ID A0A4W6EPM2_LATCA Unreviewed; 2777 AA.
AC A0A4W6EPM2;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Lates calcarifer (Barramundi) (Holocentrus calcarifer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangaria incertae sedis; Centropomidae; Lates.
OX NCBI_TaxID=8187 {ECO:0000313|Ensembl:ENSLCAP00010039131.1, ECO:0000313|Proteomes:UP000314980};
RN [1] {ECO:0000313|Proteomes:UP000314980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sai Rama Sridatta P.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLCAP00010039131.1}
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR Ensembl; ENSLCAT00010040053.1; ENSLCAP00010039131.1; ENSLCAG00010018173.1.
DR GeneTree; ENSGT00940000154766; -.
DR Proteomes; UP000314980; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13240; PH1_Kalirin_Trio_like; 1.
DR CDD; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd11852; SH3_Kalirin_1; 1.
DR CDD; cd11853; SH3_Kalirin_2; 1.
DR CDD; cd00176; SPEC; 6.
DR Gene3D; 1.20.58.60; -; 5.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR047054; Kalirin_TRIO_PH_1.
DR InterPro; IPR028570; Kalirin_TRIO_SH3_1.
DR InterPro; IPR047053; Kalirin_TRIO_SH3_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR PANTHER; PTHR22826:SF104; TRIPLE FUNCTIONAL DOMAIN PROTEIN; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF16609; SH3-RhoG_link; 2.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00150; SPEC; 6.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR SUPFAM; SSF46966; Spectrin repeat; 6.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50002; SH3; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000314980};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 31..162
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1245..1420
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1432..1544
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1608..1676
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1852..2034
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2046..2160
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2209..2274
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2341..2436
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2471..2726
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1555..1603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1694..1812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2180..2211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 715..742
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1555..1579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1694..1712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1774..1794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1796..1812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2777 AA; 316804 MW; DCBDE7C9A1E63D37 CRC64;
LCVLGFHRNE DMKAIDVLPI LKEKVAFLSG GRDRRGGPVL TFPARSNHDR IRPEDLRRLI
AYLATIPSEE VARHGFTVIV DMRGSKWDSI KPLLKILQES FPSCIHVALI IKPDNFWQKQ
