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Database: UniProt
Entry: L7Y3K5_9VIRU
LinkDB: L7Y3K5_9VIRU
Original site: L7Y3K5_9VIRU 
ID   L7Y3K5_9VIRU            Unreviewed;       690 AA.
AC   L7Y3K5;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Putative phosphatidylinositol kinase {ECO:0000313|EMBL:AGD92687.1};
GN   ORFNames=LBA_00769 {ECO:0000313|EMBL:AGD92687.1};
OS   Megavirus lba.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Megamimivirinae; Megavirus; Megavirus chilense.
OX   NCBI_TaxID=1235314 {ECO:0000313|EMBL:AGD92687.1, ECO:0000313|Proteomes:UP000236749};
RN   [1] {ECO:0000313|EMBL:AGD92687.1, ECO:0000313|Proteomes:UP000236749}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LBA111 {ECO:0000313|EMBL:AGD92687.1};
RX   PubMed=23709652;
RA   Saadi H., Pagnier I., Colson P., Cherif J.K., Beji M., Boughalmi M.,
RA   Azza S., Armstrong N., Robert C., Fournous G., La Scola B., Raoult D.;
RT   "First isolation of Mimivirus in a patient with pneumonia.";
RL   Clin. Infect. Dis. 57:E127-E134(2013).
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DR   EMBL; JX885207; AGD92687.1; -; Genomic_DNA.
DR   Proteomes; UP000236749; Genome.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR015433; PI_Kinase.
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; PTHR10048:SF7; PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT TYPE 3; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AGD92687.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transferase {ECO:0000313|EMBL:AGD92687.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          21..99
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          391..668
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   690 AA;  80044 MW;  0ED71C2D44B6BD2E CRC64;
     MSEKTTTSIV IGNKNNIWVE DHRVSSCHGC NATFGAFLRK HHCRSCGNIF CYKCAGYSIV
     IPDFLDRPDP ADYWNMSYYI TSLKKNKKRV CKSCHTLIIN KTKIYDKIAN ILENPKPIDE
     IYELSNSYTD VKEHYLNHLR NIQYYLPNHV YTTIDKNLLN INSKYFCKHS KYIVHLIKCM
     DWKPIKSTNI QISSYQKSGQ YVESIQKANL KIIVDVVNSA KNMNCNKLCC TRTCNEQLSF
     DDCICVLYSN AYDLPDALIE YMFNIINNTP ESIILCHVTF FVNIIKNNYH NISLQNLIYK
     VISKSNKIIY HTFWLLNNAK EMANMQHVSN INRFIRLIDK ELVNKMDREY RFYVGLIDNL
     ENPQRYLTDV FERCDPISLP FDPEIKLFKA KINQIEIKSS YTKPVIIPFE TSHGDIKILF
     KKECVMNDLV VQNLMYLCDI IIKENMDDTE SNVNFGLVSY HIMPLTNNSG MIQIIENAET
     IYSIINSKTS IMQHIINKNE HKTVSTVSSI IDKYMCSLVS YTLHSYFMGL GDRHLQNIMI
     TDDGELFHID FGFILGNDAH PLTSSDVKLN SDMLSVIGGK KSLRYDTYLR LCAEAVVILR
     KYYNMFFVLL VCGTNFKEQD VEKFILSRFQ PRQLDKAVIS ELITIINGSD TCSDYIRDFL
     HYHTQERTIQ NGLTEIIKNA YTTVKSLTNG
//
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