ID A0A0V0TDL6_9BILA Unreviewed; 437 AA.
AC A0A0V0TDL6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 Name=ULK3 {ECO:0000313|EMBL:KRX36643.1};
GN ORFNames=T05_1823 {ECO:0000313|EMBL:KRX36643.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX36643.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX36643.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX36643.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC {ECO:0000256|RuleBase:RU000304}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX36643.1}.
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DR EMBL; JYDJ01000351; KRX36643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0TDL6; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Kinase {ECO:0000313|EMBL:KRX36643.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000313|EMBL:KRX36643.1}.
FT DOMAIN 62..328
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 437 AA; 49719 MW; 6C6DD2120C6627A8 CRC64;
MSETVDRPIQ NLSAIFLSDS PLSISLRTSS FCSLSSSRHT GQKLANNRML QMETVKPQPK
GYVLSECLGS GSFGTVYKAR SSTTQTGGES SRGNYVAVKC ILRRQIVRYK ESEDNLIAEI
SLLKKLKHPH IVELVDFSWD LNFIYLILEY CADKDLEELL KKQGHFSESE TKQLIRQLAS
ALQYLRSKSI GHFDLKPQNI LVACKKPNPV LKLGDFGFAR SFSVEDKAVG LRGSLLYMAP
EMLLRRQFDP KADLWSVGVI LYRCLYGRTP FIGNMQSIRR QLQAVRGSVP LPTTLSLSVD
CRDLMIRLLR VDPKQRIEFD HFFSHPFVDM QHYPSAACLA RADSYAKMAI AADEAGRVHQ
AFLLYREALE YYMPCLLCSE NVCWNRDDLR DKMCQYLNRA EALKRSLANR DPKTPLTRST
NQVDIARLFS VCTVESR
//
