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Database: UniProt
Entry: S9V7N4_9TRYP
LinkDB: S9V7N4_9TRYP
Original site: S9V7N4_9TRYP 
ID   S9V7N4_9TRYP            Unreviewed;       335 AA.
AC   S9V7N4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=STCU_07993 {ECO:0000313|EMBL:EPY22966.1};
OS   Strigomonas culicis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Strigomonadinae; Strigomonas.
OX   NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY22966.1, ECO:0000313|Proteomes:UP000015354};
RN   [1] {ECO:0000313|EMBL:EPY22966.1, ECO:0000313|Proteomes:UP000015354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23560078;
RA   Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R.,
RA   Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P., Brocchi M.,
RA   Colabardini A.C., de Araujo Lima B., Machado C.R., de Almeida Soares C.M.,
RA   Probst C.M., de Menezes C.B., Thompson C.E., Bartholomeu D.C., Gradia D.F.,
RA   Pavoni D.P., Grisard E.C., Fantinatti-Garboggini F., Marchini F.K.,
RA   Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L., Elias M.C.,
RA   Goldman M.H., Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P.,
RA   Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P.,
RA   de Souza W., Schenkman S., de Vasconcelos A.T.;
RT   "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and Their
RT   Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae
RT   Family.";
RL   PLoS ONE 8:E60209-E60209(2013).
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. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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:EPY22966.1}.
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DR   EMBL; ATMH01007993; EPY22966.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9V7N4; -.
DR   EnsemblProtists; EPY22966; EPY22966; STCU_07993.
DR   OrthoDB; 146975at2759; -.
DR   Proteomes; UP000015354; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00821; PH; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR44899; CAMK FAMILY PROTEIN KINASE; 1.
DR   PANTHER; PTHR44899:SF3; SERINE_THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50003; PH_DOMAIN; 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EPY22966.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015354};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..141
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          212..330
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
SQ   SEQUENCE   335 AA;  37113 MW;  6A42E54CE704FD92 CRC64;
     MIHRDIKSAN ILLCSNGLVK LGDFGFSRMY AATVSDDVGR TFCGTPYYVA PEIWRRRPYS
     KKADMFSLGV LLYELLTLKR PFDGANMNEV MQKTLAGRYD PLPSKISPEM KEMVSSLLAG
     DPRQRPSSSK LLNTAICKLF MSGLLEIVQS QPAFQGKLRT TITDQIQVTK HMLKNEIKKA
     AVNPMEDSRA GAAASTTILA GATPLNSNIG GLTVYEGIVK KQSSGMVWKR RYLCIRAELA
     EGQTLENNVN PKFKSLDLVL AVSKDTMEQQ CIATPFGELE DVFPVPSKYT GSNAPHVFAV
     AFKTGKRLLF QARGEPECEE WMEKIQEVLG IGDEE
//
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