ID A0A0D2IIL8_9EURO Unreviewed; 880 AA.
AC A0A0D2IIL8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Non-specific serine/threonine protein kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Z518_06692 {ECO:0000313|EMBL:KIX03141.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX03141.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX03141.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX03141.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847479; KIX03141.1; -; Genomic_DNA.
DR RefSeq; XP_013270277.1; XM_013414823.1.
DR AlphaFoldDB; A0A0D2IIL8; -.
DR STRING; 1442369.A0A0D2IIL8; -.
DR GeneID; 25294763; -.
DR VEuPathDB; FungiDB:Z518_06692; -.
DR HOGENOM; CLU_000288_52_1_1; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000053617; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd11651; YPK1_N_like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF245; AGC_AKT PROTEIN KINASE SCK2; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 493..754
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 755..839
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 880 AA; 97420 MW; 28C9FD9B4ED5394F CRC64;
MTLTDPLNSS AKHENRDDLH DQIGSNSPTP SGVETPRPDL HDKRLPGIMH SYFGQVGRDP
SQSTPSRSSQ AATSAEANEQ SAPFSLQHGK ETENRRVSSA SLGSMVMVER EQDSVSTPPP
EGPHPESSQS ATETDTSRLP PTPISSAASV VHRDGEVAEN GGSVIDGGIA SITQALRNFV
LPKTAFGMKE RRHQSLPVSS VTKSTVSAAH ISNPASSTHS SRPQSPQSPS PSSAKPPSSQ
NLQETNELTS DVAAGPRDKS TPPHTPRALS QEDRRNDARS PLSSTSTTVG DVSAETEKQQ
LSKDQIPTNT PRGKLSIKIA EGRNLKPSYD PYVVCQFEWN EYVSKGPRQD KMDVDEDDRK
GPVAALQSIP IRRTDSDMGK PMAIPMRSRQ SSTNGASEDR GLTKVTDPQW NHEAMFDVIS
QQSELDVTVY DRHSESFLGH VRLCLNLTEQ HPTLEGFFKL EPRSVEDHDI SGEIHIRLHF
SKVDKKHFGP NDFQILKLIG KGTFGQVYQV RKKDTQRIYA MKVLSKKVII QKKEIQHTIG
ERNILVRTAT TESPFIVGLK FSFQTPTDLY LVTDFMSGGE LFWHLQKEGR FKEDRAKFYI
AELILALKHL HDHNIVYRDL KPENILLDAN GHIALCDFGL SKANLTQDDT TNTFCGTTEY
LAPEVLLDEQ GYTKMVDFWS LGVLVFEMCC GWSPFYAEDT QQMYKNIAFG KVRFPRDALS
TEGRNFVKGL LNRNPKHRLG ANGDADELIH HPFFADIDWD ALGKKNLVPP FKPKLSSVAD
TSNFDPEFTN ALNTSSSLNA RAAALAAGAA PASTPLSPTM QNAFQGFTFV DESTMEERFG
GSRDAEDDRA DESHLSRSRT QEHRMSGVQR TGDDGFFFEE
//
