ID A0A091R6J5_9GRUI Unreviewed; 1063 AA.
AC A0A091R6J5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=N332_04781 {ECO:0000313|EMBL:KFQ34569.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ34569.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ34569.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ34569.1};
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; KK809573; KFQ34569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091R6J5; -.
DR Proteomes; UP000053369; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20814; CRIK; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR22988:SF71; CITRON RHO-INTERACTING KINASE; 1.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFQ34569.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053369};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 403..452
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 484..604
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 632..922
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 365..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2..253
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 299..333
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 954..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ34569.1"
FT NON_TER 1063
FT /evidence="ECO:0000313|EMBL:KFQ34569.1"
SQ SEQUENCE 1063 AA; 120665 MW; C85650D246C251EC CRC64;
VITDLEEQLN QLSEDNAELN NQNFFLSKQL DEATGASDEV VQLRSEVDHL RREITEREMQ
LTSQKQTMEA LKTTCTMLEE QVMDLEALND ELLEKERQWE AWRNVLGDEK SQFECRVREL
QRMLDTEKQS RVRADQRITE SRQVVELAVK EHKAEILALQ QALKEQKLKA ESLSDKLNDL
EKKHAMLEMN ARSLQQKLET ERELKQRLLE EQAKLQQQMD LQKNHIFRLT QGLQEALDRA
DLLKTERSDL EYQLENIQVL YSHEKVKMEG TISQQTKLID FLQAKMDQPA KKKKVPLQYN
ELKVALEKEK ARSAELEEAL QKTRIELRSA REEAAHRKIS DHPHPSTPAT ARQQIIMSAI
VRSPEHQPTP ISLLAPPSSR RKESSTPEEY SRRLKERMHH NIPHRFNVGL NMRATKCAVC
LDTVHFGRQA SKCLECQVMC HPKCSTCLPA TCGLPAEYAT HFSEAFCRDK MNSPGLQLKE
PSSSLRLEGW MKVPRNNKRG QQGWDRKYIV LEGTKVLIYD AEAREAGQRP LEEFELCLPD
GDVTVHGAVG ASELTNTAKT DVPYILKLES HPHTTCWPGR TLYLLAPSFP DKQRWVTALE
SVVAGGRVSR EKAEADAKLL GNSLLKLEGE DRLDINCTMP FSDQVVLVGA EEGLYALNVL
KNSLTHIPGM GAVFQIHLIK DLEKLLMIAG EERALCLVDV KKVKQSLAQS HLPAQPDVSP
NVFEAVKGCH LFAAGKVENG LCICAAMPNK VVVLRYNESL SKFCIRKEIE TSEPCSCIHL
TSYSIIIGTN KFYEIEMKQY TLEEFLDKND HTLASAVFAA STNSFPVSII QVNPTGQREE
YLLCFHEFGV FVDSYGRRSR TDDLKWNRLP LAFAYREPYL FVTHFNSLEV IEIQARASLG
TPARAHLEIP NPRYLGPAIS SGAIYLASSY QDKLRVICCK GNLVKETNNE QHHRGSSATR
SSPNKRGPPT YNEHITKRVA SSPGPPEGPS HPREPSTPHR YREGRTELRR DKSPGRPLER
EKSPGRLLST RRERSPGRLF DESSRGRMPV SGARTPLAQV NKV
//
