ID A0A9Y4N9W0_9TELE Unreviewed; 3110 AA.
AC A0A9Y4N9W0;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 10-JUN-2026, entry version 12.
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=trioa {ECO:0000313|RefSeq:XP_008293382.1};
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|Proteomes:UP000694891, ECO:0000313|RefSeq:XP_008293382.1};
RN [1] {ECO:0000313|RefSeq:XP_008293382.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2026) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); 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:ARBA00048679};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00047899};
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 RefSeq; XP_008293382.1; XM_008295160.1.
DR GeneID; 103367201; -.
DR CTD; 557667; -.
DR Proteomes; UP000694891; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:TreeGrafter.
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:0007411; P:axon guidance; IEA:TreeGrafter.
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 FunFam; 1.20.900.10:FF:000001; Guanine nucleotide exchange factor DBS; 1.
DR FunFam; 1.10.510.10:FF:000152; kalirin isoform X1; 1.
DR FunFam; 2.30.30.40:FF:000038; kalirin isoform X1; 1.
DR FunFam; 2.30.30.40:FF:000040; kalirin isoform X1; 1.
DR FunFam; 2.60.40.10:FF:000368; kalirin isoform X1; 1.
DR FunFam; 1.20.58.60:FF:000034; kalirin isoform X2; 1.
DR FunFam; 3.40.525.10:FF:000003; kalirin isoform X2; 1.
DR FunFam; 1.20.58.60:FF:000024; Kalirin RhoGEF kinase a; 1.
DR FunFam; 1.20.58.60:FF:000023; Kalirin RhoGEF kinase b; 1.
DR FunFam; 1.20.58.60:FF:000032; Kalirin RhoGEF kinase b; 1.
DR FunFam; 2.30.29.30:FF:000040; Kalirin RhoGEF kinase b; 1.
DR FunFam; 1.20.900.10:FF:000008; rho guanine nucleotide exchange factor 25; 1.
DR FunFam; 1.20.58.60:FF:000015; triple functional domain protein-like; 1.
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; 3.30.200.20; Phosphorylase Kinase, domain 1; 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_dom.
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; IPR058918; KALRN/TRIO-like_spectrin.
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; IPR051336; RhoGEF_Guanine_NuclExch_SF.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR055251; SOS1_NGEF_PH.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR PANTHER; PTHR22826:SF106; TRIO, ISOFORM A; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF07679; I-set; 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; PF23587; SH3_KALRN; 1.
DR Pfam; PF22697; SOS1_NGEF_PH; 2.
DR Pfam; PF00435; Spectrin; 4.
DR Pfam; PF23323; Spectrin_6; 1.
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; 7.
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; 1.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694891};
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}.
FT DOMAIN 52..198
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1294..1469
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1481..1603
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1668..1733
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1984..2160
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2558..2623
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2693..2783
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2804..3059
