ID C5FVW9_ARTOC Unreviewed; 1591 AA.
AC C5FVW9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=MCYG_06872 {ECO:0000313|EMBL:EEQ34053.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ34053.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS995706; EEQ34053.1; -; Genomic_DNA.
DR RefSeq; XP_002844908.1; XM_002844862.1.
DR STRING; 554155.C5FVW9; -.
DR GeneID; 9227951; -.
DR VEuPathDB; FungiDB:MCYG_06872; -.
DR eggNOG; KOG1035; Eukaryota.
DR HOGENOM; CLU_001222_2_0_1; -.
DR OMA; EFYHRSG; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000002035; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IEA:InterPro.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR CDD; cd14012; PK_eIF2AK_GCN2_rpt1; 1.
DR CDD; cd14046; STKc_EIF2AK4_GCN2_rpt2; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR016255; Gcn2.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR024435; HisRS-related_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF12745; HGTP_anticodon2; 1.
DR Pfam; PF00069; Pkinase; 3.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF000660; Ser/Thr_PK_GCN2; 2.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50908; RWD; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000660-
KW 2}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEQ34053.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002035};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 39..148
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 262..534
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 574..945
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..226
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 7..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 792
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 580..588
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 603
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 604
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1591 AA; 179731 MW; B35D37CF09E73C38 CRC64;
MPRKQRKGST KTNGSPVEDK QKTASNQALA TNYEEIHKNE ADALRSIYGD EFEDVETKPS
AWNQSSTISF KLQLKASSNP EVRVCLLVEL PTTYPKSIPI LKLESVQDVR HSARQRLEDV
LKSKPVELLG SEMIYELAVA IEDVLEDSAQ AQAQDKDLPS LEEERIVQEA AALQQAEKLK
QEELARQQEA SVEEEKSLQL LVEDKLKQRQ RENEQLSRRK SRTNADDFGL LESAVDVPGS
ISFDPPMTIT DLHDRPLLFK SVSGKNILGK SHYKETFLVR PNVLGNTPLV PLLVLKEIFI
HESESKSIDL RFQISLSEDK LEFLKKLRHP NLVDFIGFKI QRPIESFTGQ AGTWHIYALF
EHANKGSLSE LLDIVGGVPA ENVRAWMIQL VEALEYYNRH GVVHGNIHSG RVLLFRSPSS
TTTVKLLGNV EEVLPLSSTA RRRSLTTPKS PFWLPPELAG EGMKPTIKTD VWDLGILFLQ
MGFGKDILQR YTSADAVINS IDLSPQLEDM LVEIFRSDPK KRPTPFQIQP FEFFRVDTPL
VIPVGTPGSS SLPNRTRHDS QGHLAAVSRY SHDFDEVGRL GRGGYGLVVK ARNKLDGRFY
AVKKISQKSP VALKDTLSEI MLLSRLNHPY VVRYFTAWLE ENYGAVDDED DSDAVLSSEG
SSSHSGDNIE FGYSTSGLDF ISSSGYPKVE FGYDTDEEAE SDTISDGTGV QKKGGDASTT
EERLSLRRIR SGSQSRAIPT TLFIQMEYCE KHTLRDLIRY GLHENIDSSW RLFRQILDGL
NHIHSHGILH RDLKPDNIFI DMANNPRIGD FGLATSGQLS STDRSSALES IGGGFTQSIG
TTYYVAPEVK KASMGQYNEK VDMYSLGIIF FEMCYPLETG MERDRTLQDI RQKQHTLPEA
FNLPEKVAQG EIILSLISHR SSERPTTTEL LQSDKIPLQV EEEMFRKAVM GLLSDPNSPD
YKKILSAIFS QPRKKFEDIA WDMDSRTSPT ATELLLHGMI KDRLTSLFRK HGAVETSRQS
LFPRSSHYGP GAVRLLDPGG NLVQLPYDLT LPNARALPKQ DLSVEKAFSF GTVYRESIHR
GEPRGHKEVD FDIVSYNTLD LPLKEAEVIK VLDEIIDEFP PLKASQMCFH INHSDLLEAV
VGFCRITPEQ RPIVKEVISK LNIGQYTMQR IRSELRSPSI GVPSTSIDDL SRFDFRDTPE
KALSRLHAIM DGTEYADRLS PIFNRLNMLV SYLEKFKVKR KVYISPLSSL NDKFYNGSIL
FQCVFDKKRR DVFAAGGRYD SLIQEFQPSL RSNRPRSHAV GFNLGLDKLN GSMTNYLKGS
NKAFLKPDAE VGNIWRRNKC DVLVASFDPS VLRTVGVGIV STLWANDISA ELAADTTPSL
EDLLTRYVDD NYSWVVIVKQ DSIERGLRVK SVQRKEDFDV RSSDLVPWLR NEMRARKKFK
HDRPPESPKL IKHPSQSEAI LSSKERDPEV RILTPLHKNK KTNRRNIVEF ALRRSREVLD
KGLDGPIAAI DIRDDVLESI RDTRLSDPDS WRNAIQSAPL VERKYLGNIH ELLMDLASES
VAQDGTVKYS NAFVYNYRTG NCIYYDLKRG N
//
