ID A0A3P9P5G4_POERE Unreviewed; 3064 AA.
AC A0A3P9P5G4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000017060.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000017060.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000017060.1};
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 STRING; 8081.ENSPREP00000017060; -.
DR Ensembl; ENSPRET00000017241.1; ENSPREP00000017060.1; ENSPREG00000011453.1.
DR GeneTree; ENSGT00940000154766; -.
DR OMA; ESYYTEI; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000011453; Expressed in head and 1 other cell type or tissue.
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; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 5.
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:UP000242638};
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 28..159
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1235..1410
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1422..1534
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1598..1666
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1912..2088
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2100..2214
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2516..2581
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2648..2738
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2758..3013
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1551..1592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1685..1850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1864..1900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2230..2393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2405..2519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 173..222
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 700..727
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1551..1569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1570..1592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1764..1778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1779..1798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1821..1850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1867..1898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2236..2260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2271..2292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2321..2370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2487..2519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2787
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 3064 AA; 344967 MW; 0F07F8A2A5B1ED50 CRC64;
SGFHRNEDMK AIDVLPILKE KVAFLSGGRD RRGGPILTFP ARSNHDRIRP DDLRRLVAYL
ATIPNEEVAR HGFTVIVDMR GSKWDSIKPL LKILQESFPS CIHVALIIKP DNFWQKQRTN
FGSSKFEFET VMVSLEGLTK IVDPSQLTAD FDGSLEYNHD DWIEVRLSFE TFASDAARAL
ARLEELQETL SQRDLPRDLE GARRLMEEHA ALKKRATKAS IEELDTQGRR LLQRLQLQTA
GVGGGDAHNL VAKVTALLDK LHGTRQNLQQ LWHMRKLKLD QCFQLRLFEQ DAEKMFDWIM
HNKGLFLTSY TEIGGNHQHA VELQTQHNHF AMNCMNVYVN INRIMSVGNR LLESGHYASQ
