ID A0A0N0P787_LEPSE Unreviewed; 386 AA.
AC A0A0N0P787;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=ABL78_2412 {ECO:0000313|EMBL:KPI88516.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI88516.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI88516.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI88516.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
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 -!- 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:KPI88516.1}.
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DR EMBL; LJSK01000048; KPI88516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0P787; -.
DR EnsemblProtists; KPI88516; KPI88516; ABL78_2412.
DR VEuPathDB; TriTrypDB:Lsey_0048_0360; -.
DR OMA; RYYAANL; -.
DR OrthoDB; 117096at2759; -.
DR Proteomes; UP000038009; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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 InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR24356:SF163; 3-PHOSPHOINOSITIDE-DEPENDENT PROTEIN KINASE 1-RELATED; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 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.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|RuleBase:RU000304};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|RuleBase:RU000304};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 10..295
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 321..381
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 386 AA; 43072 MW; 07C94539855BD7A4 CRC64;
MPTKMAAADF EFGPPLGTGA FSKVVIGLYK PTGVKYAVKF ISKRSILDAP SDEERTRMAE
MARRETRMLL MCEHPNIVKF YASMQTTEDL LYVTELCDGG ELLKHIERWG RIPLEAARCA
IAELFSAVFY LHYGEKKTNT PNGPAMKPIT VIHRDIKPEN IMLTADKHLR LIDFGTAVVC
ESANDKATEG DTGGSGRAQT FCGTTFYMSP ELLENSYTCC ASDYWGCGCV LYLMLVGRRP
FDASTQYLLI KTILEKEPEF PDDIDPDAKD LIRKLLVKNP TERIGMNDIK RHPFLSSVNL
NTVPSQNVVD YWLREIPWVD ESTVSACSNC KKPFGFLLGK KVCYNCGKIA CSACLSEMRH
IPESRFAAPQ HVCAVCASVL DDARPS
//
