ID A0A087VBK5_BALRE Unreviewed; 1538 AA.
AC A0A087VBK5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=N312_02281 {ECO:0000313|EMBL:KFO09997.1};
OS Balearica regulorum gibbericeps (East African grey crowned-crane).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO09997.1, ECO:0000313|Proteomes:UP000053309};
RN [1] {ECO:0000313|EMBL:KFO09997.1, ECO:0000313|Proteomes:UP000053309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO09997.1};
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};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL487168; KFO09997.1; -; Genomic_DNA.
DR Proteomes; UP000053309; Unassembled WGS sequence.
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-KW.
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: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; 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; PS50011; PROTEIN_KINASE_DOM; 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};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFO09997.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053309};
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 1..150
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 151..221
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 818..868
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 888..1007
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1033..1305
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1377..1390
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 311..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1410..1538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 515..627
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 721..748
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 447..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1487..1501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1502..1538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO09997.1"
FT NON_TER 1538
FT /evidence="ECO:0000313|EMBL:KFO09997.1"
SQ SEQUENCE 1538 AA; 173938 MW; 1FC013F5AA1DDE2F CRC64;
EMCFICRDIK PDNILMDMNG HIRLADFGSC LKLMEDGTVQ SSVAVGTPDY ISPEILQAME
DGKGKYGPEC DWWSLGVCMY EMLYGETPFY AESLVETYGK IMNHKERFQF PAQVTDVSES
AKDLIRRLIC SREHRLGQNG IEDFKNHPFF AGIDWDNIRN CEAPYIPEVS SPTDTSNFDV
DDDCLKNSET MPPPSHTAFS GHHLPFVGFT YTSSCVLSDR SCLRLTAGPP SMDLDASIQR
TLEDSLATEA YERRIRRLEQ EKLELSRKLQ ESTQTVQALQ YSTVDGPITA SKDLEIKSLK
EEIEKLKKQV TDSGQLEQQL EEASTARREL DDASRQIKAF EKQVRTLKQE REDLNKELAD
SSDRLKSQAK ELKDAHSQRK LAMQEFSEMN ERLTDLHSQK QKLARQLRDK EEEMEVVMQK
VESLRQELRR TERLKKEVSV QAEAAAAEAS KDRKLRERSE QYSKQLESEV EGLKQKQVGR
SPGVSSIEHQ QEITKLKADL EKKSVFYEEE LSKREIMHAN EIKSLKKELR DAESQQLALK
KEIMILKDKL EKTRRENQSE REEFETEFKQ KYEREKLLLT EENKKLSNEL DKLTTMFERL
SMNNRQLEEE MRDLADKKES VAHWEAQITE IIQWVSDEKD ARGYLQALAS KMTEELEALR
NSSLGARATD MPWKMRRFAK LDMSARLELQ SALDAEIRAK QAIQDELNKV KASCISTECK
LQESEKKNME LLTDIERLKK ETEELRSEKG VKHQDSQNSF LAFLNAPTSA LDQFERSPSC
IPANKGRRVT DHPPRSIHTP TMRTAYIGSG LSAPKPKAHQ FVVKSFNTPT KCNQCTSLMV
GLIRQGCTCE VCGFSCHVTC ADKAPAVCPI PPEQTKGPLG IDPQKGIGTA YEGHVRVPKP
AGVKKGWQRA LAVICDFKLF LYDVAEGKAS QPSVIVSQVI DMRDEEFSVS SVLASDVIHA
NRKDIPCIFR VTASQLSASS NKCSILILAD GENEKSKWVG VLNELHRILK KNKLKDRSVY
VPKEAYDSTL PLIKTTQSAA IIDHERIALG NEEGLFVVHV TKDEIIRVGD NKKVHQIELI
PNEQLIAVIS GRNRHVRLFP MAALDGRETE FYKLAETKGC QSIVSGHVRH GALTCLCVAM
KRQVLCYELN QSKTRHKKIK EIQVQGNVQW MSIFSDRLCV GYQSGFLKYP LHGEGSPYSL
LHPDDHTLSF ISQQPTDAIC AVEISNKEYL LCFSSVGVYV DCQGRRSRQQ ELMWPATPSS
CCYNAPYLSV YSENAIDIFD VNSMEWIQTI PLKKVRPLNT EGSLNLLGLE TVRLIYFKNK
MAEGDELVVP ETSDNSRKQM VRNINNKRRY SFRVPEEERM QQRREMLRDP EMRNKLISNP
TNFNHIAHMG PGDGIQILKD LPMNLRPQES RTVFSGSVSI PSITKSRTEP GRSMSASSGL
AARSSAQNGS ALRREFSGGS YGAKRQPMAS PSDGSLSSGG LDQGSDAPTR DYEREDSDSP
RHSTASNSSN LSSPPSPVSP HKTKSLSLES SDHVSWDS
//
