ID A0A3B5BJV3_9TELE Unreviewed; 2746 AA.
AC A0A3B5BJV3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000027797.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000027797.1}
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 STRING; 144197.ENSSPAP00000027797; -.
DR Ensembl; ENSSPAT00000028251.1; ENSSPAP00000027797.1; ENSSPAG00000020865.1.
DR GeneTree; ENSGT00940000154766; -.
DR Proteomes; UP000261400; Unplaced.
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-KW.
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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00096; Ig; 1.
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; IPR001331; GDS_CDC24_CS.
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; 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; 5.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
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 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};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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 1..153
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1231..1406
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1418..1530
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1594..1662
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1853..2029
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2041..2155
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2220..2285
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2361..2451
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2444..2699
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1541..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1682..1759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2165..2207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..216
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 701..728
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1541..1565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2165..2182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2746 AA; 313579 MW; FCF3AF3A8FEDB25C CRC64;
MDMKAIDVLP ILKEKVAFLS GGRDRRGGPV LTFPARSNHD RIRPEDLRRL IAYLATIPSE
EVARHGFTVI VDMRGSKWDS IKPLLKILQE SFPSCIHVAL IIKPDNFWQK QRTNFGSSKF
EFETVMVSLE GLTKIVDPSQ LTADFEGSLE YNHDDWIEVR LSFETFASDA ARSLARLEEL
QETLSQRDLP RDLEGARRLM EEHAALKKRA TKASVEELDT QGRRLLQRLQ SQTTGGSDAH
NLVAKVTGLL DKLHGTRQNL QQLWHMRKLK LDQCFQLRLF EQDAEKMFDW IMHNKGLFLT
SYTEIGGNHQ HAVELQTQHN HFAMNCMNVY VNINRIMSVG NRLLESGHYA SQQIQQISGQ
LEQEWKAFAA ALDERSTLLE MSASFHQKAD QYMSKVEPWC KACGEGELPS ELQDLEDTIH
HHQGLYEHIT TAYSEVSQDG KSLLDKLQRP LTPGSADSLM SSANYSKAVH HVLDIIHEVL
HHQRQLENIW QHRKVRLHQR LQLCVFQQDV QQVLDWIENH GEAFLSKHTG VGKSLHRARA
LQKRHEDFEE VAQNTYTNAD KLLEAAEQLA QTGECDPEEI YQAAHQLEDR IQDFVRRVEQ
RKVLLDMSVA FHTHVKELWT WLEELQKELL DDVYAESVEA VQDLIKRFGQ QQQTTLQATV
NVIKEGEDLI QQLSTLDVTS AHRDSAISSN KTPHNSSMAH IESVLQQLDE AQGQMEELFQ
ERKIKLELFL QLRIFERDAI DVNLESWNEE LSQQMSDFDT EDLTLAEQRL QHHADKALTM
NNLTFDVIHQ GQELLQYVTE VQASGVELLC DRDVDMATRV QDLLEFLHEK QQELDLAAEQ
HRRHLEQCVQ LRHLQAEVKQ VLGWIRNGES MLNAGLITAS SLQEAEQLQK EHEQFQHAIE
KTHQSALQVQ QKAEALLQAN HYDMDMIRDC AEKVADHWQQ LMLKMEDRLK LVNASVAFYK
TSEQVCSVLE SLEQEYKREE DWCGGADKLG PNSESDHVTP MISKHLEQKE AFLKACTLAR
RNADVFLKYL HRNSVNMPGM LSHVKAPETQ VKNILNELLQ RENRVLHFWT MRKRRLDQCQ
QYVVFERSAK QALEWIHDTG EFYLSTHTST GSSIHHTQEL LKEHEDFQIT AKQTKERVKL
LIQLADGFCD KGHAHALEIK KWVSSVDKRY RDFSLRMDKY RTCLETALGI SSDSNKALQL
DIIPASAPGS EVKLRDAAHE LNEEKRKSAR RKEFIMAELI QTEKAYVRDL RECMDTYLWE
MTSGVEEIPP GIVNKEHIIF GNMQDLYEFH HNIFLKELEK YEQLPEDVGH CFVTWADKFQ
MYVNYCKNKP DSTQLILEHA GPYFDEIQQR HRLANSISSY LIKPVQRITK YQLLLKELLT
CCEEGKGEIK DGLEVMLSVP KKANDAMHLS MLDGFDGNID SQGELILQES FQVWDPKTLI
RKGRDRHLFL FEMSLVFSKE VKDSNGRSKY LYKSKLFTSE LGVTEHVEGD PCKFALWVGR
TPTSDNKIVL KASSIENKQD WIKHIREVIQ ERTVHLRGAL KEPIHIPKAT TTKHKGRRDG
EELDSQGDAS SQPDTISIAS RTSQNTLDSD KLSGGCELTV VIHDFVASNG GSNGELTVRR
GQTVEVLERL HDKPDWCLVR TTDRSPAQEG IVPCSMLCIA HSRSSMEMEG LFNHKDIFSY
EGPGSSQTLG PHSSPGPKRP GNTLRKWLTS PVRRLSSGKA DGHVKKLAHK HKKNRDGTRK
NMDAMAGSQK DSDDSAATPQ DETLEEPFIF FFRFLSLFQS ASRLSARPNS SETPSAAELV
SAIEELVKSK MLLERGQLIT FDFVCVLIWS ISDVHPRLSI TFVLHSDNFC FLSLSYVLLE
LVETERDYVR DLGSVVEGYM SRMKEEGVPD DMRGKDKIVF GNIHQIYDWH KDFFLGELEK
CLEDPDRLAP LFVKQERRLH MYIVYCQNKP KSEHIVSEYI DTYFEDLKQR LGHRLQLTDL
LIKPVQRIMK YQLLLKDLLK ISKKAAVDST ELEKAVEVMC VVPKRCNDMM NVGRLQGFDG
KIVAQGRLLC QDTFMVSDQD GGLLSRMKER RIFLFEQIVI FSEPLDKKKG FSTPGYLFKN
SIKVSWLGLE ENAEDPCKFT LTSRSSSGNL ERYTLHSTSP GVSQVWIHQV SQILENQRNF
LNGKRLSSSL CGPRSRPSRI PQPSSRLPQP VHHHHPPGPE GPDRSFSNLL FWQSESSNSS
SMSTMLVTQD YVAVKEDEIS VVQGEVVQML ASNQQNMFLV YRAANEHCPA AEGWIPGYVL
GHTSSSITPE LPEGTIKKSL SWHTALRIRR KSEKRDKEGR KLENGYRKSQ DSLANKVSVK
VEHTMCVSQT LISTFLPPAP PEFLIPVSDA ACESGDNVTL RCKVCGRPRA TVTWRGPDNN
TLSNNGRYSI TYSETGEASL RILAASVEDS GVYTCVATNI AGTVTSSSSL RVGRFSVTKR
CDQRGSKRTV AAKHVNKKLS RREQVLQEVR LLQTLDHPNL VRLLDTYETA NSYVLVLELA
DQGRFLDYIV SWGNLTEEKV ALYLRDILEA LHYLHSWRIA HLDLKPENIM MEHASSQPVI
KLTDFGDAVQ LNPPSSYVHP LLGSPEFSAP ELVLGQPASL MSDLWSLGVV TYVVLSGASP
FLDESLEETC LNICRLDFSF PEDYFQGVSP AAKDFVRLLL QGEPERRPSA VSCLQEPWLQ
PRGNHYSTHL DTSRLISFIE RRKHQNDVRP IGTIKAFLHS RLLNHI
//
