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Database: UniProt
Entry: G3Q0F2_GASAC
LinkDB: G3Q0F2_GASAC
Original site: G3Q0F2_GASAC 
ID   G3Q0F2_GASAC            Unreviewed;      1079 AA.
AC   G3Q0F2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=ULK1 {ECO:0000313|Ensembl:ENSGACP00000023344.1};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000023344.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000023344.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000023344.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; G3Q0F2; -.
DR   STRING; 69293.ENSGACP00000023344; -.
DR   Ensembl; ENSGACT00000023390.1; ENSGACP00000023344.1; ENSGACG00000017660.1.
DR   eggNOG; KOG0595; Eukaryota.
DR   GeneTree; ENSGT00940000156664; -.
DR   InParanoid; G3Q0F2; -.
DR   OMA; HEWEVAV; -.
DR   TreeFam; TF324551; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000017660; Expressed in camera-type eye and 12 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006914; P:autophagy; IEA:UniProt.
DR   GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR045269; Atg1-like.
DR   InterPro; IPR048941; ATG1-like_MIT2.
DR   InterPro; IPR022708; Atg1-like_tMIT.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR   PANTHER; PTHR24348:SF19; SERINE_THREONINE-PROTEIN KINASE ULK1; 1.
DR   Pfam; PF12063; ATG1-like_MIT1; 1.
DR   Pfam; PF21127; ATG1-like_MIT2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          33..302
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          325..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          784..808
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1079 AA;  116716 MW;  69EA50B757894AD4 CRC64;
     RVIRPARSPA RPSSSNSAIR LRRAMETVGK FEFSRKDLIG HGAFAVVFKG RHREKHDWEV
     AVKCINKKNL AKSQTLLGKE IKILKELKHE NIVALLDFQE TASSVYLVME TQYCNGGDLA
     DYLHTKGTLS EDTIRVFLQQ IAGAMRVLQG KGIIHRDLKP QNILLSYPPG RRSHSNNTCI
     KIDFVPTADF GFARYLQSNM MAATLCGSPM YMAPEVIMSQ SYDAKADLWS IGTIVFQCLI
     GKAPFQASSP QDLRLFYEKN KTLSPNIPRE TSSHLRHLLL GLLQRNHKDR MDFDEFFCHP
     FLEASSSLKK STPAVSMTCI PSSASASSCS SSSTSHLASP PSLAEGQHLR AKALASPTQE
     AAGFLLKDSS GGAGSSKNSS SCDTDDFVMV PAHFTTGELT CESKVLQDSL MNSGSSLLAS
     AGLCGQVKTP PQSPPCSGSP SPVSRPSEFS GSSCGGSYGN HCRSSPIPVP SQVQNYQRME
     QNMHCTRLDG SPRPSAPVRR CSSGSSLGFA RAGPSPPCGQ GAAHANRRLS LGGARPFQPS
     PQGTAEASPL WTSSTTAAGE QKHSDLCPPP TAPQPHPQQA PGLGARLHSA PSLLECTGAA
     GKQKIRKQHS DPAVAPSAGL KTLRPLHSSP RLSELMQRSP LPTILGSPSR AIPPFEFPKP
     PSSPNLVTFL TQQGLVIGSP CSRTAPPEPR DVGQRALTQV IQPAHCIHRR SDDAKVFGRS
     QSAGRLSDML LMAAFGPGGP VGDRDSAENL TSEKTIDIMV PPGGGGSPAP GSISPAQVVF
     TVGSPPSASS PPHTSRQRKY SVNPTMSSSG SFTSRYPQTC TYLDGFEAPS SPRYGFTDPI
     TANMGGRVTF EPPELPEETL MEQEHTDIVQ SLRFTLDFAR CLMEVAGACG VAALREQEDV
     SHPCLLQQQS VVADQISSLS REWSHAEQLV LYLKTAELLS TALHTAMERV KQGKLYPSST
     VKQIVRRLNE LYKSSVASCR SLSTRLERFF SRKHRLMDQI TSITAERLLF SHTVQMVQTA
     ALDEMFHQGE ASVLRYHKAL LLMEGLSLLL TEQDDILSVS KCKECIERRL TALQSGLCV
//
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