ID A0A093C1J4_9AVES Unreviewed; 2023 AA.
AC A0A093C1J4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=N339_01172 {ECO:0000313|EMBL:KFV09845.1};
OS Pterocles gutturalis (yellow-throated sandgrouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; Pterocles.
OX NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV09845.1, ECO:0000313|Proteomes:UP000053149};
RN [1] {ECO:0000313|EMBL:KFV09845.1, ECO:0000313|Proteomes:UP000053149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV09845.1};
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; KL237500; KFV09845.1; -; Genomic_DNA.
DR Proteomes; UP000053149; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20814; CRIK; 1.
DR CDD; cd05601; STKc_CRIK; 1.
DR Gene3D; 1.10.287.1490; -; 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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR017405; Citron_Rho-interacting_kinase.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR037708; CRIK_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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 Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF038145; Citron_Rho-interacting_kinase; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 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, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFV09845.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053149};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 71..334
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 335..405
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1363..1412
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1444..1564
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1592..1882
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 349..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1325..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1908..2023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 417..1213
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1259..1293
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1914..1929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1953..2001
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
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:KFV09845.1"
FT NON_TER 2023
FT /evidence="ECO:0000313|EMBL:KFV09845.1"
SQ SEQUENCE 2023 AA; 231983 MW; DAF7D5F267CFA36A CRC64;
LLFFFQGKPL FVTQQQMSPL SREGILDSLF VLFEECRNPA LMKIKHVGNF VKKYAETIAE
LRELQPSVKD FEVKSVVGCG HFADVKVVRE KVTGDVYAMK VMSKESLLAQ EHVSFFEEER
SILSQSTSPW IPQLQYAFQD KKNLYLVMEY QPGGDLLSLL NRYEDQLDES MVQFYLAELV
LAIHSVHQMG YVHRDIKPEN VLIDRTGHIK LVDFGSAAKM TVNRMVNAKL PVGTPDYMAP
EMLTGLNGDG KASYGPECDW WSLGVIAYEM IYGRSPFTEG TSAKTFNNIM NFQRFLKFPE
DVKVSSEFLD LIQSLLCGQK ERLGYEGLCC HPFFSKIDWN NIRNSPPPFV PTLKSDDDTS
NFDEPEKNSR VLSSTRQLNP AGFSGEDLPF VGFSFIKALG ILRSESVFSS VDSPAKVNSM
EKKLLLKSKE LQDAQDKCHK MEQEMTRLHR RVSEVEAVLS QKEVELKASE TQRSLLEQDL
ATYITECSSL KRSLEQARME VSQEDDKALQ LLHDIREQSR KLQEIKEQEY QAQVEEMRLM
MNQLEEDLIS ARRRSDLYES ELRESRLAAE EFKRKATECH NKLQKVKDQG KSEAGELYCK
LEKINTEQQA KIQELQEKLT KAVKASSEAT ELLQNIRQAK ERAEKELEKL QNREDSNESM
KKKLLEAEER RHSLENQVKR LETVERRENR LKEDIQTKSQ QIQQMAEKIL ELEEKHREAQ
IAAQHLELQL KQKEQFYEEK LKVLENQMKK DLADKEALEN MLRRHEEEAR EKCKVLAEQK
AMINAMDSKI RSLEQRIVEL SEANKLAANS SLFTQRNMKA QEEMISELRQ QKFYLETQAG
KLEAQNRKLE EQLEKMSHQD HTDKNRLLEL DTRLREVSLE HEEQKLELKR QLTELQLTLQ
ERESQITGLQ AARTALENQL REAKTELEET TAEAEEEIQA LTAHRDEIQR KFEALRNSCT
VITDLEEQLN QLSEDNAELN NQNFFLSKQL DEASGANDEV VQLRSEVDHL RREITEREMQ
LTSQKQTMEA LKTTCTMLEE QVMDLEALND ELLEKERQWE AWRSVLGDEK 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 RKEASTPEEY SRRLKERMHH NIPHRFNVGL NMRATKCAVC
LDTVHFGRQA SKCLECQVMC HPKCSACLPA TCGLPAEYAT HFSEAFCRDK MNSPGLQLKE
PSSSLRLEGW MKVPRNNKRG QQGWDRKYIV LEGTKVLIYD AEAREAGQRP LEEFELCLPD
GDVTVHGAVG ATELTNTAKT DVPYILKLES HPHTTCWPGR TLYLLAPSFP DKQRWVTALE
SIVAGGRVSR EKAEADAKLL GNSLLKLEGE DRLDINCTMP FSDQVVLVGA EEGLYALNVL
KNSLTHIPGM GAVFQIHLIK DLEKLLMIAG EERALCLVDV KKVKQSLAQS HLPAQPDISP
NVFETVKGCH LFAAGKVENG LCICAAMPNK VVVLRYNESL SKFCIRKEIE TSEPCSCIHL
TAYSIIIGTN 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 DESSRGRLPV SGARTPLAQV NKV
//
