ID A0A175W717_9PEZI Unreviewed; 1617 AA.
AC A0A175W717;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=MMYC01_203651 {ECO:0000313|EMBL:KXX78754.1};
OS Madurella mycetomatis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX78754.1, ECO:0000313|Proteomes:UP000078237};
RN [1] {ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA van de Sande W.W.J.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KXX78754.1, ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA Van De Sande W.;
RT "Madurella mycetomatis genome sequencing.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KXX78754.1}.
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DR EMBL; LCTW02000109; KXX78754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175W717; -.
DR STRING; 100816.A0A175W717; -.
DR VEuPathDB; FungiDB:MMYC01_203651; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000078237; 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; cd00773; HisRS-like_core; 1.
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:SF197; EIF-2-ALPHA KINASE GCN2; 1.
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; 1.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00220; S_TKc; 2.
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}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KXX78754.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000078237};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 39..149
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 263..539
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 587..964
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..731
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 819
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 593..601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 616
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 617
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1617 AA; 181310 MW; 60EA476695268E41 CRC64;
MAPKKPVQTT KKNVRDSFPG LKGPGDGASK THYQELQENE VMVLQAIYGD DFTQHSATHT
AWKKSEPSFD IKIKASTDDE LAVTLGVVLV ATYPKSPPLL SIKDGGDVRE STRFKIQKFV
ETQPRIWAQE EQEMIDRIVE GIREILEEAA LKKAQGLELP SLEEERAAHE AELAKLAQDE
KELEERKKLE ETKEEERVLG DMVQEELKRQ RTKAKESRKK NKTQRLSPDR AADDPLATDV
AVVFDQPCKL TDGSGNALYF QTVIGRTVYR EGPVTTVYKV KPVLSARNVR PSLALKQVEL
KYHGKDSVQF KKQLQALEVQ LESLKKLHHQ NLLAVIDFKI DRSISETDSS SPAVWSMSVL
SLLSDKGPLD ELLELAGQID ISKAKIWTVD LLDALAFLHN NGVVHQDIHP GNVLLYREPA
GDIVPKLADA GYQRELHNIC TKVATLTATR AAKSAYWFPP EIASVSKPQY TQKTDVWDFG
IVFLQMLFGL DVPDKYHSPS ALMESLSLSD PLEELVAKFF KSDPKKRPRA FELCSSEFLA
TNAPILAEDE SAVVGGSFIS APQTVPRRVR HDSMNRSAVS SRYLQDYVEE ARLGKGGFGE
VVRARKMIDG RLYAIKKITQ RSHETLSEML KEVRMLSQMN HPAVVRYYNT WLEEVPDFSD
AEGDTSTEGP ATEASRDTIS RKIDIEFAES KSRGLDFMSS SGHPYIEFGY DSAIEDDDDE
EEGDDQGGDG NSSSDEDTST TDDRVPRDHL AIRGQRTRMG STRPFRTIMY ISMEYCEKRT
LRDLISRNLY KDAQEIWRLF RQILEGLVHI HSLNIVHRDL KPENVFISAS PDGVENVKIG
DFGLATSGQL AIEKNMPNLD SSDITRSIGT AVYVAPEVRT GGSGSYTAKV DMYSLGVIFF
EMSYPPMLGM QRAQVLEQVR RSPPLLPSDF KPSDKNHADI LLSLLNHNPK ERPSSAELLK
SGMMPVQMES EAIRRAIAGM ADPSSPYFQK MLRTLFDRQI EQAKDYAWDM SSSGPNPADL
MRRFVVKDTL ISIFRRHGAV EAPTACLYPR SPHYSKNAVH LLDRNGTVLQ LPFDLTMGHA
RSLARITNGQ VPQRSYSFGN IFRDRHDGGQ PDVYGEVDFD IVTTDALDLA LKEAEVIKVL
DEIVTAFPTT SSTPICFQLG HSDLLHLILE YCGVEVGARQ AAAEVLSKLN IRNFTWQKVR
SELRSPAVGI SATSVDELQR FDFRDTPSKA IAKLRNLFEG TEYHQRVSST LAHLREVYEY
TKKFGVCSKI YIAPLSSLNE AFFRGGILFA CLYDKKVKDV FAAGGRYDSL IKEHRPKIGG
RFEERHAVGF SLNWEKQLAK QVPKTTGKAF LKKAVEEETQ GIFSTKRCDV LVASFDPSVL
RSSGIELVQT LWAHGISAEL ARDARSPEDL LTTYRDESYS WIIIIKQDNM LKIKTMGRKD
APDADIAAKE LLNWLKSEIR DRDSRSGMKF RSTTGIPHSE SANSAAGMSG AGPGEHEPQD
VHVLVAQTKS KKFNRRAVVE QAQASASRLV QTFLEGPIAA IETSDAVVDM IRSTSLSDPE
SWRRVEHGVG TAEKKYVREI HDMLKAWRWD WEAKRGPGHA FVYNFRTGKC IYYDLGA
//
