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Database: UniProt
Entry: A0A194Q2S2_PAPXU
LinkDB: A0A194Q2S2_PAPXU
Original site: A0A194Q2S2_PAPXU 
ID   A0A194Q2S2_PAPXU        Unreviewed;       523 AA.
AC   A0A194Q2S2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Serine/threonine-protein kinase ULK3 {ECO:0000256|ARBA:ARBA00021644};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE   AltName: Full=Unc-51-like kinase 3 {ECO:0000256|ARBA:ARBA00032242};
GN   ORFNames=RR46_02547 {ECO:0000313|EMBL:KPI99633.1};
OS   Papilio xuthus (Asian swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI99633.1, ECO:0000313|Proteomes:UP000053268};
RN   [1] {ECO:0000313|EMBL:KPI99633.1, ECO:0000313|Proteomes:UP000053268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI99633.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPI99633.1};
RX   PubMed=26354079; DOI=10.1038/ncomms9212;
RA   Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA   Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA   Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA   Wang W.;
RT   "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL   Nat. Commun. 6:8212-8212(2015).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; KQ459564; KPI99633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194Q2S2; -.
DR   STRING; 66420.A0A194Q2S2; -.
DR   Proteomes; UP000053268; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR045269; Atg1-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR007330; MIT_dom.
DR   InterPro; IPR036181; MIT_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:SF65; SERINE_THREONINE-PROTEIN KINASE ULK3; 1.
DR   Pfam; PF04212; MIT; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00745; MIT; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF116846; MIT domain; 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}; Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW   Kinase {ECO:0000313|EMBL:KPI99633.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000053268};
KW   Transferase {ECO:0000313|EMBL:KPI99633.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        493..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          9..266
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          384..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..405
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   523 AA;  59340 MW;  0F787E967FAAEA19 CRC64;
     MSFPKIEGYV VTEKLGSGSY STVYKAITKV GARSTVAIKC IDKSRVKHSG AAVDNLITEI
     RLLKTLTHPH IVHMKQFTWD DRNIYIIMEY CCGGDLSKYI QRYGRVPEKQ VTISILHKLS
     KYLAISMCVV HMDLKPHNLL LHKGSDGKYI LKVADFGFAQ HMTEEQLRCL RGSPLYMAPE
     MLRGRYDARV DLWSVGVIMY ECLFGRAPYS SATFKELVDK IQRQAPIEIP PRSSISPGCQ
     DLLTRLLQHD PDKRISYEEF FAHEYLDLEH MPSKENYEKA VGLIKRAIEL DSAGELAGAL
     TAYSDSLRYL VPAVAAESDA LRRSALAAKL TRYMERAEEI KRYLKGESNP QVQSTPQQRY
     VQGRVEVAQT IQDTTSCVQE VINEQDQESE QTEGQNKNET CPERAKRPGA LARLLRRSQV
     SHLLRGDATV EDAERERGEM TSPRGLREGM PRERCMCTGF DCIQAVQAMQ GATYHPPFRI
     RGPLHGADDC LGRYYWCIIM TISCIFCVLV FVIFIVVIVK YTD
//
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