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Database: UniProt
Entry: E4UUA5_ARTGP
LinkDB: E4UUA5_ARTGP
Original site: E4UUA5_ARTGP 
ID   E4UUA5_ARTGP            Unreviewed;       755 AA.
AC   E4UUA5;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=CAMKK/META protein kinase {ECO:0000313|EMBL:EFR00872.1};
GN   ORFNames=MGYG_03875 {ECO:0000313|EMBL:EFR00872.1};
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN   [1] {ECO:0000313|Proteomes:UP000002669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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DR   EMBL; DS989824; EFR00872.1; -; Genomic_DNA.
DR   RefSeq; XP_003173702.1; XM_003173654.1.
DR   AlphaFoldDB; E4UUA5; -.
DR   STRING; 535722.E4UUA5; -.
DR   GeneID; 10028985; -.
DR   VEuPathDB; FungiDB:MGYG_03875; -.
DR   eggNOG; KOG0585; Eukaryota.
DR   HOGENOM; CLU_000288_165_0_1; -.
DR   InParanoid; E4UUA5; -.
DR   OMA; FVEPPME; -.
DR   OrthoDB; 5489318at2759; -.
DR   Proteomes; UP000002669; 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; cd14008; STKc_LKB1_CaMKK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR24346:SF77; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE KINASE 1; 1.
DR   PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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:0000313|EMBL:EFR00872.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002669};
KW   Transferase {ECO:0000313|EMBL:EFR00872.1}.
FT   DOMAIN          87..386
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          649..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..510
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..529
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..677
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   755 AA;  83013 MW;  458B08C42974C9B2 CRC64;
     MDADPILKHG RTAQLALDTE VPTSRSSEPG PNALKGARPA SGSYDSPLRQ HARYPTAPRQ
     VKETLNAQST YTNSQDDNTA EHRINQYLIK QEIGRGSFGA VHLATDQYGQ EYAVKEFSKS
     RLRKRAQSHG LRRRTGKHPG VQPAGVGFNS PLHRHPSGID EGENGNSLYL IREEIAIMKK
     LNHSNLVSLI EVLDDPTEDS LYMVMEMCKK GVIMKVGLGE QADPYSEENC RCWFRDLILG
     IEYLHAQGIV HRDIKPDNCL LTNDDVLKVV DFGVSEMFEK SSDMFIAKSA GSPAFIPPEL
     CVAKYGEVSG RAVDVWSMGV TLYCLRYGRI PFHTSNIFDL YNAIRNDEVE LPGETNEAFK
     DLMKQILEKD PAKRITMPQL RVHPWVTKGG IDPLLSEEEN TATLVGPPTE EEMDSAITRN
     LGHALIVVKA VQKFKRLISD GSPLPMESIL GEGEESHFVQ PPLLMGEDEE EEFSAILHNR
     NMKEHVYPRR PDQPKRPSQA TMNSSPYVSL PPPNTFEPCA FPSPQPQSTP GADTPTRQTG
     SEGTRGHARD PLEEEMPFLN IGPSNFGSEA ELNPTNDTAM ESGGIPIPSK PAVTESPMIV
     SESPPAADID IYETAYKEII ERINSRSREA QSPTPKVYLN RRVEKKPTAS SGLWSVARKN
     SKLSSPLSRS VTDTVPDNRP PRPSPIKRFT AAAASFAASS GKQSPSPLAK AVQVNDAVRS
     DEGIEPNPLD TSAAVIETTA SPTALSPVDD AKKDM
//
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