QIQQISGQLE QEWKAFAAAL DERSTLLEMS ASFHQKADQY MSKVEPWCKA CGEGELPSEL
QDLEDTIHHH QGLYEHITTA YSEVSQDGKA LLDKLQRPLT PGSADSLMAS ANYSKAVHHV
LDIIHEVLHH QRQLENIWQH RKVRLHQRLQ LCVFQQDVQQ VLDWIENHGE AFLSKHTGVG
KSLHRARALQ KRHEDFEEVA QNTYTNADKL LEAAEQLAQT GECDPEEIYQ AAHQLEDRIQ
DFVRRVEQRK VLLDMSVAFH THVKELWTWL EELQKELLDD VYAESVEAVQ DLIKRFGQQQ
QTTLQATVNV IKEGEDLIQQ LRDSAISSNK TPHNSSMAHI ESVLQQLDEA QGQMEELFQE
RKIKLELFLQ LRIFERDAID IISDLESWNE ELSKQMNDFD TEDLTLAEQR LQHHADKALT
MNNLTFDVIH QGQELLQYVT EVQTSGVELL CDRDVDMATR VQDLLEFLHE KQQELDLAAE
QHRRHLEQCV QLRHLQAEVK QVLGWIRNGE SMLNAGLITA SSLQEAEQLQ KEHEQFQHAI
EKTHQSALQV QQKAEALLQA NHYDMDMIRD CAEKVADHWQ QLMLKMEDRL KLVNASVAFY
KTSEQVCSVL ESLEQEYKRE EDWCGGADKL GPNSETDHVT PMVSKHLEQK EAFLKACTLA
RRNADVFLKY LHRNSVNMPG MLSHVKAPET QVKNILNELL QRENRVLHFW TMRKRRLDQC
QQYVVFERSA KQALEWIHDT GEFYLSTHTS TGSSIHHTQE LLKEHEDFQI TAKQTKERVK
LLIQLADGFC DKGHAHALEI KKWVSSVDKR YRDFSLRMDK YRTSLETALG ISSDSNKASK
ELQLDIIPAT APGSEVKLRD AAHELNEEKR KSARRKEFIM AELIQTEKAY VRDLRECMDT
YLWEMTSGVE EIPPGIVNKE HIIFGNMQDL YEFHHNIFLK ELEKYEQLPE DVGHCFVTWA
DKFQMYVNYC KNKPDSTQLI LEHAGPYFDE IQQRHRLANS ISSYLIKPVQ RITKYQLLLK
ELLTCCEEGK GEIKDGLEVM LSVPKKANDA MHLSMLEGFD GNIDSQGELI LQESFQVWDP
KTLIRKGRDR HLFLFEMSLV FSKEVKDSNG RSKYLYKSKL FTSELGVTEH VEGDPCKFAL
WLGRTPTSDN KIVLKASSIE NKQDWIKHIR EVIQERTVLL RGALKEPIHI PKATTAKHKG
RRDGEDLDSQ GDASSQPDTI SIASRTSQNT LDSDKLSGGC ELTVVIHDFM ASNGSSNGEL
TVRRGQTVEV LERLHDKPDW CLVRTTDRSP AQEGIVPCSI LCIAHSRSSM EMEGLFNHKD
TLSVSSNDAL QPGSSHTLGP HSSPGPKRPG NTLRKWLTSP VRRLSSGKAD GHVKKLAHKH
KKNRDGTRKN MDAIPGSQKD SDDSAATPQD ETLEERMRNE GLSSGTLSKS SSSGMQSCGE
EEGEEGADAV PLPPPMAIQQ HSLLQPDSQD DKSTSRLSAR PSSSETPSAA ELVSAIEELV
KSKMSLEDRP SSLSVEQGDS SSPSLNPSDN SLLSSSSPID EMDERKTNFL KRRHYVLLEL
VETERDYVRD LGSVVEGYMS RMKEEGVPDD MRGKDKMVFG NIHQIYDWHK DFFLGELEKC
LEDPERLAPL FVKQERRLHM YIVYCQNKPK SEHIVSEYID TYFEDLKQRL GHRLQITDLL
IKPVQRIMKY QLLLKDLLKV SKKAGADTTE LEKAVEVMCV VPKRCNDMMN VGRLQGFDGK
IVAQGRLLLQ DTFMVSDQDG GLLSRMKERR VFLFEQIVIF SEPLDKKKGF STPGYLFKNS
IKVSCLGLEE NSDDPCKFTL ISRSSSGNLE RFTFHSSSPG VSQAWVHQVS QILENQRNFL
NALTSPIEYQ RNHVGGGGPP SSSSSSTGGS STNSTSSMGG GGGGGGGGGS GGSGGNSSSL
CGPRSRPSRI PQPSSRLPQP VHHHHPPGPE GPDRSAGMWS PSHPSLPSYP YSDSPTNGEL
LSSEVFTLKR SDSSQGNNYN NSNRPADNTD GGLRQTFGAY EETQAHQKTA VPQMPVAPLS
FSLRSPRVGT VSPHISPQTP GGGKEPFVPS SPAHKGNPFW AVVPPMPPSP AGRPGSFSFP
SDNSGGGDSL GRGMPPFLRN SGHSKETDRM STCSSTSEQS VTSTQSNGSE SSSSSSSVST
MLVTQDYVAV KEDEISVVQG EVVQMLASNQ QNMFLVYRAA NEHSPAAEGW IPGYVLGHTS
SSTTPDLPEG TIKKSLSWHT ALRIRRKSEK RDKDGRKLEN GYRKSQDGLA NKVSVKLLNP
NFIYDAPPEF LIPLSDASCE SGDSVTLRCK VCGRPRAAVS WRGPDNSILS NNGHYSVTYS
ETGEASLHVL RVSVEDSGVY TCVATNVAGT VTSSACLTVS APNNGSEDIW KSSFESYFTE
ITELGRGRFS VTKRCDQRGS KRTIAAKHVN KKLLCREQVL QEIRLLQTLD HPNLVRLLDT
YETAHSYVLV LEMADQGRFL DYIVSWGNLT EEKVALYLRD ILEALQYLHG WKVAHLDLKP
ENIVVEQVCS QPVIKLTDFG DAVQLDPHSS HIHPLLGSPE FSAPELVLGQ PVSLTSDLWS
LGVVTYVLLS GASPFLDESL EETCLNICRL DFSFPEDYFQ GVTTEAKDFV CLLLQGELER
RPSAGFCLQY PWLQPRGVAS GGHYGTYLDT SRLISFIERR KHQNDVRPVG AIQAFLHSRL
YNHT
//
