ID   VP15_YEAST     STANDARD;      PRT;  1453 AA.
AC   P22219;
DT   01-AUG-1991 (Rel. 19, Created)
DT   01-OCT-1994 (Rel. 30, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   PROTEIN KINASE VPS15 (EC 2.7.1.-).
GN   VPS15 OR YBR097W OR YBR0825.
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Ascomycota; Saccharomycetes; Saccharomycetales;
OC   Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=91105858; PubMed=1988155;
RA   Herman P.K., Stack J.H., Demodena J.A., Emr S.D.;
RT   "A novel protein kinase homolog essential for protein sorting to the
RT   yeast lysosome-like vacuole.";
RL   Cell 64:425-437(1991).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=S288C;
RX   MEDLINE=95208357; PubMed=7900426;
RA   Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT   "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL   Yeast 10:1363-1381(1994).
RN   [3]
RP   FUNCTION, MYRISTOYLATION, AND MUTAGENESIS.
RX   MEDLINE=92097523; PubMed=1756716;
RA   Herman P.K., Stack J.H., Emr S.D.;
RT   "A genetic and structural analysis of the yeast Vps15 protein kinase:
RT   evidence for a direct role of Vps15p in vacuolar protein delivery.";
RL   EMBO J. 10:4049-4060(1991).
CC   -!- FUNCTION: SER/THR-PROTEIN KINASE. BY REGULATING SPECIFIC PROTEIN
CC       PHOSPHORYLATION REACTIONS (AND PROBABLY ITS AUTOPHOSPHORYLATION),
CC       VPS15 APPEARS TO BE ESSENTIAL FOR THE EFFICIENT DELIVERY OF
CC       SOLUBLE HYDROLASES TO THE YEAST VACUOLE. PHOSPHORYLATES VPS34.
CC   -!- SUBUNIT: VPS15 AND VPS34 FORM A COMPLEX.
CC   -!- SUBCELLULAR LOCATION: PERIPHERALLY ASSOCIATED WITH THE CYTOPLASMIC
CC       FACE OF A LATE GOLGI OR VESICLE COMPARTMENT.
CC   -!- PTM: AUTOPHOSPHORYLATED.
CC   -!- SIMILARITY: WITH THE CONSERVED CATALYTIC DOMAINS OF SER/THR-
CC       PROTEIN KINASES.
CC   -!- SIMILARITY: CONTAINS 7 HEAT REPEATS.
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DR   EMBL; M59835; AAA35214.1; -.
DR   EMBL; X78993; CAA55602.1; -.
DR   EMBL; Z35966; CAA85050.1; -.
DR   PIR; S44679; S44679.
DR   SGD; S0000301; VPS15.
DR   INTERPRO; IPR000719; -.
DR   INTERPRO; IPR002290; -.
DR   PFAM; PF00069; pkinase; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; UNKNOWN_1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; UNKNOWN_1.
KW   Transferase; Serine/threonine-protein kinase; ATP-binding;
KW   Myristate; Phosphorylation; Repeat.
FT   INIT_MET      0      0
FT   LIPID         1      1       MYRISTATE.
FT   DOMAIN       26    299       PROTEIN KINASE.
FT   DOMAIN      418    730       HEAT REPEATS DOMAIN.
FT   BINDING      53     53       ATP (BY SIMILARITY).
FT   ACT_SITE    146    146       BY SIMILARITY.
FT   MUTAGEN      53     53       K->D: LOSS OF ACTIVITY.
FT   MUTAGEN     146    146       D->R: LOSS OF ACTIVITY.
FT   MUTAGEN     148    148       K->D: LOSS OF ACTIVITY.
FT   MUTAGEN     164    164       D->R: LOSS OF ACTIVITY.
FT   MUTAGEN     199    199       E->R: LOSS OF ACTIVITY.
FT   CONFLICT    133    133       T -> A (IN REF. 1).
