ID   YL615_MIMIV             Reviewed;         701 AA.
AC   Q5UR69;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Putative phosphatidylinositol kinase L615;
DE            EC=2.7.1.-;
GN   OrderedLocusNames=MIMI_L615;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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DR   EMBL; AY653733; AAV50877.1; -; Genomic_DNA.
DR   RefSeq; YP_003987132.1; NC_014649.1.
DR   SMR; Q5UR69; -.
DR   PRIDE; Q5UR69; -.
DR   GeneID; 9925255; -.
DR   KEGG; vg:9925255; -.
DR   Proteomes; UP000001134; 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:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1070.11; -; 1.
DR   Gene3D; 3.30.40.10; -; 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; PTHR10048; 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; SSF56112; SSF56112; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   3: Inferred from homology;
KW   Kinase; Metal-binding; Reference proteome; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..701
FT                   /note="Putative phosphatidylinositol kinase L615"
FT                   /id="PRO_0000309204"
FT   DOMAIN          407..677
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   ZN_FING         36..115
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          413..419
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          537..545
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          556..579
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   BINDING         42
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         61
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ   SEQUENCE   701 AA;  82069 MW;  1A9C85C9C98B0943 CRC64;
     MNQKQDNHGN NNHRDDNIDI NSSIMFNNKN NVWVDDVMVS RCYNCKKKFS MLRRKHHCRN
     CGNIFCYNCA NKFIVIPNFI NDRPEPADYW NISYYITSLK DEAERVCDNC YYKVKEKTAN
     SEKIANILKN PGSIVDISKL SVSYSDIKDH YYNHLRNIQY YLPNHVYSQI DKKIILANAK
     YFSKHSKYLV HLIKAIDWNT IKITDDKFDS PSVSIYKNRS QHKQKFLDHI CEIIENPKKV
     SCQDLLCTRT CQEQLSFDDC INILYSKVQE LPDSLLQYLF AIIELTPDDI IKNHAVLFVN
     IIKNNSNIFL EKLLYELLTK SEDMIYYIYW LLVISKEKAD YQDITNIQRF IELLDKQLVV
     KMDREYRFYA GLIKHLNDPK DYLENIFDIC DEISLPYNPS IKLTGVYTDQ IRIKNSYTRP
     VIIAFETNVG RIDILFKKES VMNDLIVMNL ISLCDVIIKE NIGLELGIVV YPIMPLTNNF
     GMIEIIKNAE TIHSIINQKK TVFQHIIDKN ENKVISDIMK TYMYSLVSYT LHSYFIGLGD
     RHLENIMITD NGEIFHIDFG FILGTDAFPL TLTSDIKLNS GMLDVIGGRG SDRYKIYLDL
     CAKGVIILRK YFNMFFILLS QNSNYKINHI ENFIMSRFQP RQHDTVVISE LMTIIEKSHD
     AYTGIIRDFL HYHNQEKTLQ NGMTKVLKEA YDVVKSFTNS T