ID A0A059JEU8_TRIIM Unreviewed; 422 AA.
AC A0A059JEU8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=H109_01888 {ECO:0000313|EMBL:KDB26314.1};
OS Trichophyton interdigitale (strain MR816).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB26314.1, ECO:0000313|Proteomes:UP000024533};
RN [1] {ECO:0000313|EMBL:KDB26314.1, ECO:0000313|Proteomes:UP000024533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR816 {ECO:0000313|EMBL:KDB26314.1,
RC ECO:0000313|Proteomes:UP000024533};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Trichophyton interdigitale MR816.";
RL Submitted (FEB-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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KDB26314.1}.
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DR EMBL; AOKY01000143; KDB26314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059JEU8; -.
DR STRING; 1215338.A0A059JEU8; -.
DR HOGENOM; CLU_018693_0_0_1; -.
DR OMA; IDFPQCI; -.
DR Proteomes; UP000024533; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05144; RIO2_C; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR030484; Rio2.
DR InterPro; IPR015285; RIO2_wHTH_N.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR45852; SER/THR-PROTEIN KINASE RIO2; 1.
DR PANTHER; PTHR45852:SF1; SERINE/THREONINE-PROTEIN KINASE RIO2; 1.
DR Pfam; PF01163; RIO1; 2.
DR Pfam; PF09202; Rio2_N; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KDB26314.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000024533};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 66..316
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 350..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..390
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 47512 MW; 3FAC4C795AE0C31B CRC64;
MKLDAKALRY LTGEDFRVLT GVETGSRNHE VVPTPLIVRL SGLRGGSAVH KSISNLAKLN
LIARVKNAKY DGYRLTYGGL DYLALNTYQK QQVVYSVGNQ IGVGKESDII AVAEASGAQR
ILKIHRLGRI SFRSIKNNRD YLRHRSSASW MYMSRLAAIK EFTFMKALRD HGFSVPEPIS
QNRHTIVMSM IDAFPLRQIS SVPNPAALYA ELIDTIMELA KFGLIHGDYN EFNILIKEEE
IPMETNEENK DKKEDNIKLT PVVIDFPQMV SVDHANAEMY FDRDVNCIKR YFQRRFGFVS
DEPGPFFSEA RKLVGADGTP RLDVAVEASG FSKKMAKELE AYMKEVGVDG DARGIEDDDE
DIDNEQDIDE NEENEDDNLG QEEEGINDFE NSEANEQLEQ KPQIPEPDAK IGMEKLTISG
SS
//