ID A0A091IYZ2_EGRGA Unreviewed; 1192 AA.
AC A0A091IYZ2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=Z169_12329 {ECO:0000313|EMBL:KFP13924.1};
OS Egretta garzetta (Little egret).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP13924.1, ECO:0000313|Proteomes:UP000053119};
RN [1] {ECO:0000313|EMBL:KFP13924.1, ECO:0000313|Proteomes:UP000053119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP13924.1};
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR EMBL; KK501297; KFP13924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091IYZ2; -.
DR STRING; 188379.A0A091IYZ2; -.
DR Proteomes; UP000053119; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFP13924.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053119};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFP13924.1}.
FT DOMAIN 1..249
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 879..1166
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 266..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..298
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP13924.1"
FT NON_TER 1192
FT /evidence="ECO:0000313|EMBL:KFP13924.1"
SQ SEQUENCE 1192 AA; 135487 MW; 4CF4ECCEF6582DFC CRC64;
QGRHVKTGQL AAIKVMNVTE NEEEEIKLEI NMLKKYSHHR NIATYYGAFV KKSPAGQDDQ
LWLVMEYCGA GSVTDLVKKT KGNCFKEDWI AYICREVLRG LAHLHAHHVI HRDIKGQNVL
LTENAEVKLV DFGVSAQLDR TIGRRNTFIG TPYWMAPEVI ACEENPDSTY DYRSDLWSLG
ITAIEMAEGA PPLCDMHPMR ALFLIPRNPP PKLKSRKWSK KFLNFVESCL VKNYLHRPST
ETLLKHSFIR DMQNERQVRI MLKDHLDRTR KKKGEKEETD YDYSGSEEED DELNEDEGEP
SSIVNLPGES TLRREFLRLQ QENKNRSDPH RQQQQLKDQE KYKKQLLTER QKRIEQQKEQ
RRRLEDHQRR EQELRRQQEC EQRWPEAKAI QRKEERCKED KRAVEDERFI VEGQRKAEKK
QKVEDVQHNR KVHRTLPKDQ TQLLSLQHDH KQKKKEPSKS SNSAVHPPSS STSKEAEDRK
KKSDSIQPSL QWPAVLGHEA MPHARMGSGS SSSPCTPAPQ RAVLVQCENF RASKDVYHSS
SLSDMVTTPL SPVQDDVFWN MSHNEEQPPK VPERTTSKFY SRDQPGHQRC LSSNTHQSSP
GEHALKLNSS STSGNKQWEM GSHQSSRSTS GNPGPAKAEN ALSQNHLQLH KKSEKVSHPG
QIASPGSFAK GKDSASSFVK AADYSSSSDE VSSSDEDDTN HTRQLLSSRV ADFSRTRVPD
GIELKPQSTA AEQKDQILGK QISSTQEGLW SINNQNYLLP DLLQQSQISD SSVNPPKVPL
TSQEPQNKPL NKTPCTESTS SKSSTSSTAS FTSFIDPRLL PIPPPTSPVG PSCSSPSSAK
PEPVRRENAR KGSVVNVNPT NIRPQSDSPE IRKYKKKFNS EVLCAALWGV NLLVGTENGL
WLLDRSGQGR VYSLITRRRF QQMDVLEGLN VLITISGKKN KLRVYYLSWL RNKILRNDPE
VEKRQGWVSV GDLEGCVHYK VVKYERIKFL VIALKNSVEV YAWAPKPYHK FMAFKSFTSL
HHKPLSVDLT VENGQRLKVI YGSLVGFHAI DVDSGSVYDL YLPTHIQGTI RPHAIIILPN
TSGMELLLTY EDEGIYIDIY GHFTKETVLQ WGEMPASVAY LQSNQVMGWG EKAIELRSVE
TGNLEGVFMH KKAQKLKFLC ERNDKVFFAS VQSGGSSQIY FMTLGQNVLF NW
//
