ID E5QZR7_ARTGP Unreviewed; 923 AA.
AC E5QZR7;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=AGC/AKT protein kinase {ECO:0000313|EMBL:EFQ98218.1};
GN ORFNames=MGYG_01253 {ECO:0000313|EMBL:EFQ98218.1};
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; DS989822; EFQ98218.1; -; Genomic_DNA.
DR RefSeq; XP_003177170.1; XM_003177122.1.
DR AlphaFoldDB; E5QZR7; -.
DR STRING; 535722.E5QZR7; -.
DR GeneID; 10032495; -.
DR VEuPathDB; FungiDB:MGYG_01253; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_52_1_1; -.
DR InParanoid; E5QZR7; -.
DR OMA; SFVMMER; -.
DR OrthoDB; 10768at2759; -.
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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
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; 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; 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:EFQ98218.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002669};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 500..761
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 762..846
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 923 AA; 100052 MW; C4594C6CAE52576E CRC64;
MGSTPTGIAT PQPDPSDKRV PGIMPSFFAQ VGAGSDSNSI PTAATTSIRP STSFSPSPPP
PPPPPPHPIS SPSSTHHTPG KHSSDDGVVA VGDPCQQTGE TQQQEIQPDV LKPPTSTSTS
PPLTESTNLL DRGCQNPALV NTPSRPATAQ SLEVISDKDY LLASSKDTSS GGGGRTDAGA
VAVNPLPTPP RSSFCSIANR DTEEAQNGAP EVDTGVSSVY RALKNLIFSK TSQKQKPKRH
TSFPVSSVSP DAVMASHFSK PSRPSSQSIS KPNSLSSSSK SSSQTHNDHL HHHHSISSSC
EDLEKLTHSV AAGPRTKNTP PLTPRAMSNE TDAAEKRDPP RSIIEHSPPH QGNKTPDSSS
QGGRHSTASS SHARKSKSNK PTASSRSSGA SEESGVPVTA SLKGKLTVKI VEGRGLRPSV
DPDVLGHQSE LDVSVYDRSN HEAFLGHLKL SLHLKDDRTT LSGWYPLQPL AHGQGPVSGE
IFLQMSFQKT DKKQFGPNDF QILKLIGKGT FGQVYQVRKK DTQRIYAMKV LSKKVIIQKK
EIAHTLGERN ILVRTAMTDS PFIVGLKFSF QTPTDLYLVT DYMSGGELFW HLQKEGRFLE
ARAKFYIAEL ILALQHLHDH DIVYRDLKPE NILLDANGHI ALCDFGLSKA NLTKDDTTNT
FCGTTEYLAP EVLLNETGYT KMVDFWSLGV LVFEMCCGWS PFYAEDTQQM YKNIAFGKVR
FPRDALSAEG RNFVKGLLNR NPEHRLGYRD DAKELMAHPF FHDIDWVVLA NKGVIPPFKP
TLTSVMDTSY FDPEFTTALE QSASLNARAA ALANGLNPAG TPLSPGMQAN FKGFTFVNES
SMEHHMSHGE NYSSNAADDY MEEDFPEQWA QPHKVGGGSG RAGTGHGAGP DHSHRMSGVE
RTNAASNGDA DAGIFHDDYH FEM
//
