ID A0A0A0ANW0_CHAVO Unreviewed; 2049 AA.
AC A0A0A0ANW0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=N301_16436 {ECO:0000313|EMBL:KGL96209.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL96209.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL96209.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL96209.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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; KL872580; KGL96209.1; -; Genomic_DNA.
DR STRING; 50402.A0A0A0ANW0; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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:KGL96209.1};
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:UP000053858};
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 97..360
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 361..431
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1389..1438
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1470..1590
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1618..1908
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 1351..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1934..2049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 443..1239
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1285..1319
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1940..1955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1979..2027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 2049
FT /evidence="ECO:0000313|EMBL:KGL96209.1"
SQ SEQUENCE 2049 AA; 234756 MW; 389AB269C5E5FBAB CRC64;
MLKFKCGARN PVETGPMEPI TSRISRLNLL FQGKPLFATQ QQMSPLSREG ILDSLFVLFE
ECRNPALMKI KHVGNFVKKY AETIAELREL QPSVKDFEVK SVVGCGHFAD VKVVREKVTG
DVYAMKVMSK ESLLVQEHVS FFEEERSILS QSTSPWIPQL QYAFQDKKNL YLVMEYQPGG
DLLSLLNRYE EQLDESMVQF YLAELILAIH SVHQMGYVHR DIKPENVLID RTGHIKLVDF
GSAAKMTVNK TVNAKLPVGT PDYMAPEMLT GLNGDGKASY GPECDWWSLG VIAYEMIYGR
SPFAEGTSAK TFNNIMNFQR FLKFPEDVKV SSEFLDLIQS LLCGQKERLG YEGLCCHPFF
SKIDWNNIRN SPPPFVPTLK SDDDTSNFDE PEKNSRVLSS TCQLSPAGFS GEDLPFVGFS
FIKALGILRS ESVFSSVDSP AKVSSMEKKL LLKSKELQDA QDKCHKMEQE MTRLHRRVSE
VEAVLSQKEV ELKASETQRS LLEQDLATYI TECSSLKRSL EQARMEVSQE DDKALQLLHD
IREQSRKLQE IKEQEYQAQV EEMRLMMNQL EEDLISARRR SDLYESELRE SRLAAEEFKR
KATECHNKLQ KVKDQGKNET GELYSKLEKI NTEQQAKIQE LQEKLTKAVK ASSEATELLQ
NIRQAKERAE KELEKLQNRE DSNESMKKKL LEAEERRHSL ENQVKRLETV ERRENRLKED
IQTKSQQIQQ MAEKILELEE KHREAQIAAQ HLELQLKQKE QFYEEKLKVL ENQMKKDLAD
KEALENMLRR HEEEAREKCK VLAEQKAMIN AMDSKIRSLE QRIVELSEAN KLAANSSLFT
QRNMKAQEEM ISELRQQKFY LETQAGKLEA QNRKLEEQLE KMSHQDHTDK NRLLELETRL
REVSLEHEEQ KLELKRQLTE LQLTLQERES QITGLQAART ALENQLREAK TELEETTAEA
EEEIQALTAH RDEIQRKFEA LRNSCTVITD LEEQLNQLTE DNAELNNQNF FLSKQLDEAS
GASDEVVQLR SEVDHLRREI TEREMQLTSQ KQTMEALKTT CTMLEEQVMD LEALNDELLE
KERQWEAWRS VLGDEKSQFE CRVRELQRML DTEKQSRVRA DQRITESRQV VELAVKEHKA
EILALQQALK EQKLKAESLS DKLNDLEKKH AMLEMNARSL QQKLETEREL KQRLLEEQAK
LQQQMDLQKN HIFRLTQGLQ EALDRADLLK TERSDLEYQL ENIQVLYSHE KVKMEGTISQ
QTKLIDFLQA KMDQPAKKKK VPLQYNELKV ALEKEKARSA ELEEALQKTR IELRSAREEA
AHRKISDHPH PSTPATARQQ IIMSAIVRSP EHQPTPISLL APPSSRRKES STPEEYSRRL
KERMHHNIPH RFNVGLNMRA TKCAVCLDTV HFGRQASKCL ECQVMCHPKC STCLPATCGL
PAEYATHFSE AFCRDKMNSP GLQLKEPSSS LRLEGWMKVP RNNKRGQQGW DRKYIVLEGT
KVLIYDAEAR EAGQRPLEEF ELCLPDGDVT VHGAVGATEL TNTAKTDVPY ILKLESHPHT
TCWPGRTLYL LAPSFPDKQR WVTALESIVA GGRVSREKAE ADAKLLGNSL LKLEGEDRLD
INCTMPFSDQ VVLVGAEEGL YALNVLKNSL THIPGMGAVF QIHLIKDLEK LLMIAGEERA
LCLVDVKKVK QSLAQSHLPA QPDVSPNVFE AVKGCHLFAA GKVENGLCIC AAMPNKVVVL
RYNESLSKFC IRKEIETSEP CSCIHLTTYS IIIGTNKFYE IEMKQYTLEE FLDKNDHTLA
SAVFAASTNS FPVSIIQVNP TGQREEYLLC FHEFGVFVDS YGRRSRTDDL KWNRLPLAFA
YREPYLFVTH FNSLEVIEIQ ARASLGTPAR AHLEIPNPRY LGPAISSGAI YLASSYQDKL
RVICCKGNLV KETNNEQHHR GSSATRSSPN KRGPPTYNEH ITKRVASSPG PPEGPSHPRE
PSTPHRYREG RTELRRDKSP GRPLEREKSP GRLLSTRRER SPGRLFEESS RGRMPVSGAR
TPLAQVNKV
//