ID K7GHH3_PELSI Unreviewed; 1758 AA.
AC K7GHH3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 75.
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:ENSPSIP00000019734.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000019734.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000019734.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AGCU01051964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01051965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01051966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01051967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01051968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01051969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01051970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01051971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01051972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01051973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006118121.1; XM_006118059.2.
DR STRING; 13735.ENSPSIP00000019734; -.
DR Ensembl; ENSPSIT00000019827.1; ENSPSIP00000019734.1; ENSPSIG00000017372.1.
DR GeneID; 102460743; -.
DR CTD; 8476; -.
DR eggNOG; KOG0612; Eukaryota.
DR GeneTree; ENSGT01030000234517; -.
DR OMA; SYCEGYL; -.
DR OrthoDB; 988261at2759; -.
DR TreeFam; TF313551; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0042641; C:actomyosin; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
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:0031032; P:actomyosin structure organization; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
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 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; SSF69322; Tricorn protease domain 2; 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:UP000007267};
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 77..343
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 344..414
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1038..1088
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1108..1227
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1253..1525
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1597..1610
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 550..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1632..1758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 708..820
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 914..941
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1632..1674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1683..1704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1722..1758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1758 AA; 199968 MW; 52D1D88A0890FF80 CRC64;
MSGEVRLRQL EQFILDGPTR TNGQCFSVET LLDILICLYD ECNNSPLRRE KNILEYLEWA
KSFTSKVKQM RLHKEDFEIL KVIGRGAFGE VAVVKLKNAD KVFAMKILNK WEMLKRAETA
CFREERDVLV NGDNQWITTL HYAFQDENYL YLVMDYYVGG DLLTLLSKFE DRLPEDMARF
YLAEMVIAID SVHQLHYVHR DIKPDNILMD MNGHIRLADF GSCLKLMEDG TVQSSVAVGT
PDYISPEILQ AMEDGKGKYG PECDWWSLGV CMYEMLYGET PFYAESLVET YGKIMNHKER
FQFPAQVTDV SENAKDLIRR LICSREHRLG QNGIEDFKNH PFFAGIEWDN IRNCEAPYIP
EVSSPTDTSN FDVDDDCLKN SETMPPPTHT AFSGHHLPFV GFTYTSSCVL SDRSCLRDTT
GPTSMELDAS VQRTLEDSLA TEAYERRIRR LEQEKLELSR KLQESTQTVQ ALQYSTVDGP
ITASKDLEIK SLKEEIEKLR KQVTDSGQLE QQLEEASSAR RELDDASRQI KAFEKQIRAL
KQEKEDLNKE LMESSERLKS QTKELKDAHS QRKLAMQEFS EMNERLTDLH SQKQKLTRQV
RDKEEEMDMV MQKVEILRQE LRRTERLKKE LEVHAEAAAA EASKDRKLRE RSEQYSKQLE
RELEGLKQKQ VGRSPGVSST EHQQEITKLK AELEKKSVFY EEELSKREIM HANEIKTLKK
ELRDAESQQL ALKKEIMILK DKLEKTRRES QSEREEFETE FKQKYEREKT LLTEENKKLS
NELDKLTAMF ERLSMNNRQL EEEMRDLADK KESVAHWEAQ ITEIIQWVSD EKDARGYLQA
LASKMTEELE ALRNSSLGAR ATDMPWKMRR FAKLDMSARL ELQSALDAEI RAKQAIQDEL
NKVKASSIST ECKLQESEKK NLELLSEIEK LKKETEELRS EKGVKHQDSQ NSFLAFLNAP
TSALDQFEID SVENFTLSNT PSRDEDIKSH LHSRSRSPST ASDIEPIEVT DHPPRSVHTP
AMRPAFIGSG LSAPKPKAHQ FVVKSFNTPT KCNQCTSLMV GLIRQGCTCE VCGFSCHVTC
ADKAPAVCPI PPEQTKGPLG IDPQKGIGTA YEGHVRVPKP AGVKKGWQRA LAVVCDFKLF
LYDIAEGKAA QPTVIVSQVI DMRDEEFSVS SVLASDVIHA NRKDVPCIFR VTASQLSASS
NKCSILILAD SENEKSKWVG VLNELHRILK KNKLKDRSVY VPKEAYDSTL PLIKTTQAAA
IIDHERIALG NEEGLFVVHV TKDEIIRVGD NKKVHQIELI PNEQLIAVIS GRNRHVRLFP
MAALDGRETE FYKLAETKGC QTIVSGQLRH GALTCLCVAM KRQVLCYELN QTKMRHKKMK
EIQVLGNVQW MSVFSERLCV GYQSGFLKYP FHGEGNPHSL LHPDDHTLSF IAQQPTDAIC
AVEISNKEYL LCFSSVGVYV DCQGRRSRQQ ELMWPATPSS CCYNAPYLSV YSENAVDIFD
VNSMEWIQTI PLKKVRPLNT EGSLNLLGLE TIRLIYFKNK MAEGDELVVP ETSDNSRKQM
VRNINNKRRY SFRVPEEERM QQRREMLRDP EMRNKLISNP TNFNHIAHMG PGDGIQILKD
LPMNLRPQES RTMFSGSVSI PSITKSRTEP GRSMSASSGL AARSSAQNGS ALRREFSGGS
YGTKRQPIAS PSDGSLSSGG LDQGSDVPTR DYEREDSDSP RHSTASNSSN LSSPPSPVSP
HKTKSLSLES SDHVSWDS
//