RTNFGSSKFE FETVMVSLEG LSKIVDPSQL TADFEGSLEY NHDDWIEVRL SFETFASDAT
RALARLEELQ ETLSQRDLPR DLEGARRLME EHAVLKKRAT KASVEELDTQ GRRLLQRLQS
QTAGDSNDHH HGFHAHADAH NLVAKVTGLL DKLHGTRQNL QQLWHMRKLK LDQCFQLRLF
EQDAEKMFDW IMHNKGLFLT SYTEIGGNHQ HAVELQTQHN HFAMNCMNVY VNINRIMSVG
NRLLESGHYA SQQIQQISGQ LEQEWKAFAA ALDERSTLLE MSASFHQKAD QYMSKVEPWC
KACGEGELPS ELQDLEDTIH HHQGLYEHIT TAYSEVSQDG KSLLDKLQRP LTPGSADSLM
ASANYSKAVH HVLDIIHEVL HHQRQLENIW QHRKVRLHQR LQLCVFQQDV QQVLDWIENH
GEAFLSKHTG VGKSLHRARA LQKRHEDFEE VAQNTYTNAD KLLEAAEQLA QTGECDPEEI
YQAAHQLEDR IQDFVRRVEQ RKVLLDMSVA FHTHVKELWT WLEELQKELL DDVYAESVEA
VQDLIKRFGQ QQQTTLQATV NVIKEGEDLI QQLRLILDSA ISSNKTPHNS SMAHIESVLQ
QLDEAQGQME ELFQERKIKL ELFLQLRIFE RDAIDVNLES WNEELSQQMS DFDTEDLTLA
EQRLQHHADK ALTMNNLTFD VIHQGQELLQ YVTEVQASGV ELLCDRDVDM ATRVQDLLEF
LHEKQQELDL AAEQHRRHLE QCVQLRHLQA EVKQVLGWIR NGESMLNAGL ITASSLQEAE
QLQKEHEQFQ HAIEKTHQSA LQVQQKAEAL LQANHYDMDM IRDCAEKVAD HWQQLMLKME
DRLKLVNASV AFYKTSEQVC SVLESLEQEY KREEDWCGGA DKLGPNSESD HVTPMISKHL
EQKEAFLKAC TLARRNADVF LKYLHRNSVN MPGMLSHVKA PETQVKNILN ELLQRENRVL
HFWTMRKRRL DQCQQYVVFE RSAKQALEWI HDTGEFYLST HTSTGSSIHH TQELLKEHED
FQITAKQTKE RVKLLIQLAD GFCDKGHAHA LEIKKWVSSV DKRYRDFSLR MDKYRTCLET
ALGISSDSNK ALQLDIIPAS APGSEVKLRD AAHELNEEKR KSARRKEFIM AELIQTEKAY
VRDLRECMDT YLWEMTSGVE EIPPGIVNKE HIIFGNMQDL YEFHHNIFLK ELEKYEQLPE
DVGHCFVTWA DKFQMYVNYC KNKPDSTQLI LEHAGPYFDE IQQRHRLANS ISSYLIKPVQ
RITKYQLLLK ELLTCCEEGK GEIKDGLEVM LSVPKRANDA MHLSMLDGFD GNIDSQGELI
LQESFQVWDP KTLIRKGRDR HLFLFEMSLV FSKEVKDSNG RSKYLYKSKL FTSELGVTEH
VEGDPCKFAL WVGRTPTSDN KIVLKASSIE NKQDWIKHIR EVIQERTVHL RGALKEPIHI
PKATTTKHKG RRDGEELDSQ GDASSQPDTI SIASRTSQNT LDSDKLSGGC ELTVVIHDFV
ASNGSSSGEL TVRRGQTVEV LERLHDKPDW CLVRTTDRSP AQEGIVPCSM LCIAHSRSSM
EMEGLFNHKD TLSVSSNDAL QPGSSQTLGP HSSPGPKRPG NTLRKWLTSP VRRLSSGKAD
GHVKKLAHKH KKNRDGTRKN MDTISGSQKD SDDSAATPQD ETLEEVRADE AVDSYDTSAS
RLSARPSSSE TPSAAELVSA IEELVKSKMV RHKYYIHKFS SYAHANMAHF FAHRTILMDV
YTSIHTHTQS FSWVLLTENG ILGYMSRMKE EGVPDDMRGK DKIVFGNIHQ IYDWHKDFFL
GELEKCLEDP DRLAPLFVKQ ERRLHMYIVY CQNKPKSEHI VSEYIDTYFE DLKQRLGHRL
QITDLLIKPV QRIMKYQLLL KDLLKVSKKA GVDTTELEKA VEVMCVVPKR CNDMMNVGRL
QGFDGKIVAQ GRLLLQDTFM VSDQDGGLLS RMKERRVFLF EQIVIFSEPL DKKKGFSTPG
YLFKNSIKVS WLGLEENADD PCKFTLTSRS SSGNLERYTL HSTSPGVSQV WVHQVSQILE
NQRNFLNGMT LPCTQNYNSS SLCGPRSRPS RIPQPSSRLP QPSESSSSSS VSTMLVTQDY
VAVKEDEISV VQGEVVQMLA SNQQNMFLVY RAANEHCPAA EGWIPGFVLG HTSSSITPEL
PEGTIKKSLS WHTALRIRRK SEKRDKEGRK LENGYRKSQD SLANKVSVKL LNPNFIYDAP
PEFLIPVGDV TCESGDSVTL RCKVCGRPRA TVTWRGPDNS TLSNNGHYSI TYRSTCYTGE
AALRILGVSV EDSGVYSCVA TNVAGSVTSS ASLRVSGEVP VMVCTFNFLF SSELPTLVLE
VLWKGSFESH YTEITELGRG RFSVTKRCDQ RGSKRTVAAK HVNKKLLRRE QVLQEIRLLQ
TLDHPNLVKL LDTYETVNSY VLVLEMADQG RFLDYIVSWG NLTEEKVALY LRDILEALHY
LHSWRIAHLD LKPENIVVEH ASSQPLIKLT DFGDAVQLNP PSAYIHPLLG SPEFSAPELV
LGQPVSLMSD LWSLGVVTYV VLSGASPFLD ESLEETCLNI CRLDFSFPED YFQGVSAAAR
DFVCLLLQGE PERRPSVASC LQEPWLQPRG PPSQNHHTAH LDTSRLISFI ERRKHQNDVR
PISTIKAFLQ SRLLNHI
//
