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Database: UniProt
Entry: F2TYU3_SALR5
LinkDB: F2TYU3_SALR5
Original site: F2TYU3_SALR5 
ID   F2TYU3_SALR5            Unreviewed;       881 AA.
AC   F2TYU3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:EGD78767.1};
GN   ORFNames=PTSG_01744 {ECO:0000313|EMBL:EGD78767.1};
OS   Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX   NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN   [1] {ECO:0000313|Proteomes:UP000007799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Salpingoeca rosetta.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL832957; EGD78767.1; -; Genomic_DNA.
DR   RefSeq; XP_004997723.1; XM_004997666.1.
DR   AlphaFoldDB; F2TYU3; -.
DR   STRING; 946362.F2TYU3; -.
DR   EnsemblProtists; EGD78767; EGD78767; PTSG_01744.
DR   GeneID; 16078318; -.
DR   KEGG; sre:PTSG_01744; -.
DR   eggNOG; KOG1095; Eukaryota.
DR   InParanoid; F2TYU3; -.
DR   Proteomes; UP000007799; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00173; SH2; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF294; TYROSINE-PROTEIN KINASE BTK29A; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGD78767.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:EGD78767.1};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          207..515
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          740..841
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   REGION          51..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..604
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..696
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..733
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   881 AA;  96883 MW;  161894134615594D CRC64;
     MVWTTADAEL WLVFVVCILV TAVSVALLFW YKLRKSTSGV VELDDEVVLG DPSLRNHSRN
     KTAPAGNGNA YQQQHPADGD PAAPLPQLPR NSSRRSQAWT LDDDNNENSD KGDNGAKVDG
     DGTSSANGSH HAGLLVGPGT PTPLTVPANA SAGTPHRTLV DAGESANTTL SQSPPHLQQQ
     GRASSSRSAR LFSRLRGTSK SGSTTPLQTP RGAGRGSAGA AADMRTTRHH AFDTPDHPGK
     TLPQLLQSTA IAAEDVRVTK KESPLDTQFI GRFRRPRDRT RAPGAFPVEA HIIEFSNDKQ
     RDQDLLAGFA TKYEGFVCEF IQAFYGLCQP VPGKTWLLLE RLTPVTLLGA AQQLQQQHRE
     LLPHEHVHFL SQVTAALHYL HGNNICHGYL RLDQCHITPQ NTIRLASFDA FRRLQLPYTH
     DDDVYNAPEL IQDRSAVADA ACDVWSFAVL AWQLAAPTTR PYAKISVSRL LAHLQSGGRL
     EKPDGMQDEV YDLLLSCWSI RAADRPPSEA LHRQMLDLRY QHSAPTRQLK DLLPALKPSH
     SSVVLDYGAP ITQRNMSDDD DDDDIGEINP YAVASSVLPA SDGSAAFDDD DDDDDDDDDD
     DEKDPNAVYA TPVKRSDRAV VTFPNPPPLP SRSYDRSSMQ ELVDPVDGAP SASAPAQRPT
     TKPKPKPRPS KQREQQQPQL HAPSASSTGA VTPPLQPASP SSAPAPAQAP TSSSSTRGRE
     RKQQEDEAEE DDKAHLTAQW YLANHQKKAA QNLMRQSDMQ DGTFLVRPSK TGDSFVLLVA
     FEGTIHTYRI HVEEGATPDK CWYFINKANS FPTLSRLIEF YRQPSLPAGT KKLRTRLRFP
     CQRPVQDMSY TSELASTERS LTRRQRMGLN DLDDSYPLTE L
//
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