ID A0A493TW37_ANAPP Unreviewed; 1699 AA.
AC A0A493TW37;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=CDC42BPA {ECO:0000313|Ensembl:ENSAPLP00000030108.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000030108.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000030108.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000030108.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
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DR Ensembl; ENSAPLT00000040126.1; ENSAPLP00000030108.1; ENSAPLG00000012422.2.
DR GeneTree; ENSGT01030000234517; -.
DR Proteomes; UP000016666; Chromosome 3.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0043226; C:organelle; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20864; C1_MRCKalpha; 1.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01243; PH_MRCK; 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; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
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 InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF31; SERINE_THREONINE-PROTEIN KINASE MRCK ALPHA; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR Pfam; PF15796; KELK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 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 SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
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:UP000016666};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1699
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019731487"
FT DOMAIN 38..304
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 305..375
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 979..1029
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1049..1168
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1194..1466
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1538..1551
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 464..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1571..1699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 669..781
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 875..902
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1571..1615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1631..1645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1648..1662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1663..1699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1699 AA; 192986 MW; 37102E11C08C0E3A CRC64;
MFHCGFLFVC FLMVDIFLVS AKPFTSKVKQ MRLHKEDFEI LKVIGRGAFG EVAVVKLKNA
DKVFAMKILN KWEMLKRAET ACFREERDVL VNGDNQWITT LHYAFQDENY LYLVMDYYVG
GDLLTLLSKF EDRLPEDMAR FYLAEMVIAI DSVHQLHYVH RDIKPDNILM DMNGHIRLAD
FGSCLKLMED GTVQSSVAVG TPDYISPEIL QAMEDGKGKY GPECDWWSLG VCMYEMLYGE
TPFYAESLVE TYGKIMNHKE RFQFPAQVTD VSESAKDLIR RLICSREHRL GQNGIEDFKN
HPFFAGIDWD NIKNCDAPYI PEVSSPTDTS NFDVDDDCLK NSETMPPPSH TAFSGHHLPF
VGFTYTSSCV LSDRSCLRLT AGPPSMDLDA SIQRTLEDSL ATEAYERRIR RLEQEKLELS
RKLQESTQTV QALQYSTVDG PITASKDLEI KSLKEEIEKL KKQVTDSDQL EQQLEEASTA
RRELDDASRQ IKAFEKQVRT LKQEREDLNK ELAESSDRLK SQAKELKDAH SQRKLAMQEF
SEMNERLTDL HSQKQKLARQ LRDKEEEMEV VMQKVESLRQ ELRRTERLKK ELEVQAEAAA
AEASKDRKLR EKSEQYSKEL ESEVEGLKQK QVGRSPAVSY IEYQQEITKL KADLEKKSVF
YEEELSKREI MHANEIKSLK KELRDAESQQ LALKKEIMIL KDKLEKTRRE SQSEREEFET
EFKQKYEREK ILLTEENKKL SNELDKLTTM FERLSMNNRQ LEEEMRDLAD KKESVAHWEA
QITEIIQWVS DEKDARGYLQ ALASKMTEEL EALRNSSLGA RATDMPWKMR RFAKLDMSAR
LELQSALDAE IRAKQAIQDE LNKVKASCIS TECKLQESEK KNLELLTDIE RLKKETEELR
SEKANRGRCI DSVENFTLSN TPSRDEDTKS HLHSRSRSPS TASETEPIEV MDHPPRSIHT
PTMKTAYIGS GLPALKPKAH QFVVKSFNTP TKCNQCTSLM VGLIRQGCTC EVCGFSCHVT
CADKAPAVCP IPPEQTKGPL GIDPQKGIGT AYEGHVRVPK PAGVKKGWQR ALAVICDFKL
FLYDIAEGKA SQPSVIVSQV IDMRDEEFSV SSVLASDVIH ANRKDIPCIF RVTASQLSAS
SNKCSILILA DGENEKSKWV GVLNELHRIL KKNKLKDRSV YVPKEAYDST LPLIKTTQSA
AIIDHERIAL GNEEGLFVVH VTKDEIIRVG DNKKVHQIEL IPSEQLIAVI SGRNRHVRLF
PMAALDGRET EFYKLAETKG CQSIVSGHVR HGAFTCLCVA MKRQVLCYEL NQSKTRHKKI
KEIQVQGNVQ WMSVFSDRLC VGYQSGFLKY PLHGEGSPYS LLHPDDHTLS FISQQPTDAI
CAVEISNKEY LLCFSSVGVY VDCQGRRSRQ QELMWPATPS SCCYNAPYLS VYSENAIDIF
DVNSMEWIQT IPLKKVRPLN TEGSLNLLGL ETIRLIYFKN KMAEGDELVV PETSDNSRKQ
MVRNINNKRR YSFRVPEEER MQQRREMLRD PEMRNKLISN PTNFNHIAHM GPGDGIQILK
DLPMNLRPQE SRTVFSGSVS IPSITKSRTE PGRSMSASSG LAARSSAQNG SALRREFSGG
SYGAKRQPMA SPSDGSLSSG GLDQGSDAPT RDYEREDSDS PRHSTASNSS NLSSPPSPVS
PHKTKSLSLE SSDHVSWDS
//
