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Database: UniProt
Entry: A0A0A0ANW0_CHAVO
LinkDB: A0A0A0ANW0_CHAVO
Original site: A0A0A0ANW0_CHAVO 
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
//
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