ID M2XC57_GALSU Unreviewed; 1320 AA.
AC M2XC57;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=Gasu_49420 {ECO:0000313|EMBL:EME27492.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME27492.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
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DR EMBL; KB454531; EME27492.1; -; Genomic_DNA.
DR RefSeq; XP_005704012.1; XM_005703955.1.
DR STRING; 130081.M2XC57; -.
DR EnsemblPlants; EME27492; EME27492; Gasu_49420.
DR GeneID; 17086396; -.
DR Gramene; EME27492; EME27492; Gasu_49420.
DR KEGG; gsl:Gasu_49420; -.
DR eggNOG; KOG0192; Eukaryota.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000030680; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16986; ANTH_N_Sla2p_HIP1_like; 1.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR CDD; cd14270; UBA; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR23257:SF779; SERINE_THREONINE-PROTEIN KINASE WNK4; 1.
DR Pfam; PF07651; ANTH; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00627; UBA; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:EME27492.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000030680};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:EME27492.1}; Transferase {ECO:0000313|EMBL:EME27492.1}.
FT DOMAIN 20..323
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 745..792
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 1063..1320
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 325..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1090
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1320 AA; 149091 MW; 891D1077B8EA8E72 CRC64;
MSVGQVNKLD ATFIDFLEIE SGKNRKVRGG SGKVWILRFL HPVSTTSNSS NNETLLWVAE
SVDNGDKLVV KFEVAHNPSE WELLLKEAED WKALSDCSLQ KKQETVYEEL ESKTRLDGES
DKANVLYGSL QVLPFTRLLD YAKVPYARSC LIFIVEYINV APLRPPVTEE QLLAILKNII
QGVLIMRELG MGVHGDLSLD KLLYCKESGV KIGGFGLKRR KKATTLSSWL ENSPERLDKE
DVYQIGAVAY ELCCGNKPFQ GGERDSTTKI QAVFGRVSFP EAACRRYSSQ ILEVIRRCLS
KNPSQRPDSF SLSYIVAAAQ GLVPPMSDMP AQERTGRDSV TMEKESSVGR RKTEEGISLS
SSTNNLRAIE RTSQDDPVGP RNTSTQIVEP GRGLSRDDLY LLHLYHVPHN VTRGPWESYH
RPGSFESSLA KATTNTPKPA KPKHIRWIVI DIWERHMGMV LYESFASHLR SSSATVVFKY
LTVIYKVMVD GPPEFLELSY RQASDQLFEY LERVWSREHL QNVSVTDDVY LFCFAGGEIS
RFSTLLRLKA KLFHDFSAVF DGSRSKIASY QQHYQQQLLL TVSHGHSRHM GKSELPGTPE
DPLQGKREPL LHAFVNLIEH CFKLSAYFLS CNDPCRELKL MVIPSLAIEI TKAYFASLSC
FYFLTQYYRE RRDLEGLRTC YNTFCSGHQQ TYTFVDSVLA EPNVAELCRE GTLPKLCFSI
APLEAFFEPA PETPSHLESD KRLNSMVEKG RFPFQVELRE LLNMGFTRDH AQLALERTQG
DVNAAVAQLV DDFASPDKIA KLLDSERPLA VGERTVTKRM EEQVFSPFRG QQHLVEEIKD
RRQTHNVSSN AMPNGVINQP KPSNSEQKIV LNDPQGWEKF RQRLTAENST HSKSDRGYHV
GNGDEPTPEK IGNKQDAKRG RPRASSAVEF SSSHNDDILN EKVSKEFDMK KPLNAQANHS
RTIADKNAQH TRHLDDRVQA PVAKQKNLNK EQVENKNDKV QIADKMKNEK FEKPHAPFCH
CVICEAAKNI QKVSLSSKVT PFSGGGSLMR SLNPSFEIDP TELEWGPLIG QGGFGQVYKA
RFRGTAVAVK TISAMALVNQ NAVKEFQSEV AVLCTLRHPN VILFMGACTR PPHLFIVTEF
MSKGTLFDIL HRYRVPMNWS LMKRMALDVC RGMTYLHASK LLHRDLKSSN LMLDDHFTVK
VGDFGLTRLI ATQTQGPMTG QCGTFQYMAP EVLANQPYSE KADVYSFGII LWEMVAKQLP
YYGIQPMQVA VAVLSKQMRP PMPPSCPAPL AQLIQSCWQQ DPSRRPSFPE IMKLLEQMPY
//
