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Database: UniProt
Entry: A0A093CRC8_TAUER
LinkDB: A0A093CRC8_TAUER
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ID   A0A093CRC8_TAUER        Unreviewed;       748 AA.
AC   A0A093CRC8;
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:KFV18435.1};
DE   Flags: Fragment;
GN   ORFNames=N340_02076 {ECO:0000313|EMBL:KFV18435.1};
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:KFV18435.1, ECO:0000313|Proteomes:UP000053661};
RN   [1] {ECO:0000313|EMBL:KFV18435.1, ECO:0000313|Proteomes:UP000053661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV18435.1};
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; KL469840; KFV18435.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093CRC8; -.
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; cd11637; HR1_PKN3_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; 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:SF318; SERINE_THREONINE-PROTEIN KINASE N3; 1.
DR   Pfam; PF02185; HR1; 2.
DR   Pfam; PF00069; Pkinase; 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; PS50004; C2; 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:KFV18435.1};
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:KFV18435.1}.
FT   DOMAIN          1..65
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          73..152
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          173..336
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          514..748
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         543
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:KFV18435.1"
FT   NON_TER         748
FT                   /evidence="ECO:0000313|EMBL:KFV18435.1"
SQ   SEQUENCE   748 AA;  84250 MW;  1A8B5A5E3E7509C3 CRC64;
     KVEALKKQLH VEMKVKQGAE NMIQMYSTSK ERKLLATAQQ MLQDSKTKIE IIRMHIVKVS
     QSAGGMEDTV DPAVRMGTAI SALELRIEEL RHHLRIEAAV AEGAKNVLKI LGGSRVQDRK
     FLAEAQGRLQ ESSQKIDLLR LSLERQLSEL SPEHPKRALI KQELVNTSSL GAQHGNIQPT
     SVIKPTALTG TLEVRLMGCQ DLLENVPGRS RMASSSPVCG SPSDLRSLSR PRVGLGIHGR
     SVAGKYLRNE EPCNEVLAVL KVDNKVVGQT NWGPVNNQAW DQSFVIELDR SRELEIAIYW
     RDWRELCAVK FLRLDDFLDN ERHGMCLSLE PQGMLFAEVM FCNPVIERKP KLQRQRRIFP
     KQKGKEFLRA PQMNINVAAW GRLMMSFLPP CSSLSTLSPP LHDPIHTAFS PVPPQSHVDS
     MSKLSSGFPV AKLTFADEAP PKPPRLASLG EPELVLLLPV EMKVRLLPLG AVSSPVRVRK
     VRVTHSFLQW QNSSIKPNSS GFQPRKRTVH LEDFHCIAML GRGHFGKVLL AQYKPTGKLY
     AIKALKKKDI IRRDEIDSLN CEKRIFEVVN SSDHPFLVNM FACFQTPHHA CFVMEYTPGG
     DLMMRIHEDV FPEHMAQFYT ACVVLGLQFL HEKKIIYRDL KLDNLLLDAE GFVKIADFGL
     CKEGIGFGDR TNTFCGTPEF LAPEVLTDIS YTRAVDWWGL GVLIYEMLVG ESPFPGDDEE
     EVFDSIVNDE VRYPRFLSSE ALSIIRKV
//
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