ID A0A091LQR9_CARIC Unreviewed; 776 AA.
AC A0A091LQR9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Serine/threonine-protein kinase N2 {ECO:0000313|EMBL:KFP60812.1};
DE Flags: Fragment;
GN ORFNames=N322_04435 {ECO:0000313|EMBL:KFP60812.1};
OS Cariama cristata (Red-legged seriema).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP60812.1, ECO:0000313|Proteomes:UP000054116};
RN [1] {ECO:0000313|EMBL:KFP60812.1, ECO:0000313|Proteomes:UP000054116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP60812.1};
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; KK504349; KFP60812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091LQR9; -.
DR Proteomes; UP000054116; 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:KFP60812.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054116};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:KFP60812.1}.
FT DOMAIN 6..87
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 88..168
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 542..776
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 571
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:KFP60812.1"
FT NON_TER 776
FT /evidence="ECO:0000313|EMBL:KFP60812.1"
SQ SEQUENCE 776 AA; 87634 MW; A5282731BE1B320B CRC64;
TDCPRTPDTP NSDPRFSTNN RLMALKKQLD IELKVKQGAE NMIQMYSNGS SKDRKLLATA
QQMLQDSKTK IEVIRMQILQ AVQTNELAFD NAKPVISPLE LRMEELRHHF RIEYAVAEGA
KNVMKLLGSG KVTDRKALSE AQARFNESSQ KLDLLKYSLE QRLNELPKNH PKSSIIIEEL
SLVSSPTLSP RQSVISTQNQ YSTLSKPAAL TGTLEVRLMG CQDILENVPG RSKATSITLP
GWSPNEARSS FMSRTSKSKS GSSRNLLKTD DLSNEVCAVL KLDNTVVGQT SWKPISNQSW
DQKFTLELDR SRELEISVYW RDWRSLCAVK FLRLEDFLDN QRHGMCLYLE PQGTLFAEVT
FFNPVIERRP KLQRQKKIFS KQQGKTFLRA PQMNINIATW GRLVRRAIPT VNHSGTFSPQ
APVPATGPVV DAHIPELTLP ASDSPVAKLD FELEPEPPPA PPRASSLGEI CESSSEIKAP
DVPSQAITTF DFENGRNSIV PKLQPEIICE PDAPHSDIKY TNTREPDERR SQQRFQFSLK
DFRCCAVLGR GHFGKVLLAE YKNTNEMFAI KALKKGDIVA RDEVDSLMCE KRIFETVNSV
RHPFLVNLFA CFQTKDHVCF VMEYAAGGDL MMHIHTDVFS EPRAVFYAAC VVLGLQYLHE
HKIVYRDLKL DNLLLDTEGF VKIADFGLCK EGMGYGDRTS TFCGTPEFLA PEVLTETSYT
RAVDWWGLGV LIYEMLVGES PFPGDDEEEV FDSIVNDEVR YPRFLSTEAI SIMRRV
//