ID A0A1Y2DUM5_9PEZI Unreviewed; 1607 AA.
AC A0A1Y2DUM5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032};
DE EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032};
GN ORFNames=BCR38DRAFT_393526 {ECO:0000313|EMBL:ORY62973.1};
OS Pseudomassariella vexata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY62973.1, ECO:0000313|Proteomes:UP000193689};
RN [1] {ECO:0000313|EMBL:ORY62973.1, ECO:0000313|Proteomes:UP000193689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY62973.1,
RC ECO:0000313|Proteomes:UP000193689};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC IP6K kinases to synthesize the diphosphate group-containing inositol
CC pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-
CC diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-
CC InsP4, also respectively called InsP7 and InsP8, may regulate a variety
CC of cellular processes, including apoptosis, vesicle trafficking,
CC cytoskeletal dynamics, and exocytosis. Phosphorylates inositol
CC hexakisphosphate (InsP6). {ECO:0000256|RuleBase:RU365032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-
CC inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946,
CC ChEBI:CHEBI:456216; EC=2.7.4.24;
CC Evidence={ECO:0000256|RuleBase:RU365032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
CC + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate
CC + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216;
CC EC=2.7.4.24; Evidence={ECO:0000256|RuleBase:RU365032};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|RuleBase:RU365032}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC subfamily. {ECO:0000256|ARBA:ARBA00005609,
CC ECO:0000256|RuleBase:RU365032}.
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:ORY62973.1}.
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DR EMBL; MCFJ01000008; ORY62973.1; -; Genomic_DNA.
DR STRING; 1141098.A0A1Y2DUM5; -.
DR InParanoid; A0A1Y2DUM5; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000193689; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IEA:InterPro.
DR GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.11950; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR037446; His_Pase_VIP1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR040557; VIP1_N.
DR PANTHER; PTHR12750; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1.
DR PANTHER; PTHR12750:SF9; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF18086; PPIP5K2_N; 1.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365032};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU365032};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU365032};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365032};
KW Reference proteome {ECO:0000313|Proteomes:UP000193689};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 314..401
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 536..627
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1063..1090
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 192..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1607 AA; 177519 MW; 34422CD37DC0D22F CRC64;
MQSLGSPEIE NNSRRGSGQR RLSTRSASHP HTLSNSSVSS SVASSIASRK SRQAEPVGTS
DISIEPASLS MPPPTNLLKS PRSSFLHSRR ESTNSVSWSA ISDYQRSAAD DLAIDDSEST
PKLLPGSANL HDTADRQLPE PALAVSQYSQ SSFLDEGRRT MDHEGKRMSV SSLYSLSSAR
GVPSSAASIS AVSVNGSDSG NRSASGVMAS SKGLGPPSGQ QSEAELTTVT VTTSSSAQNN
QLTPRDPNHS SNLDLVKRNP PKSDANSRPQ PTRSRSMAKR RFSGSTATSS HSPSSERGPY
KEKEEVKPAP YGIIGVCALD SKARSKPSRN ILNKMVGKGD FDVVVFGDKV ILDEEVENWP
MCDYLISFYS DGFPLEKAIA YVKARKPFCV NDVPMQKILW DRRLCLRILE KINVPTPQRL
EVNRDGGSTL LTPDIAKHIK DVSGISLEPT DPNRTIYPRK VELLDDDDIL SVDGALLKKP
FVEKPTSGED HNIIIYFPKS SGGGARKLFR KIGNKSSEYI EDLTVPRAIT EPESSYIYEK
FMRVENAEDV KAYTVGPDYC HAETRKSPVV DGIVRRNTHG KEIRYVTALN AEEKEIAKRI
SNTFGQRVCG FDFLRAEGKS YVIDVNGWSF VKDNDDYYNH CAGILKNMFI KEKTRRGGVT
PPMPSPTISD SVDPLGKAAT VAKEKESQAS TLHPNQAKSP SSVGSALSKS NSAQDTKQRE
DKSPGTASPS KSDAGTQSIV SRLQSGLMSP LANLTGDAAA KILPETTPPT LPVTPLAEDQ
LTLNSQQDES TPPPPPPKHS WKLKGLVSVI RHADRTPKQK YKYTFHTQPF IDLLKGHQEE
VLLIGEAALA SVLAAVEMAL KEDEEDRAKL KSLRNVLVKK GGWAGTKVQI KPMFRKKNTD
GTTSTATPKV TEGVKLDTDG AKPSVETSEP KAATDEPPVK TEEMNVEDTA SGGEEKTRRG
PKRSDSMSGV TMSKFTAAEN QLVLDKLQLI VKWGGESTHS ARHQAIELAQ NMRNDYLLLN
KEVLDQACVY SSSERRVTAT AQIWTSTFLD MQGEPPPDFI KVRKDLLDDS NAAKDEMDKV
KKKLKGLLRK GNERPSQFAW PENMAEPSEV QNNVVTLMKF HRQVMQHNYN KLYSGAVNSL
NAISNPSVEK LNGEGSTTSM SSVISQANAV NSIQTRWCCG EDAELFRERW EKLFGEFCDH
DKVDPSKISE LYDTMKFDAL HNRAFLEWVF TPPKHMLEEE YGIVIGRDNK ITPKDPEVDD
NKSDQSQVVS SPPNERSDKS DKSDKGERPE GHKTVKRLFK RRSWMKDRHS RELAPPEQYF
HLHKGSGPTK AKTDARFEPL RELYKLAKVL FDFICPQEYG ISDSEKLEIG LLTSLPLLKE
IVQALEDMQA SDEAKSFFYF TKESHIYTLL NCILEGGIET KISRATIPEL DYLSQICFEL
YESEVKAPEA CPDQPPTFAY SIRITISPGC HIYDPLDIQL DSRHCIGCAP RRSLTPHGDW
KQVIETLRAK FHQVKLPKTF LAVNLSEAFS FQEKERHNSE VDALEMKKIE RTPVTEKLVG
EVRNNDGSAV ASAPAVTDTA INGEGGQRAV AEAVTEQQAA DKSAQQI
//
