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Database: UniProt
Entry: A0A091LQR9_CARIC
LinkDB: A0A091LQR9_CARIC
Original site: A0A091LQR9_CARIC 
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
//
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