VPS15_DICDI
ID VPS15_DICDI Reviewed; 1966 AA.
AC Q54S77;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable serine/threonine-protein kinase vps15;
DE EC=2.7.11.1;
DE AltName: Full=Phosphoinositide 3-kinase regulatory subunit 4;
DE AltName: Full=Vacuolar protein sorting protein 15;
GN Name=vps15; Synonyms=pik3r4; ORFNames=DDB_G0282627;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- 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;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000047; EAL66173.1; -; Genomic_DNA.
DR RefSeq; XP_640162.1; XM_635070.1.
DR AlphaFoldDB; Q54S77; -.
DR STRING; 44689.DDB0216334; -.
DR PaxDb; Q54S77; -.
DR PRIDE; Q54S77; -.
DR EnsemblProtists; EAL66173; EAL66173; DDB_G0282627.
DR GeneID; 8623700; -.
DR KEGG; ddi:DDB_G0282627; -.
DR dictyBase; DDB_G0282627; vps15.
DR eggNOG; KOG1240; Eukaryota.
DR HOGENOM; CLU_001696_0_1_1; -.
DR InParanoid; Q54S77; -.
DR OMA; RELILHM; -.
DR Reactome; R-DDI-1632852; Macroautophagy.
DR Reactome; R-DDI-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-DDI-1660516; Synthesis of PIPs at the early endosome membrane.
DR Reactome; R-DDI-1660517; Synthesis of PIPs at the late endosome membrane.
DR Reactome; R-DDI-5668599; RHO GTPases Activate NADPH Oxidases.
DR PRO; PR:Q54S77; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0071561; C:nucleus-vacuole junction; IBA:GO_Central.
DR GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IBA:GO_Central.
DR GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:dictyBase.
DR GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; ISS:dictyBase.
DR GO; GO:0006623; P:protein targeting to vacuole; ISS:dictyBase.
DR GO; GO:0007034; P:vacuolar transport; ISS:dictyBase.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045162; Vps15-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR17583; PTHR17583; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; WD repeat.
FT CHAIN 1..1966
FT /note="Probable serine/threonine-protein kinase vps15"
FT /id="PRO_0000362035"
FT DOMAIN 21..303
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 558..596
FT /note="HEAT 1"
FT REPEAT 604..642
FT /note="HEAT 2"
FT REPEAT 717..754
FT /note="HEAT 3"
FT REPEAT 756..793
FT /note="HEAT 4"
FT REPEAT 1460..1499
FT /note="WD 1"
FT REPEAT 1508..1547
FT /note="WD 2"
FT REPEAT 1564..1605
FT /note="WD 3"
FT REPEAT 1610..1649
FT /note="WD 4"
FT REPEAT 1790..1829
FT /note="WD 5"
FT REPEAT 1935..1966
FT /note="WD 6"
FT REGION 362..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1713..1743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1966 AA; 216970 MW; 4043C5FB5831DA7B CRC64;
MGNTVGAPIV SEYLEDEIGP IVFKKSLGNA RFLKTVKAYH SEEGYVVVKI YKKRNTKESL
EKYKIMLKEI KDNFNITPSF NIMPYQHFIE TDRSGYLIRQ YFHNNLYDRL STRPFLSMIE
KKFIAFQLLK ALEQSSFKGV FHGDIKSENV LVTTSNWVYL SDFACYKPTF IPEDNPADFS
FYFDTSGRRT CYIAPERFYE TNRGAPSNNE LTPKMDIFSL GCVIAELFLD GFPIFDFSQL
LSYRKGEYSP EPIIRQRIQD PNIQTLILHM IQKDPDQRYT PEKYISKWNT VFPQYFSFAH
QFIPELMRLE NDDRVMCISD KFDEIVDIFK NNSITNLFKS NLNQSTNSNT IGSFRVSTPS
SPILISNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNQ TTTTTTNTNI NTTQQQQQQQ
QQQQQQLQRP LSKLDDIGKN IANIIYKTEQ FVKESDEFDK TDITNIKELN IQTTPTINTS
TINRVIQTSK TNTNLDTINE NSNNNIGVNR KKVTVVEGLD LFLSVIYTAV KHCQFPSTKV
KCVGSLLVRL AEMLDDECRL QKIVPYIMSM ISPEQPTLVR VEALRSLAKV LEMVQTFPPS
ESSIFGQYIL PSLSQLSHES TDEIIRIAFA EILPQLATTA KRFLEIAQHY RDPDSEGIME
SRKDRAKFRV YDSDLQEVQD QFFNKVSDLL TKDSCNTLKK IILSDIYRLC VFFGRQKTNE
SVLPLIITFL NDRDWQLRCA FFENIVAVCT VVGAGSLESF IYPCILLALT DEEEFVTEKA
LSSLSELCSL GLLRKPILLE LLVKTSPMLL HPNNWIRYGV VSLIVKICQS LSKADVYCYV
KPKLSPFLVN LNGNGNGNAE ISDTITESNL IQLLDSPISR ESFNKIVKFI ARNRINLSSS
INSILANDND NFNGESFNSN GSGGGGNPNL VSSTGGSNRR LRALSNKFFV PNILSASNSS
INSTSGDIGS LLSQSTEESL AFLRQMTSIG ISDSDQNKII KCFDYLQSKK CKDLESANNS
EGNVIVIRTN GTTIISSSNN SNNNTLSSST TSSNSTTPTN STVNLHSVLN NTTIIQQQQQ
QLQQTITQQS ITQQQQQQQQ QQQVSGGITT GGTTTTTLGR SSSPQLTGLN PSILSNSNNI
QLSSSVVDVT KLPNSIPIRM VKIRGGDQSL NNSTVSLGSV AGGNIITPST SLSNSNTMVG
NNNNNSYNTS TSSSPLSSSV LNSSVGMNNL TNSNANSINN SSGINNNNSN NNSVNSNNYN
NMNNNTMNNS VNLMNSNQIG QQQQQNPNTV KIDLVSPSDL NVVSKKYYIR DPKMGLSTIL
KVETNVECSI KVPLPLPDLG STDSVLGGGL LSSGGVGGGV GGTGGGNING VSGINGNVGG
GGGGVGVGTV GSGGNGSIGG GNSGINNGSG GGGVNSGGNS GINSGSTNSS GSLYGNGNGL
DNLPNSTWRP MGILVSHFFE HKAAVNEIQV SSDNLFFATA SNDGTVKIWD CQRMEKSVTN
RARQTYAQQE GRITSISICE KTHSIASASD KGSIHVFRVG ISGKQKNGNI KYTNLSTVKN
ITETTRGNIV SVSHYSTNSS SVVTYATTKG GIHGWDLRSQ QDAFNLVNDA SLGLIQAFLI
DPNRNWLVTG TSRGFLTCWD LRFGIPLYSV RVSNGRILKF APYMLAKSAS ESWVYISTEQ
DNVIVFDLSN KKTTRVFKRS YEQPPQQQPQ QPQPPQQQQQ QQSQMNRSIN MTSSTTTTTT
SSYDFGTENL KTSSYSQLPS NPLVNSIVNN SNINNNNNNN DNSNNVTIFK PTPLVRALLN
PPNCPFLITA GDDKRIKLWD WNNLPQSYYV SIGKEPPPFY THKFSNDTSN AYEIHEEVWH
DTSSSSFYSN SAMFGGGGGG QPMSTSLSSS SLSQQQHQAQ LQLQYQLQQQ QQQQQYINHL
QQQKSKTSIS MPTVHHQEPI LDIKMMEVPN PMLISASTDG VVKVWK
