GenomeNet

Database: UniProt
Entry: A0A384AKJ8_BALAS
LinkDB: A0A384AKJ8_BALAS
Original site: A0A384AKJ8_BALAS 
ID   A0A384AKJ8_BALAS        Unreviewed;      2098 AA.
AC   A0A384AKJ8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000256|ARBA:ARBA00012009};
DE            EC=2.7.1.150 {ECO:0000256|ARBA:ARBA00012009};
GN   Name=PIKFYVE {ECO:0000313|RefSeq:XP_007187887.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007187887.1};
RN   [1] {ECO:0000313|RefSeq:XP_007187887.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007187887.1};
RG   RefSeq;
RL   Submitted (JAN-2023) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_007187887.1; XM_007187825.1.
DR   CTD; 200576; -.
DR   OrthoDB; 5481504at2759; -.
DR   Proteomes; UP000261681; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR   GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04448; DEP_PIKfyve; 1.
DR   CDD; cd03334; Fab1_TCP; 1.
DR   CDD; cd15725; FYVE_PIKfyve_Fab1; 1.
DR   CDD; cd17300; PIPKc_PIKfyve; 1.
DR   Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR   Gene3D; 3.50.7.10; GroEL; 1.
DR   Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR043548; PIKfyve.
DR   InterPro; IPR037378; PIKfyve_DEP.
DR   InterPro; IPR044769; PIKfyve_PIPKc.
DR   InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR   InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR   InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
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; PTHR46715; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE; 1.
DR   PANTHER; PTHR46715:SF1; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF01504; PIP5K; 2.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00330; PIPKc; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR   SUPFAM; SSF54849; GroEL-intermediate domain like; 1.
DR   SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS51455; PIPK; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW   ProRule:PRU00781}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00781}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          158..218
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          365..440
FT                   /note="DEP"
FT                   /evidence="ECO:0000259|PROSITE:PS50186"
FT   DOMAIN          1758..2084
FT                   /note="PIPK"
FT                   /evidence="ECO:0000259|PROSITE:PS51455"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          60..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          897..924
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          938..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1165..1193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1512..1554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1566..1601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1697..1801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1166..1185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1697..1712
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1718..1734
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2098 AA;  236888 MW;  AC68C60CF919C1B7 CRC64;
     MATDDKTSPT LDSANDLPRS PTSPSHLTHF KPLTPDQDEP PFKSAYSSFV NLFRFNKERG
     EGAQGEQQSL SGSWTSPQLP SRTQSVRSPT RYKKQLNEEL QRRSSVLDTR RKAEPAFGGH
     DPRTAVQLRS LSTVLKRLKE IMEGKSQDSD LKQYWMPDSQ CKECYDCNEK FTTFRRRHHC
     RLCGQIFCSR CCNQEIPGKF MGYTGDLRAC TYCRKIALSY AHSTDSNSIG EDLNALSDSA
     SSVSVLDPSE PRTPVGSRKA SRNIFLEDDF AWQSLIHPDS SNTALSTRLV SVQEDAGKSP
     ARNRSASITN LSLDRSGSPM VPSYETSVSP QANRTYVRTE TTEDERKILL DSVQLKDLWK
     KICHHSSGME FQDHRYWLRT HPNCIVGKEL VNWLIRNGHI ATRAQAIAIG QAMVDGRWLD
     CVSHHDQLFR DEYALYRPLQ STEFSETPSP DSDSVNSVEG HSEPSWFKDI KFDDSDTEQI
     AEEGDDNLTN SASPSKRTSV SSFQSTVDSD SAASISLNVE LDNVNFHIKK PSKYPHVPPH
     PADQKEYLIS DNGGQQLSIS DAFIKESLFN RRVEEKSKEL PFTPLGWHHN NLELLREENG
     EKQAMERLLS ANHNHMMALL QQLLHSESLS PSWRDIIVSL VCQVVQTVRP DVKNRDDDMD
     VRQFVHIKKI PGGKKFDSVV VSGFVCTKNI AHKKMNSSIK NPKILLLKCS IEYLYREETK
     FTCIDPIVLQ EREFLKNYVQ RIVDVRPTLV LVEKTVSRIA QDMLLEHGIT LVINVKSQVL
     ERISRMTQGD LVMSMDQLLT KPHLGTCHKF YMQMFQLPNE QTKTLMFFEG CPQHLGCTIK
     LRGGSDYELA RVKEILIFMI CVAYHSQLEI SFLMDEFAMP PTLTPNPSFH SLIEGQEDEG
     AAQEPFSGSP LPREPDFPPD FLPSDDSSLL ESRILFEKGD QETKSVPQDV ASSKHQEHAT
     AACPAGAPCA LFPSVPESLL PLHIDDQQDA IGSEQPEALQ QTEELQDPKS QMRAFRDPLQ
     DDTGLYITEE VTSSEDKRKT YSLTFKQELK DVILCISPVI TFREPFLLTE KGMRCSTRDY
     FAEQVYWSPL LNKELKEMES RRKKQMLRDL SGLQGMNGSV QAKSIQVLPS HELVSTRIAE
     HLGDSQSLGR MLADYRARGG RIQQKNSDPF AYSKDASGTS SGKSGSKSEG DEEKGLITSD
     AVWSTKVDCL NPANHQRLCV LFSSSSAQSS NAPSACVSPW IVTMEFYGKN DLTLGIFLER
     YCFRPSYQCP SMFCDTPMVH HIRRFVHGQG CVQIILKELD SPVPGYQHTI LTYSWCRICK
     QVTPVVALSN ESWSMSFAKY LELRFYGHQY TRRANAEPCG HSIHHDYHQY FSYNQMVASF
     SYSPIRLLEV CVPLPKIFIK RQVPLKVSLL QDLKDFFQKV SQVYLAVDER LASLKTDTFS
     KTREEKMEDI FAQKEMEESE FKSWTEKMQA RLLSSSVETP QQLQSVFESL IAKKQSLCEV
     LQAWNNRLQD LFQQEKGRKR PSVPPSPGRL RQGEESKISA MDASPRNASP GLQNGEKEDR
     FLATLSSQSS TNSPHLQLPT PPEGVPEQAV GGPPELDTAS SSEDVFDGHL LGSADSQVKE
     KSTMKAIFAN LLPGNSYNPI PFPFDPDKHY LMYEHERVPI AVCEKEPSSI IAFALSCKEY
     RNALEELSKV TLRNSAEEGF PTNSTLDSRP KSSSPIRLPE ISGGQTNRTA EVEPQPTKKA
     SGMLSFFRGT AGKSPDLSSQ KRETLRGADS AYYQVGQTGK EGTENQGIEP QDEVDGGDTQ
     KKQLTNPHVE LQFSDANAKF YCRLYYAGEF HKMREVILGS SEEDFIRSLS HSSPWQARGG
     KSGAAFYATE DDRFILKQMP RLEVQSFLDF APHYFNYITN AVQQKRPTAL AKILGVYRIG
     YKNSQNNTEK KLDLLVMENL FYGRKMAQVF DLKGSLRNRN VKTDTGKESC DVVLLDENLL
     KMVRDNPLYI RSHSKAVLRA SIRSDSQFLS SHLIIDYSLL VGRDDTSSEL VVGIIDYIRT
     FTWDKKLEMV VKSTGILGGQ GKMPTVVSPE LYRTRFCEAM DKYFLMVPDH WTGLGLNC
//
DBGET integrated database retrieval system