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Database: UniProt
Entry: A0A1S3WJ41_ERIEU
LinkDB: A0A1S3WJ41_ERIEU
Original site: A0A1S3WJ41_ERIEU 
ID   A0A1S3WJ41_ERIEU        Unreviewed;      1041 AA.
AC   A0A1S3WJ41;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
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|RefSeq:XP_016046403.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016046403.1};
RN   [1] {ECO:0000313|RefSeq:XP_016046403.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_016046403.1; XM_016190917.1.
DR   AlphaFoldDB; A0A1S3WJ41; -.
DR   GeneID; 103119043; -.
DR   CTD; 8408; -.
DR   OrthoDB; 8335at2759; -.
DR   Proteomes; UP000079721; Unplaced.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR   CDD; cd14202; STKc_ULK1; 1.
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}; Kinase {ECO:0000313|RefSeq:XP_016046403.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          15..277
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          283..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          700..772
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..587
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..772
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1041 AA;  111829 MW;  D9F4AF6589B1E1E9 CRC64;
     MEPRGGLETV GKFEFSRKDL IGHGAFAVVF KGRHREKHDL EVAVKCINKK SLAKSQTLLG
     KEIKILKELK HENIVALYDF QEMANSVYLV MEYCNGGDLA DYLHTMRTLS EDTIRLFLQQ
     IVGAMRLLHS KGIIHRDLKP QNILLSNPGG RRANPNNIRV KIADFGFARY LQSNMMAATL
     CGSPMYMAPE VIMSQHYDGK ADLWSIGTIV YQCLTGKAPF QASSPQDLRL FYEKNKTLVP
     TIPRETSAPL RQLLLSLLQR NHRDRMDFDE FFHHPFLDAS AAVKKSPPVP VPSYPSSGSG
     SSSSSSSTSH LASPPSLGDM QQLQKTLISP AEAAGFLQGS RDSGGSSKDS CDTDDFVMVP
     AQFAGDLVAE VAGSRPPPDS LMCSGSSLVA SAGLESHGQT PSPSPPCSSS PSPSGRCGAS
     VPIPVPTQLH NYQRIEQNLQ SPAHCQTSRS STVRRSGSAS PLGFTRASLS PPTHVEHGAA
     LARKLSLGGG RPYTPSPQVG TIPERPGWSR VPSPQGAEIR AGRSPRSGSS VPEHSSHLTG
     LGSRLHSAPN LSDLHVIRPK LPKPPTDPLG LTFSPPPASP PQLAPGLPPC RPLRGSPKLP
     DFLQRNPLPP ILGSPTKAVS TLDFPKTPSS QNLLTLLARQ GVVVTPPRNR TLPDLSEAGP
     LHGQPLGPGL RLPEDAKSPF GRSFSTGRLT DLLLKAAFGT QAPDSGSTDS LQERPMDVAP
     SAGFGGSLHP GARAGGASSP APVVFTVGSP PSGTTPPQGP RTRMFSVGSS SSLSSAGSSS
     ARHLVPAEAP PELPIPGHCC SFADPLTVNL EGAVTFEAPD LPEETLMEQE HTEILHSLRF
     TLVFAEHILE MAALKGSASE AAGGPEFQLQ ESVVADQISL LSREWGFAEQ LVLYLKVAEL
     LSAGLQTAIE QIRAGKLCLS STVKQVVREL NELYKASVVS CEGLSLRLQR FFMDKHRLLD
     RIQSVTAEKL IFSHAVQMVQ SAALDEMFHR REDCVQRYHK ALLLLEGLQH ILTDQADVES
     IAKCKLCIER RLSALLTGIC P
//
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