UniProt: W2YD75

Database: UniProt
Entry: W2YD75_PHYPR

LinkDB:  W2YD75_PHYPR 
Original site:  W2YD75_PHYPR

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (6)   
   Pfam (5)   
   PROSITE (3)   
   SMART (1)   
All databases (20)   

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ID   W2YD75_PHYPR            Unreviewed;      1038 AA.
AC   W2YD75;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=F442_18734 {ECO:0000313|EMBL:ETP32598.1};
OS   Phytophthora parasitica P10297.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP32598.1, ECO:0000313|Proteomes:UP000018948};
RN   [1] {ECO:0000313|EMBL:ETP32598.1, ECO:0000313|Proteomes:UP000018948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P10297 {ECO:0000313|EMBL:ETP32598.1,
RC   ECO:0000313|Proteomes:UP000018948};
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., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P10297.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:ETP32598.1}.
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DR   EMBL; ANIY01003960; ETP32598.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2YD75; -.
DR   EnsemblProtists; ETP32598; ETP32598; F442_18734.
DR   Proteomes; UP000018948; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 5.
DR   Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR032171; COR.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020859; ROC_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR24193:SF121; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24193; ANKYRIN REPEAT PROTEIN; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF13606; Ank_3; 1.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF16095; COR; 1.
DR   Pfam; PF08477; Roc; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 9.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 8.
DR   PROSITE; PS50088; ANK_REPEAT; 8.
DR   PROSITE; PS51424; ROC; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018948};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   REPEAT          4..36
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          37..71
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          72..104
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          105..137
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          138..170
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          171..203
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          204..236
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          237..269
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          364..587
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
SQ   SEQUENCE   1038 AA;  117446 MW;  FB302038C1C9854C CRC64;
     MVQGAAIALQ YALRNSRADV ISLLLERGAD VNSQDEFGDT ALHRAIEQYR GNTAVISLLL
     QRGADAAVQN VDGQNALHYA AAIANSEAIS LLLKQGIDID AQDETGQTVL HYATVIANTE
     VMSLLLEQGA DVGTQDEDGK TALHYAVTSH NTDVMSLLLE RGADLAARYE DDETILHYAV
     RNGDVDVISL LLEKGADVAA TDNNGEIALH YAASFGHTER ILLLLDRGSD VNASDNDQLT
     VLHHAVTRCS PEAVLLLLNK GADANALTKD GLNPLSHMIL VKEDDPDDDY LGVVRLLCSQ
     EPKLKLPPST QSLAINQLGM LACAQYWQDR YEKKQPLLEI PSEVVKGGEN AVEMYLAELE
     KTDSSEVVHR QKICVVGRTK WGKTSLVRSI TEETSVLVPL EDRTIGIEVF PLRFTVDGDG
     NKMKATHHDV TFWDFAGQGV YRVAHAVFFS KRTLYLVCVD LAAYNEILEQ AKKESKTQRD
     EVPQRFFEKH ILRWIVLILL RQPEAEFKLI GTKHDEVSDS SRSEISHDIR DRLGQFLEKL
     DGSIQITGHA ATALKKEFEE GLVTTSVTNV ESIQKVKNSI KHTITAKPHL SFKMPITYTR
     VINYILEKRQ SVVGATNQDR MDKMIVSVRQ LCKDLLKLPD FPQDTDCREI LRVLHELGDV
     LWYKGIDEEL EKWIILDPSV VLDLVREVIN HKYKEEVDEQ YKVLSQNGIL PHSLLMTFPS
     WKSLAAVEDK MVHLFKQLLH RLNLVYPVND MEAIDKADIL VPMYWKTRET PKADLKLLAT
     QKTILTQDFG DSWHVATWRY WLPIVVSDAI FVNFVVKCYR PFVHRSARRA YFESSVRREF
     RAVVNHSANK TGQYNDILIE VAAPTEKLAW AEMMYFVTDM EKILEKDYPG LTKHARVKRF
     IVDDGEDRGV NDLMENPEDG KRQRAKARWL PPDFSWFTQC AWKNGGVYEI HQLRHQLEAV
     KNIVVTSESC RLPRLWTLLY PRKGSHVELR IHSDVSDVSV LYFCPVSSLC SHPQCRGCCR
     RESSFRSVEI GIKPKDHG
//

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