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Database: UniProt
Entry: A0A0G4FXE6_VITBC
LinkDB: A0A0G4FXE6_VITBC
Original site: A0A0G4FXE6_VITBC 
ID   A0A0G4FXE6_VITBC        Unreviewed;       733 AA.
AC   A0A0G4FXE6;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=Vbra_21764 {ECO:0000313|EMBL:CEM19672.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM19672.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEM19672.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CDMY01000518; CEM19672.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4FXE6; -.
DR   STRING; 1169540.A0A0G4FXE6; -.
DR   VEuPathDB; CryptoDB:Vbra_21764; -.
DR   InParanoid; A0A0G4FXE6; -.
DR   OrthoDB; 198307at2759; -.
DR   Proteomes; UP000041254; 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   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR019530; Intra-flagellar_transport_57.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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; PF10498; IFT57; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..247
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          255..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          703..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          605..646
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        264..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   733 AA;  81319 MW;  AEEBF973683147DE CRC64;
     MARSPSDDER VVALKKVNAF DEMDQKSKEK CLKEVRLLQS LDHPHIVAYL DSFISAGELY
     IIVEWAERGD LKRLIKRTAQ DESAFSESEC VEYGRQLASA IAHMHDKRIL HRDLKPANIF
     LAQDGRLKVG DLGLGRIMSS QTFEAHSKVG TPLYMSPEVL GGGGYDFKSD VWALGCILYE
     LATLKSPFRG EKQMSLYELY MKISKGDYPP LPYSLSEELR SLIVSMLSTA PAHRPSIREV
     LSRLEALCKP PAACVIPRTP PPQPEAERPD EGEREEVLER PTTSRAHRAP PLLVMDDIVD
     KLMMLDYQRL FAAPRGYPPL HRAFFAQAPP PGQRVDAFQY HYDLLMWLFS LQSDPTASDR
     PPTRTGGQRP SSLSPPVSRE EALGRLRDEL SRRGISMASV GSLSQLSSGY GEQACLVLNE
     VINQELLRRD FHFSPPSLRA HEAITFPEGP GEATDEEGVE HDDMLIVACP LSRSEDTDAA
     DQHDAAVIDE SLLPLSIRRP PPSHCGADVA EDHHDMIETS IEPSAWRQEC DRVGDRLNVV
     LPAGARDGAF GVGGSVEVFM RYAAAAIDAS GEAVRERLEG VSGSLGEELE TIRLTEGQMN
     DDGALRQLAE EATTLRASLA TAESDLEAAR ERVTHLTETL EALSCRHDDL QDAQEQQAES
     HSSDEAIPRM RDMTNRLRDD IRALDIRIGV ASADLLRHAV ERRRGVASET RADEGGEEGD
     LGCLDERHVR DFM
//
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