ID F0WVT6_9STRA Unreviewed; 1367 AA.
AC F0WVT6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Phosphatidylinositol kinase putative {ECO:0000313|EMBL:CCA25536.1};
GN Name=AlNc14C304G10417 {ECO:0000313|EMBL:CCA25536.1};
GN ORFNames=ALNC14_116800 {ECO:0000313|EMBL:CCA25536.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA25536.1};
RN [1] {ECO:0000313|EMBL:CCA25536.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA25536.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00008941}.
CC -!- SIMILARITY: Belongs to the peroxidase family.
CC {ECO:0000256|RuleBase:RU004241}.
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DR EMBL; FR824349; CCA25536.1; -; Genomic_DNA.
DR EnsemblProtists; CCA25536; CCA25536; ALNC14_116800.
DR HOGENOM; CLU_256613_0_0_1; -.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd14947; NBR1_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032350; N_BRCA1_central.
DR InterPro; IPR044571; P4KG1-8.
DR InterPro; IPR002207; Peroxidase_I.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR PANTHER; PTHR45800; PHOSPHATIDYLINOSITOL 4-KINASE GAMMA; 1.
DR PANTHER; PTHR45800:SF11; PI3K_PI4K CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF16158; N_BRCA1_IG; 1.
DR Pfam; PF00141; peroxidase; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR PRINTS; PR00459; ASPEROXIDASE.
DR SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:CCA25536.1};
KW Transferase {ECO:0000313|EMBL:CCA25536.1}.
FT DOMAIN 907..1193
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1236..1367
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1367 AA; 155484 MW; 32D0B0BF5C78DACC CRC64;
MEKAISKSAH PTHELKQFQK SESRQSRRSF TLPLHKNSKV MENQREGNSG TKVAKVRCIK
VDARLLRPTR ASIAGRRNRF TGTEKARKMQ TRSTKKIETK TSHRKLTIPK SPNFHYHPQN
AVKKSHLSMT SKELLEIRAL WKRVDKQKKK NQRYHQSIVS FVQIPASANA TDKERFVQTI
RSSGSIGIPT VRRPKLTVPI GFDLQIDKRF AHRQKKASLV CERIEEEIKT KPKQIAGETE
ISNEAENKVR LSNQNLDHFD QKEATSQKND TKRSDIPMAT LKISWREKND MRRVKVYAVN
KTLNDYDSRD IKDWNSLKLD NLKEYICHVS QNIGISPSAL QIYYLDDEEE KICVTNDQEL
EEGLRLSREI AVFNGRQESD SICRIIVEIR NREEKITSNE REAHLEKSRI LALLTEMNNL
LVTWKAGPEF YQLESDLASI LNEEGTQQAL LQIFMDPELS TYLSHFLTQV KNGQNIITEM
RNAENHRPLD SLASIVITKC PQALARVTRL TDYLKYGPSN SCAYLSSSDF FENVTKKGAE
EKEACFAIFQ DDVTCPDGTV LPPKYPFDKI WKIRNPGPTR WPQGVRLLCV GGDRLQAPDN
VLVPHIAPGN SIEICIRMIA PDQVGRYTGY WRLSTQENVR FGQRIWVDIN VIDSNMSLSN
CASLTPKLFY PRVTPKQFDD TSVNVVSDIK AETRAEKVKW KTEQCALCEM GFIDSTLGAT
DGDNFYAYII YLNSQLFENK SNKSAKKLGA CEGIQQLTLH KVPKASLCLL LLQKVHPQSV
KMAIFQRKMS SAQGRPECPS HNTLVLDSSA GQPVELHSLS MQRNRCITNH SLFSLRFTKK
PVLLLRTSIQ WRVPSLRYSD TKVVHPSPSI VISPFKLDLH PVESVPEASE IDVFETNLTS
QVAKIEQVGM EMTSEGCGGV YFVYDKNQRE PNKWLAVFKP RDEEYMAAHN PRGYVQEDSI
VGKSRHPIQK GLFIGEGAIR ERAAYLLDAA YGNFSGVPVT EITKLKLDGH LKEGSLQQFV
SSSSSAEDMG TLRFSVSEVH KIGILDLRLF NTDRHAGNVL LSTNASEMNT FLMTPIDHGM
CLPSFEHLDG ACFDWMSWPQ SRLPFLPAEK EHIASIDTQK DASILRNLRI REECITTMRL
STFVLQQCAT LDLSLFDIAK IVHRSGNRTE PCLLETLVSA YMKDYTEEDT SSRDFCDTLV
EKVTQKLAQT LAEVPKKRKP RSLFIKNLRV NDKGCPVKTA EHVRDVFSRL GFNDRETVAL
IGAHAVGRAH PELSGFSGPW TKTERTFSNQ YFKNLLQVEW KPTEGKSPTQ FDNPSKTLMM
LPSDMVLIQD KEFRPFVELY AQDQDLFFKD FAAAFQKVTE NGVSFEN
//
