ID   W2LPR3_PHYPR            Unreviewed;      1310 AA.
AC   W2LPR3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=LNR domain-containing protein {ECO:0000259|SMART:SM00004};
GN   ORFNames=L917_03724 {ECO:0000313|EMBL:ETL99432.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL99432.1};
RN   [1] {ECO:0000313|EMBL:ETL99432.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL99432.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the stealth family.
CC       {ECO:0000256|ARBA:ARBA00007583}.
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   EMBL; KI678364; ETL99432.1; -; Genomic_DNA.
DR   EnsemblProtists; ETL99432; ETL99432; L917_03724.
DR   VEuPathDB; FungiDB:PPTG_08035; -.
DR   Proteomes; UP000054423; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR   Gene3D; 4.10.470.20; -; 2.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR000800; Notch_dom.
DR   InterPro; IPR047141; Stealth.
DR   InterPro; IPR031358; Stealth_CR1.
DR   InterPro; IPR021520; Stealth_CR2.
DR   InterPro; IPR031357; Stealth_CR3.
DR   InterPro; IPR031356; Stealth_CR4.
DR   PANTHER; PTHR24045; -; 1.
DR   PANTHER; PTHR24045:SF0; N-ACETYLGLUCOSAMINE-1-PHOSPHOTRANSFERASE SUBUNITS ALPHA_BETA; 1.
DR   Pfam; PF00066; Notch; 2.
DR   Pfam; PF17101; Stealth_CR1; 1.
DR   Pfam; PF11380; Stealth_CR2; 1.
DR   Pfam; PF17102; Stealth_CR3; 1.
DR   Pfam; PF17103; Stealth_CR4; 1.
DR   SMART; SM00004; NL; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1240..1257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          229..267
FT                   /note="LNR"
FT                   /evidence="ECO:0000259|SMART:SM00004"
FT   DOMAIN          291..333
FT                   /note="LNR"
FT                   /evidence="ECO:0000259|SMART:SM00004"
FT   REGION          598..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1281..1310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          644..671
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1296..1310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1310 AA;  147920 MW;  6A797E04F0587DA3 CRC64;
     MLSRSRRALA PDSSGPSPRS GCFVPFIFFL GVLITCFGFI LSEWEPVDRS NIGGVKAEDF
     LSYGPIDVVY TWVNGTDPRW KKEKEFWHKH WIASLTGQPL PVWGQEADVK GKDDSNSDNR
     FRDNEELRYS LRSLEKYAPW VRHIYVVTDG QIPSWLDIES PKLSIVKHRD IFANKSHLPV
     FSSPAIEWNL DNIPGLSDMF LYFNDDVFLG SPVRPEDFVS QAGVQKAYFA WEIPLCSNRC
     WESSLANGRC DKECNVTACD FDMGDCGCDV NPLDGSVTCD AEKIASILEQ SPKPPKIGNH
     ICQGLCHYQW LGNGMCDRTC NVSSCAFDGG DCRVVKPYDR NRPYLHDEED EGMSPLVKDL
     WSADVELNHT LVQVPLDVNA TYMNLTDAFG VNGSILSAAH DNEELVRFAS VYEKEMVLLL
     VFGRDSDANP MTSSVQITVV GEDAEGTPIQ LDFSLMRGKN QIEEVTSPAQ VEGVEEISSG
     VSTFQNTSIR PQLIRLPFGF RQAKFRNVMP STDEETEIKL ATASEDGEEV LLDGQIAVVA
     NKLANKVPLI EVFLPFNITG KKLNDGDILN LGWNMDLRLH NDVKDIDWSD HDACQLKVPK
     KKPATQPATD DSAGQAKKNI ADGRKEGSVA GEDQAEDMII PLLADSLEEK IEQNDKTLDA
     AQDEANQDEN MEAEVAEYDG GITKCRLADD NRGVIVTVRV LTNHAHAILS ATGVLDDEEK
     ESETDAPDTP ETSSSAASDT DGIDYSAVNK MMEEWKTSPQ AADGQICFFD ADRADPSRYR
     YCFALALGHY HSEEVELMHK PTLWALLHPP KPKVVYTPYT GDDPALLELL DRCIDTTRRL
     IGIRPRLCYK NEVPIPRPAK DEDKVDLQKE KEEEGRRLAC EAQKRRLVQR EQREKEERVA
     QSSGLFGGLS RLVGNIKTTV GLGHVVSTNE SLDDVEYADV CGPAEPKEEK PKITLRDAQA
     HLSKDTFGDS LRYVNKLYNR AFGKPKTSDR RRVPSHMPFL LQKSIIREIK DHWTKEIQDT
     SAHRFRHPQD MQFSFSYFHY LINRAKIHPH TLEEIWREYL DANRNGILDE NEVLTAASLA
     HGDAPPEDFV NEVRECVQPE KREKVREIPT AEGTLRLSET LTPYITLENL ERCPSVRDAL
     IKNVRYETKV ELMPETEVTF HMLSDNFKFA WKQMMGTRAR RTKFVCINDD MKNPSTAVSQ
     ILHELFLSIW PKRSQFELPY HLKNRYAHID EFNAAQERRH LAAAIAVVIL LLIAFVFRAE
     LRAMFGFQDI ARARAASASQ LTQDFQQAQD EEDKEDDDPT SKRRPRKASA
//