ID K1V150_TRIAC Unreviewed; 1474 AA.
AC K1V150;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 28-JUN-2023, entry version 49.
DE SubName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000313|EMBL:EKC97624.1};
GN ORFNames=A1Q2_08083 {ECO:0000313|EMBL:EKC97624.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC97624.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKC97624.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC97624.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKC97624.1}.
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DR EMBL; AMBO01000406; EKC97624.1; -; Genomic_DNA.
DR STRING; 1220162.K1V150; -.
DR eggNOG; KOG0230; Eukaryota.
DR HOGENOM; CLU_004488_0_0_1; -.
DR InParanoid; K1V150; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd03334; Fab1_TCP; 1.
DR CDD; cd15725; FYVE_PIKfyve_Fab1; 1.
DR Gene3D; 3.50.7.10; GroEL; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_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; PTHR45748; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR PANTHER; PTHR45748:SF7; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EKC97624.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 308..380
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1474 AA; 164399 MW; 1DED6678F6F28436 CRC64;
MADRDRLSID TSTTAGAAPP PPAVSAGASQ ASSSRPSPVS QLTTFPNPFQ DEPEPGLLPS
LISKVKSTFG GATPQAPPPP SEAQQIAEAA RKSGVGQGTK PTGPKPTQKP PAEAPTAPAP
KPKQPAPPSS SQPTSASSSA ATSVAPSVTS APRRHLMPGE RWRPAGASPA QVTVSPITSL
TTTGPQHPEG LTPIPTTAPS VVPSFTNQPA TPALPQIDIT NAKGSAIHRI RRGSISTIPD
SPSSASLNAM MSNPSDYNNF SFVPGFQLPA DDTRSVRSFA LAKRPGSVSK IIRRMRGEGL
SKHYWMADEN CKECYDCKSV SDQICVRSDW QVFTTWRRKH HCRICGQIFC GRCASNIIGA
RRFGQDGMVR VCNLCLKIME DYDDEDDRRS ISSGISSLPD RVFSPEVSYA QSPFAASQLL
RSHAANESLS AIDETDVPRY WNRDPDRPFT PEGVSEAGSD TEEDGLWTGA RPSTAAPFRR
QDDEASDDHH NQVVPHGTPP NLGNEGDRRD FPTTPHHFFP RTETMDSETD PRYFALMDST
NGRPGIRSRL SSANSVLGIN ALLDSDRKDG LWRARSQSFV TPPEFLCGPS LAHFNTMLQQ
AIETADLSTP AQWHRVLGRL LLRVSTNVRP VLRAGDSIDV RAYIKIKKVP GGKISDSEYV
DGIVITKNVA HKGMSRRLVN PRIMVVTFPL DYHRVETQFM SLDPIMKQER DYLRLLTKRI
IDLRPHIVLA ERFVSRIALD YLYQANIVVA RGVKYSAVHQ VARCTHADII ASMDRLALEP
RLGRCAEFRV QTFENEAIPG RRKTYMRFEG THNGFGGTII LRGGELATLR KVKVIADFMS
LVAYHLKNET FLYGDEFHML PPHPPMPQKY QELLAMLAED EVPSKIYGRP VNSTSNEEDS
DELTPRALPE RDEERADALR LTKDIAESLR PYLVTVLSAS VAVRFPPPHP LAKMADLDRQ
LNHLLLQKDE KEAQQILQEE LRIPSGRFEA IEDEKDKAQE KEKPQEKGKE DEKESKEDKD
KSNDEEKQPE ADATPKKAPE KPALGEPIIE EIGSDTDTED EKVLSSNNET PRADDTPRAE
RTEFKPLTPV AMDSSPESST SSKRSSQLGP APSTAAPSAS TAPTSIPPSS SVPSTSTPSQ
ILPTPASKGD PYRVLLNPAD FEDATKLAFV EYEHAEQLKV WEHYVRKHDE PLDPQNYQGI
IYTQALFRQG QDKPCTEFAR QQINYYQDDD QSLGQFLDGM VNNAGLRCPG KNCEQLMLFH
YDVLVHGERR LQIVMEQFMC PLVGHEEQIL TWSYCRQCNK SWEPQVMRDE TSRISWGTYL
EHCFYPPQTN TGFGCTHDAY REHIRYFAHR NMVIRIHNDE IELFEPVRPP TKLLVRVEDK
VRIKNQEYES ALQRTAAFFD SVLFRLRSFS EELVHPEKLS SMRVERDALL ARAVADRDEM
VNSLNRTYKQ TPPTDVLAIN VVLQTLQEKV IQWE
//
