ID A0A093CAP4_9AVES Unreviewed; 1025 AA.
AC A0A093CAP4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=N339_02704 {ECO:0000313|EMBL:KFV11478.1};
OS Pterocles gutturalis (yellow-throated sandgrouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; Pterocles.
OX NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV11478.1, ECO:0000313|Proteomes:UP000053149};
RN [1] {ECO:0000313|EMBL:KFV11478.1, ECO:0000313|Proteomes:UP000053149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV11478.1};
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};
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DR EMBL; KL240144; KFV11478.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093CAP4; -.
DR Proteomes; UP000053149; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0035091; F:phosphatidylinositol binding; 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; cd02677; MIT_SNX15; 1.
DR CDD; cd05576; STKc_RPK118_like; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR035053; STK_RPK118-like.
DR PANTHER; PTHR15508; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR15508:SF2; RIBOSOMAL PROTEIN S6 KINASE DELTA-1; 1.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00745; MIT; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF116846; MIT domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50195; PX; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFV11478.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053149};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..98
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 743..1017
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 148..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV11478.1"
FT NON_TER 1025
FT /evidence="ECO:0000313|EMBL:KFV11478.1"
SQ SEQUENCE 1025 AA; 113622 MW; CF14ED4BEAE5BFDC CRC64;
QIVSRKNPED VQEIVVWKRY SDFKKLHKEL WQIHKNLCRH TELFPPFAKA IVFGRFDETV
IEERRQCAED LLQFSANIPA LYNSKQLEEF FKGGEVHDGS ELIGPVEPAS DSLADNLSDC
SSEGISSDSD LISLTVDVDS LAELEDGMAS NQSSPSRAVG LCPASEPQVQ STLAPEQEWS
KPEGERESHS LFTGSLNPKP GKQDYLEKAG ELIKLALKKE EEEDYETAFS FYRKGVDLLL
EGVQGESSPT RREAVKRKTA EYLMRAEKIS GLYQKSSEDA SVSLPPGSLS SRPSWNLRSP
AEELKAFRVL GVIDKVLLVM DTRTQETFIL KGLRKSSEYS RSRTTIIPRC VPNMVCLHKY
IISEESVFLV LQHAEGGRLW SYISKFLNRS PEESFEIPGP RTSCSTKIYL EQPTPSPKEI
GSSADSRESY GEGMLKVVPL KSSLTPSSQD DSSNAEDGQE SLKWMDSESS SEEECTTSYL
TLCNEYGQEK IDSGSLNEEP VVKMESEGLN TKERRCLQKC SVVGSDSFTS QIAPQERKLF
IDDAHSEIAS PTRIVDSLTR SKNSAMELFR IDSKDSTSEL LGLDFGEKLY NLKSEPLKPL
FSVPDHDRSL DALESKMGVR AHDTVSRGSN DSVPVISFKD AAFDDVNSVD EGRPDLLINL
PGMSDETEEA AASRPTKFTK TDRDISEVKL LETPDVLQLN NSAEPCKAFD QEPNRVAPEV
GDPSHKEAHG QSGVTQGALG TLFTSDQEVG SSEDGALFRG LGDCSLNMAS KEESLFVSNL
LSGAQDVSLE GDAIRNEAVL LFSDQTEDFG KEEADAALIP AAESKKTAAK REDKIAVAGE
KEIHQIFQDL DERLAITSRF YIPEDCIQRW AAEMVVALDA LHREGIVCRD LNPNNILLND
RGHIQLTYFS RWREVEDSCD NDAIERMYCA PEVGAILEET EACDWWSLGA ILFELLTGKT
LVECHPSGIN THTSLSIPDH VSKEARSLIQ QLLQFNPAER LGAGVAGVED IKSHPFFALI
EWADL
//