GGPDDSAIMN
DVLHLQSYWR SPIHLFVVQP NLADGCSINP EDPGYRDMLS VSEKASGTVY WFPQQNRARI
GEFYLQHALH TFYRSQLMLS NDIRICSNQA LYKPISVDAD IDRMVITATG TNLTLMITDP
MANRVTFDLV YNDGTNYIWQ KHGVLIGQWF ITLMSSTPQS SCSFKVYQKN FDNAISAIPD
FDMFFTYTEA IMSDGFQMQP IYGWNAAPVF HVNNIAAFAM DTSTIFANLQ IYASRNGNQT
EVYASNGMFR DACSFHFYFN AFTCQVPEET LYFNLFVRDR LGFTLQRAGT MFCSRINVTP
PPSHICQNGG VMNPSNNTCF CYPGYTGTYC QNIQCYNGGT PQGTQCACVQ SWTGQFCETP
RCIQQGFNPA DLRYGVDMVF AVELTANGLA SLAMLDKNIE EVIRDVVFQD FRWIRQFVLV
GFNSTWGGVL ATAPAFNPSA VVNTLHNLTQ SVPTDKGCLV QLWRALDAAV FQRDTPPGSF
IEVFQTTPEN DNDTFNLGAF YEWTRTGQLT VYGFLSALPS WQPNGLACNA TYDQFNTLFG
VAASARGMTY VMQPGEIQYA TRAIPLQFSN GLVYGQQQDD CTGAPLYAYF PVDAYAQTLI
VNAWGANMEV HLYTGAGDEW PYDTVWSDDW LDYKMIEARR PCDEDWDQVG QYCIKFVGGT
DALNWTDAQA YCRSAGGFLV DDLTSDKNTY LYQAAFKNQF WMGLFNNGSG WMWDRGATQP
ANLDQDQQFW KGGGGPPPYD ANNPCVYLDG AAGDSGQVWT PDSCATQRNF VCQKHRYDQD
YHPFSLDADL LPPGYWYVTI KTSPNNTSSG DWAGCAASVR VQSSLQIVTG FVTDISSDEL
LPDPVQDSVV NRVSTFVYSE EHEAKVPIMT DAILVDAYNL TFYNALKYQM RRNCNKPWIT
QTFACPNGDN PGNEFAVAHK GEDERGYPFS RITFGHCSPE ELSCGNGGVR WNGTCVCDDF
WTGSFCTVPI CVNGGTRDPT DRFCNCPAGY TGRNCEFAFC TPRQPDTYTF DNKTLLFIVE
TTNNNKAAAQ SLADNIPAII GNATANNPYW FQNYALVTFD STGVKSQNFA LTDANSLQSA
LNTQIGQISD NGNCNMALFG VLQTALSAQN NIAYPSSEVI MVTMAGVSDA NNRIPSTQEV
SSSRAKLHYV YINGTCGQAP SNDSMNYLAR LAYGSSGNVL VVIPENVGPL FTSYVPTLYG
ASTLTHPTAH LGFTCGAGVW YVEVDRNTTQ IYATSSSEYG SLTAVDPLNQ MLVPNVLFND
GNQKVYSVDV NSIPGIYKFS LSSPGYCFAH IYSAGGAKVY PKFAQVTADD PTGTHIDGTF
TNPYSNVSTV INIHMMGRLF TRGYLQYVDI FDPDTLTLIL RSELYERFDC AYQFYSDPFM
CNSEMLGIFI YGVDEYNQQF RRQEIAYCLN SQPPMSTLSP PPPQSSSNTP PQGQTTQTPN
PGQTTQTPNP GQTTQTPNPG QTSQTPPQGQ TSATPPPQTS PGTAPPASTT FGPNSMAVDV
VFMVDMGQEA NQTYQDFSQF MKTVTIPWNI DASGARTRVA LTAVYADIAI NTNALNSMGS
RASFMGALDT FFRNWPDTNP GQNLTAGLTL VSSDDYLAPS NGYRKDIKNH VVVYLTATDN
INGDPTAIAQ NVRSTNLYGV LVIGYGGGVS NQAVLKNVAG KDSCAAFPAD VHALNTDTVT
WVQNAVWAAA SGGANYCN
//