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Database: UniProt
Entry: A0A1Y2BVL5_9FUNG
LinkDB: A0A1Y2BVL5_9FUNG
Original site: A0A1Y2BVL5_9FUNG 
ID   A0A1Y2BVL5_9FUNG        Unreviewed;       536 AA.
AC   A0A1Y2BVL5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Pkinase-domain-containing protein {ECO:0000313|EMBL:ORY38812.1};
GN   ORFNames=BCR33DRAFT_754493 {ECO:0000313|EMBL:ORY38812.1};
OS   Rhizoclosmatium globosum.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Chytridiales;
OC   Chytriomycetaceae; Rhizoclosmatium.
OX   NCBI_TaxID=329046 {ECO:0000313|EMBL:ORY38812.1, ECO:0000313|Proteomes:UP000193642};
RN   [1] {ECO:0000313|EMBL:ORY38812.1, ECO:0000313|Proteomes:UP000193642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL800 {ECO:0000313|EMBL:ORY38812.1,
RC   ECO:0000313|Proteomes:UP000193642};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORY38812.1}.
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DR   EMBL; MCGO01000042; ORY38812.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2BVL5; -.
DR   STRING; 329046.A0A1Y2BVL5; -.
DR   OrthoDB; 10768at2759; -.
DR   Proteomes; UP000193642; 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   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; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 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; PS50004; C2; 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ORY38812.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193642};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          13..138
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          179..434
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          435..507
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         208
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   536 AA;  60907 MW;  89F3D39D7DFA4633 CRC64;
     MASTQSLNTP LSKSQELDTA EKVTKEFEQP GLLYVRIVEA RNLNHVANAK ALKESQPMPY
     LVIEFDKNET MSWGKEPKQE EYASAGTIDF NFNTSFDVSR ESDLVVTMYQ KKALRGDIPV
     GTVRISPAFD QKEQDEWFKL LPVGSASTPL TTSVGEIRVH ILFKEHPKTA VKPLGVDDFE
     ILRVLGKGSF GKVVQVRKKD TGRVYAMKIL KKASIVERDE VQHTLAERNV LAKVSHPFIV
     NIKFSFQTKD KLYLVLAFVN GGELFHHLQM EGRFEESRAR MYAAELLSAL ECLHSFNIIY
     RDLKPENILL DYSGHIALCD FGLCKLNMKD GHTTNTFCGT PEYLAPEILL NQPYTKAVDW
     WTLGVLIYEM IVGLPPFYDE NHSVMYERIL GDELKFPDYM GTAVMDLLKK LLNRDPAQRL
     GANGAQELKS HPFFAEINWQ KLNARKYRPA FRPEVSHAAD TSNFDQEFTS EEARDSCVDP
     HNRLPDSQQA QFAGFSYRKT SAESMQIGSL NGRRGSLPRG SLALRREGHG LRRWEE
//
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