FT   CONFLICT    442    442       L -> PV (IN REF. 1).
FT   CONFLICT    609    609       F -> S (IN REF. 1).
SQ   SEQUENCE   1453 AA;  166227 MW;  4D0A77B4A4B8870C CRC64;
     GAQLSLVVQA SPSIAIFSYI DVLEEVHYVS QLNSSRFLKT CKALDPNGEI VIKVFIKPKD
     QYSLRPFLQR IRAQSFKLGQ LPHVLNYSKL IETNRAGYMI RQHLKNNLYD RLSLRPYLQD
     IELKFIAFQL LNTLKDIHNL NIVHGDIKTE NILVTSWNWC ILTDFAAFIK PVYLPEDNPG
     EFLFYFDTSK RRTCYLAPER FNSKLYQDGK SNNGRLTKEM DIFSLGCVIA EIFAEGRPIF
     NLSQLFKYKS NSYDVNREFL MEEMNSTDLR NLVLDMIQLD PSKRLSCDEL LNKYRGIFFP
     DYFYTFIYDY FRNLVTMTTS TPISDNTCTN STLEDNVKLL DETTEKIYRD FSQICHCLDF
     PLIKDGGEIG SDPPILESYK IEIEISRFLN TNLYFPQNYH LVLQQFTKVS EKIKSVKEEC
     ALLFISYLSH SIRSIVSTAT KLKNLELLAV FAQFVSDENK IDRVVPYFVC CFEDSDQDVQ
     ALSLLTLIQV LTSVRKLNQL NENIFVDYLL PRLKRLLISN RQNTNYLRIV FANCLSDLAI
     IINRFQEFTF AQHCNDNSMD NNTEIMESST KYSAKLIQSV EDLTVSFLTD NDTYVKMALL
     QNILPLCKFF GRERTNDIIL SHLITYLNDK DPALRVSLIQ TISGISILLG TVTLEQYILP
     LLIQTITDSE ELVVISVLQS LKSLFKTGLI RKKYYIDISK TTSPLLLHPN NWIRQFTLMI
     IIEIINKLSK AEVYCILYPI IRPFFEFDVE FNFKSMISCC KQPVSRSVYN LLCSWSVRAS
     KSLFWKKIIT NHVDSFGNNR IEFITKNYSS KNYGFNKRDT KSSSSLKGIK TSSTVYSHDN
     KEIPLTAEDI NWIDKFHIIG LTEKDIWKIV ALRGYVIRTA RVMAANPDFP YNNSNYRPLV
     QNSPPNLNLT NIMPRNIFFD VEFAEESTSE GQDSNLENQQ IYKYDESEKD SNKLNINGSK
     QLSTVMDING SLIFKNKSIA TTTSNLKNVF VQLEPTSYHM HSPNHGLKDN ANVKPERKVV
     VSNSYEGDVE SIEKFLSTFK ILPPLRDYKE FGPIQEIVRS PNMGNLRGKL IATLMENEPN
     SITSSAVSPG ETPYLITGSD QGVIKIWNLK EIIVGEVYSS SLTYDCSSTV TQITMIPNFD
     AFAVSSKDGQ IIVLKVNHYQ QESEVKFLNC ECIRKINLKN FGKNEYAVRM RAFVNEEKSL
     LVALTNLSRV IIFDIRTLER LQIIENSPRH GAVSSICIDE ECCVLILGTT RGIIDIWDIR
     FNVLIRSWSF GDHAPITHVE VCQFYGKNSV IVVGGSSKTF LTIWNFVKGH CQYAFINSDE
     QPSMEHFLPI EKGLEELNFC GIRSLNALST ISVSNDKILL TDEATSSIVM FSLNELSSSK
     AVISPSRFSD VFIPTQVTAN LTMLLRKMKR TSTHSVDDSL YHHDIINSIS TCEVDETPLL
     VACDNSGLIG IFQ
//