ID A0A093FWE4_GAVST Unreviewed; 782 AA.
AC A0A093FWE4;
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=N328_00895 {ECO:0000313|EMBL:KFV58664.1};
OS Gavia stellata (Red-throated diver) (Colymbus stellatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gaviiformes; Gaviidae; Gavia.
OX NCBI_TaxID=37040 {ECO:0000313|EMBL:KFV58664.1, ECO:0000313|Proteomes:UP000054313};
RN [1] {ECO:0000313|EMBL:KFV58664.1, ECO:0000313|Proteomes:UP000054313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N328 {ECO:0000313|EMBL:KFV58664.1};
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; KK636415; KFV58664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093FWE4; -.
DR Proteomes; UP000054313; 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; cd14407; UBA_MARK3_4; 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:SF1; MAP_MICROTUBULE AFFINITY-REGULATING KINASE 3; 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:KFV58664.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054313};
KW Transferase {ECO:0000313|EMBL:KFV58664.1}.
FT DOMAIN 39..290
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 309..348
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 733..782
FT /note="KA1"
FT /evidence="ECO:0000259|PROSITE:PS50032"
FT REGION 353..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68
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:KFV58664.1"
FT NON_TER 782
FT /evidence="ECO:0000313|EMBL:KFV58664.1"
SQ SEQUENCE 782 AA; 87522 MW; B5B3E4FA0DC48E33 CRC64;
HTSHGDGRQE VSSRTGRSGA RCRNSIASCA DEQPHIGNYR LLKTIGKGNF AKVKLARHIL
TGREVAIKII DKTQLNPTSL QKLFREVRIM KILNHPNIVK LFEVIETEKT LYLIMEYASG
GEVFDYLVAH GRMKEKEARA KFRQIVSAVQ YCHQKHIVHR DLKAENLLLD ADMNIKIADF
GFSNEFTVGN KLDTFCGSPP YAAPELFQGK KYDGPEVDVW SLGVILYTLV SGSLPFDGQN
LKELRERVLR GKYRIPFYMS TDCENLLKRF LVLNPTKRGT LEQIMKDRWI NAGHEEDELK
PFVEPELDIS DQKRIDIMVG MGYSQEEIQE SLSKMKYDEI TATYLLLGRK SSELDASDSS
SSSNLSLAKV RPSSDLNNST GQSPHHKVQR SISSSQKQRR YSDHAGPSIP SVVAYPKRSQ
TSTTDSDLKE EGIQSRKSSS SAVAGRGIAP ASPMLGNASN PNKADIPERK KSSAVPSNNT
APGAMTRRNT YVCSERTTAD RHSVIQNGKE NSLTEMCAYA ASPASVCTTS FSSVRLRHQK
SMSMSASVHT KMMLPPIDNG ADNFRPITVP DQRTPVASTH SISSATTPDR IRFPRGTASR
STFHGQLRER RTATYNGPPA SPSLSHEATP LSQTRTRGST NLFSKLTSKL TRRLPTEYER
NGRFEGSSRN VAVDQKDENK EAKPRSLRFT WSMKTTSSMD PNDMMREIRK VLDANNCDYE
QRERFLLFCV HGDGHAENLV QWEMEVCKLP RLSLNGVRFK RISGTSIAFK NIASKIANEL
KL
//
