ID A0A2P8AJG2_9PEZI Unreviewed; 749 AA.
AC A0A2P8AJG2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=B9Z65_741 {ECO:0000313|EMBL:PSK60591.1};
OS Elsinoe australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK60591.1, ECO:0000313|Proteomes:UP000243723};
RN [1] {ECO:0000313|EMBL:PSK60591.1, ECO:0000313|Proteomes:UP000243723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:PSK60591.1,
RC ECO:0000313|Proteomes:UP000243723};
RA Cheng Q.;
RT "Draft genome sequence of Elsinoe australis.";
RL Submitted (MAY-2017) 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. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196}.
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:PSK60591.1}.
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DR EMBL; NHZQ01000003; PSK60591.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8AJG2; -.
DR STRING; 40998.A0A2P8AJG2; -.
DR Proteomes; UP000243723; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; 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; cd05147; RIO1_euk; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR PANTHER; PTHR45723; SERINE/THREONINE-PROTEIN KINASE RIO1; 1.
DR PANTHER; PTHR45723:SF2; SERINE_THREONINE-PROTEIN KINASE RIO1; 1.
DR Pfam; PF01163; RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01245; RIO1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000243723};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 121..373
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..67
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..490
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 85016 MW; 167B95D7F8ACA2B5 CRC64;
MEGASPSNPA DGAVPPMQYD PRSGYKTDNG NEAGLDREPV EAPFGDGEFD DLEEEDDADD
FFDDDFEDSS PGISTGKVGD RPAINMKARI DDQIQSLAKH TSKLRLTELE TGASSKTGDK
DRSDRATSEQ VLDPRTRMIL LQLLNRNVVS EINGVLSTGK EANVYHALTI PQEDADSEPQ
TLHRAIKIYK TSILVFKDRD KYVTGDFRFR KGYNKSSNRA MVKVWAEKEY RNLRIIHESG
IPCPEPVSLK NHVLVMSFLG DKKGWPAPRL RDAVFSGSND EQSQTMKDLY IQLLGYVRKM
YRVCKLVHAD LSEYNILYHE GKLWMIDVSQ SVEHDHPRSL EFLRMDVKNV SDYFSRQGVD
TLSERTVFSF VTMYQGDCDD AGMKATIDKL YEDRATGKLN EEDEAVDNEV FRQQYIPQNL
DQVYDIERDA ERIGKGEGDD LVYRALLANK VTDAKPNAGA DGEGLAKTGD DDGSGGSDDA
NEDEGSEGEG SGFESENGVP RGKRFQDKDA KKEHKKAVKE EKRERRKTKI PKHVKKKMEG
RSGVITLKSI HEKGDTEGAD DPEAVRAMLD FFYGVERYYT NNNWGSELFH LAGLYIISDK
YRVAGMKDDV LRHFRRTLVS SRRSDGSELA PVLRRLWDNL PSVEDPIFKV FFEFVVCCKS
RVLRQSDMEA LVMQVPGLAV KTLNVFQKWC CQPAKNRSVD GRLIPERTGV EPRVETRQWE
ELQCRCDEAW EKMRSPRPGR HEFDSPNLW
//
