ID G4ZTS2_PHYSP Unreviewed; 609 AA.
AC G4ZTS2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=SAP domain-containing protein {ECO:0000259|PROSITE:PS50800};
GN ORFNames=PHYSODRAFT_361180 {ECO:0000313|EMBL:EGZ13196.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ13196.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ13196.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ13196.1,
RC ECO:0000313|Proteomes:UP000002640};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the OST5 family.
CC {ECO:0000256|ARBA:ARBA00009825}.
CC -!- SIMILARITY: Belongs to the pinin family.
CC {ECO:0000256|ARBA:ARBA00010386}.
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DR EMBL; JH159156; EGZ13196.1; -; Genomic_DNA.
DR RefSeq; XP_009530625.1; XM_009532330.1.
DR AlphaFoldDB; G4ZTS2; -.
DR STRING; 1094619.G4ZTS2; -.
DR EnsemblProtists; EGZ13196; EGZ13196; PHYSODRAFT_361180.
DR GeneID; 20650159; -.
DR KEGG; psoj:PHYSODRAFT_361180; -.
DR InParanoid; G4ZTS2; -.
DR OMA; DEQKHEM; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0034998; C:oligosaccharyltransferase I complex; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR InterPro; IPR039853; Pinin.
DR InterPro; IPR006786; Pinin_SDK_MemA.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR007915; TMEM258/Ost5.
DR PANTHER; PTHR12707:SF0; PININ; 1.
DR PANTHER; PTHR12707; PINN; 1.
DR Pfam; PF05251; Ost5; 1.
DR Pfam; PF04696; Pinin_SDK_memA; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS50800; SAP; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002640};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 551..570
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 582..605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 480..514
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT REGION 1..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 67798 MW; 99796F75C03AD8DB CRC64;
MADRAESADE RALRRELQEL SKKREALDNS KRRGSGAAAE GVAGRRSVFA RLGGEPARGG
GAGRQVQLKE NNARGNASWR LGKRDNEDNG QNSAVKRQRL HSAVSRPEGA HHTERTETSR
TSTSVSSPSA NNARAQERKQ RAVAPYAQKD GIARSRRMFG ALMGHLGKAK RQIEKDTDLF
KRQDTKQQEA EQREKMQSQD REKRARQEAE VARLEASVAR AEMDRSEQIA RTKLEHLQTV
RKSESQSKFL VTIASPPLCY LPSKHTKETE DLVAASMEAH EAKMKALSQS HDEKLRKLEA
EFATKLEQLR EELEAAKKGE KEKSPAKEAS RKEKEDAMED DDEDMDQSSK KPEEDKTTKA
DASEDRKSSD RAAEKASDME VEDEYIVQET NGSRDNVKAA PTTEASSPSQ AKDEKSNTMQ
PKKELQDSPR QPARAVVDDK AKEGAKPASR EETAAKPAED GDAQSENAAA EPKEDAVALV
DKMKVTELRA ELKKRGLDVK GLKASLVQRL KEAMQNQDES KKLAMQMYPF RQNLSYVIEI
PYTSPVDPES YGFLTVVLLL TGLVFMALFF TRAVAPKKNA LVELVLAFIA ALLLGFGSLF
LFLWAEIYV
//