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Database: UniProt
Entry: A0A0L0DJ37_THETB
LinkDB: A0A0L0DJ37_THETB
Original site: A0A0L0DJ37_THETB 
ID   A0A0L0DJ37_THETB        Unreviewed;      1096 AA.
AC   A0A0L0DJ37;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=STE/STE11 protein kinase {ECO:0000313|EMBL:KNC52086.1};
GN   ORFNames=AMSG_00914 {ECO:0000313|EMBL:KNC52086.1};
OS   Thecamonas trahens ATCC 50062.
OC   Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX   NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC52086.1, ECO:0000313|Proteomes:UP000054408};
RN   [1] {ECO:0000313|EMBL:KNC52086.1, ECO:0000313|Proteomes:UP000054408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC52086.1,
RC   ECO:0000313|Proteomes:UP000054408};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA   Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA   Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA   Ruiz-Trillo I., Lander E., Nusbaum C.;
RT   "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL349436; KNC52086.1; -; Genomic_DNA.
DR   RefSeq; XP_013762091.1; XM_013906637.1.
DR   AlphaFoldDB; A0A0L0DJ37; -.
DR   STRING; 461836.A0A0L0DJ37; -.
DR   EnsemblProtists; KNC52086; KNC52086; AMSG_00914.
DR   GeneID; 25560689; -.
DR   eggNOG; KOG0198; Eukaryota.
DR   eggNOG; KOG0586; Eukaryota.
DR   OrthoDB; 1342069at2759; -.
DR   Proteomes; UP000054408; 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; cd00060; FHA; 1.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR   PANTHER; PTHR48016:SF29; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 1A; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KNC52086.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054408};
KW   Transferase {ECO:0000313|EMBL:KNC52086.1}.
FT   DOMAIN          7..57
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          269..366
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          488..752
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          824..1090
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          399..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          772..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..807
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1096 AA;  115439 MW;  313DE406CFADB895 CRC64;
     MEASGQGRVD CVRLPVPPSN TTVSGVHFKI WYEDRVRSFF VADCGSTNGT WYAEPALAEE
     LKDYRFLGDR YEDAGAQCVM ALKPLSSFKA ADTVFVVEDV ILPAGLGLGA TEALDLDATA
     SSTGGRAATL PESRPVDTVI QMLRGPLAGA HYVREFPQTY ALGRAPGKPS LHAPGAVPVL
     VETDDPHLSR HHLNLRFVTP PDAAEPGTYM VDVLSTTYYC RKLALGRIDA QLDALPWRRL
     EPGSSKLLRH DDLVRAGSVI FLVTSHAEVP RKMDPPYLVA SSPSSLFLKW DPPLSPTTLR
     GFVLAISDGQ PGTAAEKWRK LYGGPLREFV AQGLKPSSYY WFRIHARNSG GDGPWSKVIR
     FLTVASDDDG SAGNLTPTVS LSMASVASPL GQRRIAFGPT TAAAGPHDPE PESDDDATAS
     VTMTGPIGGG GGGESSAALD SSTFTLSTIK ATMEPALLSS GSLPASDSGR DAVTLIREAL
     ASSDDLSWRV RSVLGVGGQA RVYLAHMEAP VSMPVAVKEY QLAEGDTSGL ADVTHRINAI
     LATLDHPNIV RFYGSATRAQ ADAAVTVVHV FLEYVAGGSL SRMLADLKSG LSEPDAAHYL
     GQMVAGVAYL HRHSVIHGDL KPDNVLLKVD GHRTVVKLAD FGGASLLSGA DHTSAFVGTP
     HFMAPEAIRT ETATPESDVW SLGCTLLEML TGRMPWSHLN KQAAIFSIGT TLSGPSRPES
     LSHPASLFLD ACFALDPAAR ASATDLLDHP FVLGGGDAAE CGDATNASAR RVSSTAAAPV
     ADVARSSGSP PHAGSRRSSS RSPMRASHGR GSPSGGASDV VAFEELNVLA AHGESEFVCE
     CQDGTEVVVR FLGQSASAET LARVEAMASM RHPNCILFRG SCTRLVAGTV ATGYMVEYMS
     STLASLVAEP DFGSSCPLLA KLLLVKNIAS GLYYLHAQNV THGALVPWNV LYDPRSRSCK
     VGELGRVSPF YLGSQPDAVC GSLHLYLAPE VALFDALTPS ADVFSLGAIL MLVVFGLAPY
     TGLDASEPGG AHTSSPPHTA LLTLASDAGI ATAWSDIQRA CCELVADCLA LKASARPPIE
     EVVRKLKALV AQGYAS
//
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