ID A0A0W8C8R4_PHYNI Unreviewed; 1093 AA.
AC A0A0W8C8R4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Coatomer subunit zeta-1 {ECO:0000313|EMBL:KUF80459.1};
GN ORFNames=AM587_10017518 {ECO:0000313|EMBL:KUF80459.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF80459.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF80459.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KUF80459.1}.
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DR EMBL; LNFO01004567; KUF80459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8C8R4; -.
DR STRING; 4790.A0A0W8C8R4; -.
DR EnsemblProtists; KUF80459; KUF80459; AM587_10017518.
DR OMA; SIFMAVC; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IEA:InterPro.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00139; PIPKc; 1.
DR CDD; cd14829; Zeta-COP; 1.
DR Gene3D; 3.30.450.60; -; 1.
DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR011012; Longin-like_dom_sf.
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; IPR023610; PInositol-4/5-P-5/4-kinase.
DR PANTHER; PTHR23086; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; 1.
DR PANTHER; PTHR23086:SF151; RPKA; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR Pfam; PF01504; PIP5K; 2.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
DR PROSITE; PS51455; PIPK; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Kinase {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 171..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 424..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 492..857
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1093 AA; 123169 MW; E264C5FF9B3A3D62 CRC64;
MSRSYSTETP YRRSQSVTSH SQQHRGTPVL EDQNYMNAFS PPSNGVYVME TPQEHNSDAA
PDGRRSMRQL PPVDQNGSFR QRHGTRGTSG GFVTMDNSST ISSSSGNYID AMSLNNTMSA
TAQQPLISTP RATQKNIVRV IDKDMTQQFR GRSKSVGQGR IRWFENRKSQ LLGFCLTMAF
LGVSVAMYNY RWTGLIAGSV NTIICGSAVV ITYCRKKQWH QHPNPIVHNR SVLSIFMAIC
LLLNVLVDFD PSGSNTDCQR LAGITEFFFF TGEAWGLVMA CDLFFSLTSP FTSYKRLMKF
YHLWVWLGGI TMGVITYSVQ GAGGFFTVDG QSMTYESDTD TVIGFCLASS RICCDSGETC
PDDVQKCSTT ASFLNAQKWP WILIYAFVLL VLFVSVCVLT LAWHRLYLRG VPKTYNIRLR
VLNYISFFTG AYVFYWLLLL LLYMCAYFLS TKSDTSNSKA VAQVLRQLVI FLISSKGYLD
YVIWFAVNNI ERKGGNGRDE SADVDVDLSP QVNTALRSEI LYYTTSGIKE SVRAVTDELI
SIPISGESEA GKSIKFWSFC PASFRNIRLT FGISDADYIQ MFGATTKERF SEGRSGAFMF
YTSDESLIVK TMSPEECAFL RKIAPNYEAY MTSNPDTLLT RFYGCHSVSL YGKMYYFVVM
GNLFADTDVV HHRYDIKGSW VDRNAKVPSP GDKTACRYCN ASYTFGSTKN QECGDGMNFH
EPDIVLKDND LMTKIRIDPA TAHRIYDQIH KDSDFLCSQG IMDYSLLMGI QSSEYFVDTS
QLPQARRGVL FTQPATSVAG PSLYHFGIID FLQQWTLEKK MERFYKTFFK RKDPEGVSAL
PPKPYKFRFQ QKMSRIFALS THTRAENDTA FNHNYPALID VLDQGNFDNQ RHNTFINNSV
VDQRPVFNPD LQQDIRAAAS PSVKAIFILD SDGNRVCAKY YDKSYPTQKE QLALEKKLFA
KTKNSSARME ADIVLIENIV SVFRCGSDTT MHVIGSASEN ELILLTVLDS AFDAVSNLLK
GRMDRHVMLD NIELVLLTFG EVVDGGIILE VDTPSISNRV LMRGIDNEVP MAELTISQAF
ASAREQFSRS FRS
//
