ID   A0AAN8NPZ5_9PEZI        Unreviewed;       786 AA.
AC   A0AAN8NPZ5;
DT   02-OCT-2024, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2024, sequence version 1.
DT   27-NOV-2024, entry version 2.
DE   SubName: Full=Serine/threonine-protein kinase Nek2 {ECO:0000313|EMBL:KAK6518700.1};
GN   Name=NEK2 {ECO:0000313|EMBL:KAK6518700.1};
GN   ORFNames=TWF506_005838 {ECO:0000313|EMBL:KAK6518700.1};
OS   Arthrobotrys conoides.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Arthrobotrys.
OX   NCBI_TaxID=74498 {ECO:0000313|EMBL:KAK6518700.1, ECO:0000313|Proteomes:UP001307849};
RN   [1] {ECO:0000313|EMBL:KAK6518700.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TWF506 {ECO:0000313|EMBL:KAK6518700.1};
RA   Palmer J.M.;
RL   Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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:KAK6518700.1}.
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DR   EMBL; JAVHJM010000002; KAK6518700.1; -; Genomic_DNA.
DR   Proteomes; UP001307849; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00180; PKc; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR050660; NEK_Ser/Thr_kinase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00248; ANK; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
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   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:KAK6518700.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:KAK6518700.1}.
FT   DOMAIN          89..388
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          628..660
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          698..730
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          430..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   786 AA;  86482 MW;  7D13E366C97D983F CRC64;
     MFLWRSRPAA EPEAAAPAPA PVAPLITTSP TSAAPLPARP VISANSISVT FSTSDFAIIK
     GTLGRIDDRT KTDGQKAGPR KLKGKDTDYE YIQHLGQGSY GNVSKVRRAK DGKIMACKTI
     DCARNPQLYD FTCREVDIWS SFKNEKYIAQ YAQDYSWNPS TKSMRLYMEF YEGGDLQKVL
     EACRADEVAI HPLVATYWAT EIARGLKNCH DRGVVHKDLK PSNVLLSMPY VYNDMLWTAT
     LGENLTEKEK QLAGQFTQWL KTRSPWCHIS DFGVGKNSKG GLNGESPVSL STETTYVPPE
     CVDSAAKYTT KSNVFSLGRI LYALCQCDLP VDTPLEDIQP LPVEYPERLR ALIPRCLKTD
     PAERPTASEV VLELMESLVD FCCDNQFLKL KSNIDRQINP TRPIARTRTL SSASTLANVY
     TALNGAIADT TTTERPTSPA VLSVSDIDPI SRTGTPSQEP RKSTSSPTVK HVSLAVIPEQ
     ASPTVGPSAP PAPAQPPAKT AEELREDLVK AWHSRDINAM ERALVAGADA NTVARSWPKI
     GITTEYPLLN WTIKDGWSKM MRLLVTHGAT FDAPISDIVT KLSTQTEVKS FQNQYHPIYL
     AVFIADFGIL DFFFVEQGYN VNSQHLERGD TPLHIAVMRQ DLRVVKYLLQ KGASTEFRNE
     FGESGVHQAA RSWGTKVNPC LEYLLEVFPD GVNEVDASGN TPLHIAAKDG CLEGIKVLLR
     KGAKTTVRNE EGSTPEMLAI GRQSIAQALR EAEGLVPIKE KDEFTPEMSV GVMPVMSVLT
     NPSVVA
//