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Database: UniProt
Entry: A0A0D2GSB4_9EURO
LinkDB: A0A0D2GSB4_9EURO
Original site: A0A0D2GSB4_9EURO 
ID   A0A0D2GSB4_9EURO        Unreviewed;      1058 AA.
AC   A0A0D2GSB4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=CAMK protein kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Z517_03109 {ECO:0000313|EMBL:KIW83863.1};
OS   Fonsecaea pedrosoi CBS 271.37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW83863.1, ECO:0000313|Proteomes:UP000053029};
RN   [1] {ECO:0000313|EMBL:KIW83863.1, ECO:0000313|Proteomes:UP000053029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW83863.1,
RC   ECO:0000313|Proteomes:UP000053029};
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 Fonsecaea pedrosoi CBS 271.37.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. CHEK2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005575}.
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DR   EMBL; KN846970; KIW83863.1; -; Genomic_DNA.
DR   RefSeq; XP_013287671.1; XM_013432217.1.
DR   AlphaFoldDB; A0A0D2GSB4; -.
DR   STRING; 1442368.A0A0D2GSB4; -.
DR   GeneID; 25302599; -.
DR   VEuPathDB; FungiDB:Z517_03109; -.
DR   HOGENOM; CLU_003637_1_0_1; -.
DR   OrthoDB; 2045964at2759; -.
DR   Proteomes; UP000053029; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd00060; FHA; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR44167:SF24; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK; 1.
DR   PANTHER; PTHR44167; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK-RELATED; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000053029};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          101..155
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          241..527
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          731..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..767
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         270
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1058 AA;  117828 MW;  226B7289AF55774D CRC64;
     MVSQPTQPST QPIEDPRRLR RNVSNISNED AIDVICLLSP TSPAAFEAVK ANLLDSPMHI
     LQNADLQDIS EDDLLFRDEF NQPRDLALRM SSPVTNLKDG FRFGRARNQC DVLLTAYDDD
     NLVSKVHFKI FVNSQGSLML EDLSTNGTVV DDVHLRARAR RDNPNLRPAT IALKHGSIIS
     LFGGGRKNEI KMMVRIPSRG DYEDEYEENL RRYLAARGDV AQFASMREST YGNYWNGGSL
     YNFTGLLGKG AFATVYKVQT KEEGDIYAAK ELDKRRFIKN GVLDMKFDSE LNIMKNLSHP
     NIVNYVDCHT YQHWIYILME YVPYGELAKE LGRHGAIPES DVQQIAKQIL HALYYLHRRN
     ITHRDIKPDN ILIASRNPLV VKLSDFGLSK CVTDQETFLK TFCGTLLYCA PEVYPDYATY
     AQGTATKRRR LGEPATKQPP SPYDQSVDMW SFGAVIFHLL CGKPPVTGRG DDRGAQMLNN
     IMTKNVNFDT LRQAGVSEMA IDFVGKLLNR NPALRPKEPE CLRHPWLRDL PDHCNYEDIE
     ELVDNPQNCL EVVDEVNEDI IDEELINTLN QLTQPPSSVR TPDRPAKRIR TRTELSPLAG
     AIAYPRLPEP GESFLPLPVA PELPAQRLFG EISASALRSS GIFGGELSPS SPTAVQDIRN
     RVEQISVNDF GDRGPRRVAE NADISGQPPQ YPQVLGVPEI AGGSAASLMG AENQIGQLNM
     ASPEADISDV ATPETTNPVT PDTRQLSPSA SVTPHANNES GDTAQVSEEP VCTRRIDLGL
     VDDPAHFEAE VEARKVSRAS RLRAKAETFH GNLITRNSPP SAELAVTIDA KTGHEVKSMG
     RLDRFIRPAP ELESTTRTSS QTTQFIKPAR RYGKLTSIPG SFANVTINLE ARFVLWGRGI
     DCTVKYPDTK DTRIPKFALK ITFWAPGMEA HVNRGNDWTA LPGVRTLVAT SASGSVFVND
     VELRKESPSG EAALFGKLYT GDVITIFDNG KGEFLKFKVE ITFGDSARPR PPDEEGFIVQ
     EERHHHQRMK ERESMRLSMR DNAGEVPIAP TVRLEPDC
//
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