ID   ATG1_PICAN              Reviewed;         804 AA.
AC   Q8TFN2;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-NOV-2008, entry version 35.
DE   RecName: Full=Serine/threonine-protein kinase ATG1;
DE            EC=2.7.11.1;
DE   AltName: Full=Autophagy-related protein 1;
DE   AltName: Full=Peroxisome degradation deficient protein 7;
GN   Name=ATG1; Synonyms=PDD7;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Pichia.
OX   NCBI_TaxID=4905;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / IFO 1476 / NRRL Y-5445;
RX   MEDLINE=22588459; PubMed=12702243; DOI=10.1016/S1567-1356(02)00135-6;
RA   Komduur J.A., Veenhuis M., Kiel J.A.K.W.;
RT   "The Hansenula polymorpha PDD7 gene is essential for micropexophagy
RT   and microautophagy.";
RL   FEMS Yeast Res. 3:27-34(2003).
RN   [2]
RP   NOMENCLATURE.
RX   MEDLINE=22912406; PubMed=14536056; DOI=10.1016/S1534-5807(03)00296-X;
RA   Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
RA   Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M.,
RA   Ohsumi Y.;
RT   "A unified nomenclature for yeast autophagy-related genes.";
RL   Dev. Cell 5:539-545(2003).
CC   -!- FUNCTION: Serine/threonine-protein kinase involved in glucose-
CC       induced peroxisome degradation (micropexophagy), ethanol-induced
CC       macropexophagy and microautophagy. Probably also involved in
CC       cytoplasm to vacuole transport (Cvt).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. APG1/unc-51/ULK1 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AY053423; AAL23618.1; -; Genomic_DNA.
DR   HSSP; P49137; 1NY3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_bd_CS.
DR   InterPro; IPR017442; Se/Thr_pkinase-rel.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   InterPro; IPR002290; Ser_thr_pkinase.
DR   Pfam; PF00069; Pkinase; 1.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Autophagy; Cytoplasm; Kinase; Nucleotide-binding;
KW   Protein transport; Serine/threonine-protein kinase; Transferase;
KW   Transport.
FT   CHAIN         1    804       Serine/threonine-protein kinase ATG1.
FT                                /FTId=PRO_0000085650.
FT   DOMAIN       12    308       Protein kinase.
FT   NP_BIND      18     26       ATP (By similarity).
FT   ACT_SITE    158    158       Proton acceptor (By similarity).
FT   BINDING      41     41       ATP (By similarity).
SQ   SEQUENCE   804 AA;  89844 MW;  052186AA1F7FC585 CRC64;
     MSKHQTQVVG DFTIGPEIGR GSFANVYKGY DNRTKAPVAV KSVFRSRLKN QKLVENLEIE
     ISILKNLKNP HIVALLDCVK TDQYFHLFME YCSLGDLSYF IRRRDQLVQT HPLISSILER
     YPSPPNSHGL NKVLVVNFLK QLASALEFLR DQNLVHRDIK PQNLLLSPPV HSKEEFKRKG
     YSGLWELPVL KIADFGFARF LPSTSMAETL CGSPLYMAPE ILRYEKYNAK ADLWSVGAVI
     YEMSVGKPPF RASNHVELLR KIEKSKDEIT FPVSAEVPDD LVRLICGLLK ANPTERMGFQ
     EFFNDPLIVY DVQCADEPLE CSNVDEQLFI SEYLPNLKTS PPAKPAPETI KEESEEEERA
     ERAPTDSLLI GKEADLRIPR PMEGSGKDEV IKKLINKSSP PPDTVKDGQI KKGARRDKDD
     FVYEKDYVVV EKRTVEVNAI ADELAKAGAG AVAIPSPHLG TNEHSAANPS GPTETQTQRR
     FSPSSRTSSI GSNRRPSWGD RKMPISISPT NALTKALGYT SNRLFGQQQQ QPQQAQQAAI
     ESAITNVTTN LLATKTLRPL KPSQETSLED TEVINQLELL ATMAHAISLF AEVKFSQLIP
     LPPSSSSPGS ADYDEMYQND AFPPQMVKSI SSEGVALYVE TLSLLAKAMS IASDWWHQNS
     SKPSTSPKLN DLVQWIRSRF NESLEKAEFL RLRLADANEQ LVGESGSSLN KPVVAEKLIF
     DRALEMSRTA AMNELKNEDL LGCELSYSTA IWMLEALLSN DEEPVTGNEK LDAEDKKIIE
     LFINSIGNRL KVLRQKIDKQ GVRS
//