ID A0A091SCS7_NESNO Unreviewed; 777 AA.
AC A0A091SCS7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN ORFNames=N333_00681 {ECO:0000313|EMBL:KFQ55426.1};
OS Nestor notabilis (Kea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ55426.1, ECO:0000313|Proteomes:UP000053840};
RN [1] {ECO:0000313|EMBL:KFQ55426.1, ECO:0000313|Proteomes:UP000053840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ55426.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC {ECO:0000256|ARBA:ARBA00004279}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000256|ARBA:ARBA00006234}.
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DR EMBL; KK947287; KFQ55426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091SCS7; -.
DR Proteomes; UP000053840; Unassembled WGS sequence.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd12196; MARK1-3_C; 1.
DR CDD; cd14072; STKc_MARK; 1.
DR CDD; cd14405; UBA_MARK1; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR049508; MARK1-4_cat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF21; SERINE_THREONINE-PROTEIN KINASE MARK1; 1.
DR Pfam; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF103243; KA1-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50032; KA1; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:KFQ55426.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053840};
KW Transferase {ECO:0000313|EMBL:KFQ55426.1}.
FT DOMAIN 43..294
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 312..352
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 728..777
FT /note="KA1"
FT /evidence="ECO:0000259|PROSITE:PS50032"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ55426.1"
FT NON_TER 777
FT /evidence="ECO:0000313|EMBL:KFQ55426.1"
SQ SEQUENCE 777 AA; 87144 MW; A88F25B37A75DCF3 CRC64;
HTSVDGYTEP HVQPIKSSSR QNIPRCRNSI TSTNEEHPHI GNYRLLKTIG KGNFAKVKLA
RHVLTGREVA VKIIDKTQLN PTSLQKLFRE VRIMKILNHP NIVKLFEVIE TEKTLYLVME
YASGGEVFDY LVAHGRMKEK EARAKFRQIV SAVQYCHQKC IVHRDLKVEN LLLDADMNIK
IADFGFSNEF TVGNKLDTFC GSPPYAAPEL FQGKKYDGPE VDVWSLGVIL YTLVSGSLPF
DGQNLKELRE RVLRGKYRIP FYMSTDCENL LKKLLVLNPI KRGSLEQIMK DRWMNVGHEE
EELKPYTEPE PDFNDTKRID IMVTMGFSRE EIHESLVNQK YDEVMATYLL LGRKPPEFEG
GESLTSSNLG QRSRPSSDLN NSSVQSPAHL KVQRSISTNQ KQRRFSDHVG PSIPPAVSYT
KRAQANSVES EQKEDWDKDV SRKLSSTTVG SKSEMTASPL VGPERKKSTT VPSNNVFSGS
GMTRRNTYVC ERSSDRYSAI QNGKDNSLTE MSASSTSSAG SAVASAVSTR PRHQKSMSAS
GHPIKVTLPT IKDGTEAYRP SATQRVPAAS PSAHSISTTT PDRTRFPRGS SSRSTFHGEQ
LRERRNATYN GPPASPSHET GAFAHARRGT STGIISKITS KFVRRDPSEG EASGRTDTSR
SASGEPKDRE KEDSKDSKPR SLRFTWSMKT TSSMDPNDMM REIRKVLDAN NCDYEQKERF
LLFCVHGDAR QDSLVQWEME VCKLPRLSLN GVRFKRISGT SIAFKNIASK IANELKL
//
