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Database: UniProt
Entry: G7X568_ASPKW
LinkDB: G7X568_ASPKW
Original site: G7X568_ASPKW 
ID   G7X568_ASPKW            Unreviewed;       615 AA.
AC   G7X568;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Serine/threonine-protein kinase ATG1 {ECO:0000256|ARBA:ARBA00018572};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE   AltName: Full=Serine/threonine-protein kinase atg1 {ECO:0000256|ARBA:ARBA00019599};
GN   ORFNames=AKAW_00346 {ECO:0000313|EMBL:GAA82231.1};
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA82231.1};
RN   [1] {ECO:0000313|EMBL:GAA82231.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA82231.1};
RX   PubMed=22045919; DOI=10.1128/EC.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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DR   EMBL; DF126447; GAA82231.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7X568; -.
DR   STRING; 1033177.G7X568; -.
DR   VEuPathDB; FungiDB:AKAW_00346; -.
DR   eggNOG; KOG0615; Eukaryota.
DR   eggNOG; KOG4177; Eukaryota.
DR   InParanoid; G7X568; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR045269; Atg1-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00248; ANK; 5.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 3.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          1..284
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          383..415
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          491..523
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          524..558
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          559..591
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          290..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   615 AA;  68841 MW;  A557240BCD429890 CRC64;
     MDEIAKSFRL NVTAVSESCN REILQHSSDD AGKDNGRTVV IWNRKDDLTK DVYLEKSQSG
     QLRVVKQVTT TDKSINYSKP LFVQFIGWFP YKNHVCLAME YCPYGDLKSY YTRPIPEAEA
     RNICTQLLDG LEVLHSLGIV HRDIKPENVL VFQKTPMKVK ITDFGVSKRA LEGQTEHRTA
     CGTMGFMAPE VLHLVDDTKE DSTFTSAVDI WSLGCLLYYI LTKQTPFSKY ELLRDYAKGR
     TAFPDGHLKE YHVSRQGRKF IERLLDPLPE ARPSASADLT SYWTIPDTGE ESIYPEPPSP
     GDADPSGFSR AFGDSTQPPI NDAQWIGFPD VPFELGPLSD NDMDYFSTEL WNFVKSARTF
     DRASTVKLQA LLTTHASPSR LHNGYTALHI ASESAPAEWV KLLLEYGADA HIRTEPGRET
     SLHLSTSKGD LEDFTKKSEL LLAIRAVREG INAQNSNGDT VLHLAIARFG TVSAIQPLLD
     AEASTNIKGR QGRTPLLYAL YLEQEAVATE LLDRDSDPHA LDNGGFSALH YAIASRTISI
     QFIKRLLDAG VDVNWKNEDD RTPLYLAAQK SKQEVMRLLL DHGAIPELGN PRLDIRVNQV
     QFATKIGLKS LWPFS
//
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