ID A0A091UKQ4_PHORB Unreviewed; 1350 AA.
AC A0A091UKQ4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=N337_00828 {ECO:0000313|EMBL:KFQ90275.1};
OS Phoenicopterus ruber ruber.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Phoenicopteriformes; Phoenicopteridae;
OC Phoenicopterus.
OX NCBI_TaxID=9218 {ECO:0000313|EMBL:KFQ90275.1, ECO:0000313|Proteomes:UP000053700};
RN [1] {ECO:0000313|EMBL:KFQ90275.1, ECO:0000313|Proteomes:UP000053700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N337 {ECO:0000313|EMBL:KFQ90275.1};
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}.
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DR EMBL; KK436096; KFQ90275.1; -; Genomic_DNA.
DR Proteomes; UP000053700; Unassembled WGS sequence.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
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 InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR031597; KELK.
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; 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 SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 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};
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:KFQ90275.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053700};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 630..680
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 700..819
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 845..1117
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1189..1202
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 257..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 327..439
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 533..560
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 257..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ90275.1"
FT NON_TER 1350
FT /evidence="ECO:0000313|EMBL:KFQ90275.1"
SQ SEQUENCE 1350 AA; 152637 MW; CB146114DA04155B CRC64;
ETMPPPSHTA FSGHHLPFVG FTYTSSCVLS DRSCLRLTAG PPSMDLDASI QRTLEDSLAT
EAYERRIRRL EQEKLELSRK LQESTQTVQA LQYSTVDGPI TASKDLEIKS LKEEIEKLKK
QVTDSGQLEQ QLEEASTARR ELDDASRQIK AFEKQVRTLK QEREDLNKEL AESSDRLKSQ
AKELKDAHSQ RKLAMQEFSE MNERLTDLHS QKQKLARQLR DKEEEMEVVM QKVESLRQEL
RRTERLKKEL EVQAEAAAAE ASKDRKLRER SEQYSKQLES EVEGLKQKQV GRSPGVSSIE
HQQEITKLKA DLEKKSVFYE EELSKREIMH ANEIKSLKKE LRDAESQQLA LKKEIMILKD
KLEKTRRENQ SEREEFETEF KQKYEREKIL LTEENKKLSN ELDKLTTMFE RLSMNNRQLE
EEMKDLADKK ESVAHWEAQI TEIIQWVSDE KDARGYLQAL ASKMTEELEA LRNSSLGARA
TDMPWKMRRF AKLDMSARLE LQSALDAEIR AKQAIQDELN KVKASCISTE CKLQESEKKN
MELLTDIERL KKETEELRSE KGVKHQDSQN SFLAFLNAPT SALDQFERSP SCIPANKGRR
VTDHPPRSIH TPTMRTAYIG SGLSAPKPKA HQFVVKSFNT PTKCNQCTSL MVGLIRQGCT
CEVCGFSCHV TCADKAPAVC PIPPEQTKGP LGIDPQKGIG TAYEGHVRVP KPAGVKKGWQ
RALAVICDFK LFLYDVAEGK ASQPSVIVSQ VIDMRDEEFS VSSVLASDVI HANRKDIPCI
FRVTASQLSA SSNKCSILIL ADGENEKSKW VGVLNELHRI LKKNKLKDRS VYVPKEAYDS
TLPLIKTTQS AAIIDHERIA LGNEEGLFVV HVTKDEIIRV GDNKKVHQIE LIPNEQLIAV
ISGRNRHVRL FPMAALDGRE TEFYKLAETK GCQSIVSGHV RHGALTCLCV AMKRQVLCYE
LNQSKTRHKK IKEIQVQGNV QWMSIFNDRL CVGYQSGFLK YPLHGEGSPY SLLHPDDHTL
SFISQQPTDA ICAVEISNKE YLLCFSSVGV YVDCQGRRSR QQELMWPATP SSCCYNAPYL
SVYSENAIDI FDVNSMEWIQ TIPLKKVRPL NTEGSLNLLG LETVRLIYFK NKMAEGDELV
VPETSDNSRK QMVRNINNKR RYSFRVPEEE RMQQRREMLR DPEMRNKLIS NPTNFNHIAH
MGPGDGIQIL KDLPMNLRPQ ESRTVFSGSV SIPSITKSRT EPGRSMSASS GLAARSSAQN
GSALRREFSG GSYGAKRQPM ASPSDGSLSS GGLDQGSDAP TRDYEREDSD SPRHSTASNS
SNLSSPPSPV SPHKTKSLSL ESSDHVSWDS
//
