ID A0A317UT22_9EURO Unreviewed; 1219 AA.
AC A0A317UT22;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Serine/threonine protein kinase chk2 {ECO:0000313|EMBL:PWY64278.1};
GN ORFNames=BO70DRAFT_391058 {ECO:0000313|EMBL:PWY64278.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY64278.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY64278.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY64278.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CHEK2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005575}.
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:PWY64278.1}.
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DR EMBL; MSFL01000065; PWY64278.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317UT22; -.
DR STRING; 1448321.A0A317UT22; -.
DR VEuPathDB; FungiDB:BO70DRAFT_391058; -.
DR OrthoDB; 20430at2759; -.
DR Proteomes; UP000247233; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd11042; CYP51-like; 1.
DR CDD; cd05117; STKc_CAMK; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
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:SF22; DNA DAMAGE RESPONSE PROTEIN KINASE DUN1; 1.
DR PANTHER; PTHR44167; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK-RELATED; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00067; p450; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 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}; Heme {ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Kinase {ECO:0000313|EMBL:PWY64278.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000247233};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:PWY64278.1};
KW Transferase {ECO:0000313|EMBL:PWY64278.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 647..666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 678..701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 713..734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 746..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 182..234
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 273..538
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1157
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 1219 AA; 138052 MW; 405CC809A10D21E9 CRC64;
MAPQNEKSSL KRGRASTDND SQHLKKPRCS ERIDFQNKPR AIDNELYLPT PVTQKDSTAT
DVIEETTTTP NTFNQISPRY TPSNSENFQT SPPAGDTQAL SQFVYPPRAF ADEVEDEAAE
GVWGYLIPLD DKVQHALVLR KRGNCEERKH PGSMARSRTE ARNKSTEIAD RQGPVSQIPG
GYLIGRHHEC DLVLNIPTIS NRHFLVFPEN RRGDSIAMLG DLSSNGTFVN DAIVGRNKHR
ELEDGDEITI LDEARFIFRY PRARDTNRFR QQYRILQQLG KGHFATVYLC VERATGTQYA
VKVFEKRSSD SQRPQTDTLQ QEVGLLMGVS HPNLLCLKDT FDESDGVYLV LELAPEGELF
NVIVSRQKFT ESETRHIFIQ LFEGLKYLHD RGIVHRDIKP ENILIVDKSL TVKLGDFGLA
KIIGEDSFTT TLCGTPSYVA PEILEDSLRR KYTKAVDIWS LGVVLYICLC GFPPFSDELY
TSEHPYTLAQ QIKSGRFDYP SPYWDSVGDP ALDLIDRMLK VDVNKRITVD NCLEHPWLKG
NYPSASDSTE GLSGALERLD FSKRKLARER TLLSYINDVL HVEQKQGSSA PVRVFHKNDA
GKRVHNHPAK GKQQREASPD ENSTPQQFLN LGERGDPVLF ENKPPPLGIM KLIRILYLYF
PIFHLSIKHN NAQPTLYLLP YTLVAIRSCY CAIMGFLAII LNDLYKFCSD FSTLGIFGIG
LFSLLALSIT INIVKQLVFK NPNEPPLVFH WLPFIGSTIS YGMEPYKFFF DCRAKYGDIF
TFVLLGKKTT VYLGTRGNDF ILNGKLRDVC AEEVYSPLTT PVFGRHVVYD CPNSKLMEQK
KFVKFGLTSD ALRSYVRLIT NEVDDFVENS AAFQGPNGVF DVCKTIAEIT IYTASRSLQG
KEVRNRFDST FAELYHDLDM GFAPINFMLP WAPLPHNRKR DAAQRKMTET YMEIIRQRRM
GGNEKDSEDM VWNLMSCSYK NGTPVPDEEI AHMMIALLMA GQHSSSSTAS WIVLQLAMHP
DIMEELYSEQ IRVLGSDLPP LTYENLQKLD LHAKVIKETL RIHAPIHSII RAVKNPMPVD
GTPYVIPTSH NVLSSPGVSA RSEDYFPNPL KWNPHRWDET IAANAEEDEE EIDYGYGLVS
KGTNSPYLPF GAGRHRCIGE QFAYVQLGAI TAALVRLFKF RNLPNFKDIP ETDYSSLFSK
PAGKSVIQFE RRAPVTNSR
//
