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
//