ID A0A093CWY4_TAUER Unreviewed; 775 AA.
AC A0A093CWY4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Serine/threonine-protein kinase N2 {ECO:0000313|EMBL:KFV18978.1};
DE Flags: Fragment;
GN ORFNames=N340_03302 {ECO:0000313|EMBL:KFV18978.1};
OS Tauraco erythrolophus (Red-crested turaco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV18978.1, ECO:0000313|Proteomes:UP000053661};
RN [1] {ECO:0000313|EMBL:KFV18978.1, ECO:0000313|Proteomes:UP000053661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV18978.1};
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=2.7.11.13;
CC Evidence={ECO:0000256|ARBA:ARBA00000946};
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=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KL471321; KFV18978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093CWY4; -.
DR Proteomes; UP000053661; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd08687; C2_PKN-like; 1.
DR CDD; cd11631; HR1_PKN2_2; 1.
DR CDD; cd11635; HR1_PKN2_3; 1.
DR Gene3D; 1.10.287.160; HR1 repeat; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037784; C2_PKN.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24356:SF322; SERINE_THREONINE-PROTEIN KINASE N2; 1.
DR Pfam; PF02185; HR1; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00742; Hr1; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF46585; HR1 repeat; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51860; REM_1; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207};
KW Kinase {ECO:0000313|EMBL:KFV18978.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053661};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:KFV18978.1}.
FT DOMAIN 5..86
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 87..167
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 541..775
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 452..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 570
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:KFV18978.1"
FT NON_TER 775
FT /evidence="ECO:0000313|EMBL:KFV18978.1"
SQ SEQUENCE 775 AA; 87593 MW; FC7C7724478829B1 CRC64;
DCPRTPDTPN SDPRFPTNNR LMALKKQLDI ELKVKQGAEN MIQMYSNGSS KDRKLLATAQ
QMLQDSKTKI EVIRMQILQA VQTNELAFDN AKPVISPLEL RMEELRHHFR IEYAVAEGAK
NVMKLLGSGK VTDRKALSEA QARFNESSQK LDLLKYSLEQ RLNELPKNHP KSSIIIEELS
LVSSPTLSPR QSVISTQNQY STLSKPAALT GTLEVRLMGC QDILENVPGR SKATSITLPG
WSPNEARSSF MSRTSKTKSG SSRNLLKTDD LSNEVCAVLK LDNTVVGQTS WKPISNQSWD
QKFTLELDRS RELEISVYWR DWRSLCAVKF LRLEDFLDNQ RHGMCLYLEP QGTLFAEVTF
FNPVIERRPK LQRQKKIFSK QQGKTFLRAP QMNINIATWG RLVRRAIPTV NHSGTFSPQS
PVPATGPVVD AHIPELTLPT SDSPVAKLDF ELEPEPPPAP PRASSLGEIS ESSSEVKAPD
VPSQAITNFD FENGRNSIVP KLQPEIICEP DAPHPDVKYT NTREPEDRRS QQRFQFNLKD
FRCCAVLGRG HFGKVLLAEY KNTNEMFAIK ALKKGDIVAR DEVDSLMCEK RIFETVNSVR
HPFLVNLFAC FQTKDHVCFV MEYAAGGDLM MHIHTDVFSE PRAVFYAACV VLGLQYLHEH
KIVYRDLKLD NLLLDTEGFV KIADFGLCKE GMGFGDRTST FCGTPEFLAP EVLTETSYTR
AVDWWGLGVL IYEMLVGESP FPGDDEEEVF DSIVNDEVRY PRFLSTEAIS IMRRV
//