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1618..1650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1760..1922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1939..1972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2308..2559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2634..2664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 755..785
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..285
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1807..1818
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1852..1870
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1907..1916
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1951..1969
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2340..2367
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2388..2399
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2505..2519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2543..2559
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2651..2664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2833
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 3110 AA; 349320 MW; 6386B7B16BFF7687 CRC64;
MSSGEGAEET TKDASDIEAF FKTDGSLPKE PKGDVSSQIA GFRRNEEMRA MEVLPILKEK
VAFLSGGRDR RGGPVLTFPS RSNHDRIRTD DLRRLIAYLA GIPSEEVCKH GFTVIVDMRG
SKWDSIKPLL KILQESFPSC IHVALIIKPD NFWQKQRTNF GSSKFEFETT MVSLEGLTKV
VDPSQLTADF DGSLDYNHEE WIEVRVAFEE FSGHATQMLA RLEEMQETVS RKDFPQDLEG
ARRMIEEHAT LKKKVIKAPI EELDTEGQRL LQRIQSSESF SNRNGSSGGS GGSSSSGGGV
CNADTQGLVP RITQLLDKLH STRQHLHQAW HVRKLQLDQC FQLRLFEQDA EKMFDWIMHN
KGLFLAGYTE IGNNHPHAIE LQTQHNHFAM NCMNVYVNIN RIMSVGNRLL ESGHYASQQI
KQISGQLEQE WKAFAAALDE RSTLLEMSAS FHQKCDQYMS NVDSWCKACG EVDLPSELQD
LEDAIHHHQG LYEHITAAYS EVSQDGKALL DKLQRPLTPG SADSLTASAN YSKAVHHVLD
IIHEVLHHQR QLENIWQHRK VRLHQRLQLC VFQQDVQQVL DWIENHGEAF LSKHTGVGKS
LHRARALQKR HEDFEEVAQN TYTNADKLLE AAEQLAQTGE CDPEEIYQAA HQLEDRIQDF
VRRVEQRKVL LDMSVAFHTH VKELWTWLEE LQKELLDDVY AESVEAVQDL IKRFGQQQQT
TLQVTVNVIK EGEDLIQQLR DSAISSNKTP HNSSINHIES VLQQLDEAQA QMEELFQERK
IKLELFLQLR IFERDAIDII SDLESWNEEL TGQMNDFDTE DLTLAEQRLQ HHADKALTMN
NLTFDVIHQG QELLQYVNEV QASGVELLCD RDVDMATRVQ DLLEFLHEKQ QELDLAAEQH
RRHLEQCVQL RHLQAEVKQV LGWIRNGESM LNAGLITASS LQEAEQLQRE HEQFQHAIEK
THQSALQVQQ KAEALLQANH YDMDLIRDCA ESVASHWQQL MLKMEDRLKL VNASVAFYKT
SEQVCSVLES LEQEYKREED WCGGADKLGP NCETDHVTPM ISKHLEQKEA FLKACTLARR
NADVFLKYMH RNSVNMPGML SHVKAPEQQV KNILNELLQR ENRVLHFWTM RKRRLDQCQQ
YVVFERSAKQ ALEWIHDTGE FYLSTHTSTG SSIHHTQELL KEHEDFHITA KQTKERVKLL
IQLADGFCEK GHSHAGEIKK WVTAVDKRYR DFSLRMDKYR CSLEKALGIS SDSNKASKDL
QLDIIPATAP GSEVKLRDAA AHELNEEKRK SARRKEFIMA ELIQTEKAYV RDLRECMDTY
LWEMTSGVEE IPPGIINKEH IIFGNMQDLY EFHHNIFLKE LEKYEQLPED VGHCFVTWAD
KFQMYVNYCK NKPDSTQLIL EHAGNYFDEI QQRHRLANSI SSYLIKPVQR ITKYQLLLKE
LLTCCEEGKG EIKDGLEVML SVPKKANDAM HLSMLEGFDE NIESQGELIL QESFQVWDPK
TLIRKGRERH LFLFEMSLVF SKEVKDSNGR SKYIYKSKLF TSELGVTEHV EGDPCKFALW
VGRTPTSDNK IVLKLSQGSK HGAMASSIEN KQDWIKHIRE VIQERTIHLR GALKEPIHIP
KATTAKHHKG RRDGEDLDSQ GEGSSQPDTI SLASRTSQNT LDSDKLSGGC ELTVVIHDFM
ASNSNELTVR RGQTVEVLER CHDKPDWCLV RTTDRSPAQE GLVPCSMLCI AHSRSSMEME
GIFNHKDTLS VCSNDSIMPG SSATLQPGHG IGSHTSPGPK RPGNTLRKWL TSPVRRLSSG
KADGHVKKLA HKHKKSREMR KSGEMTMGSQ KDSDDSAATP QDETLEERVR NEGLSSGTLS
KSSSSGMQSC GEEEGEEGAD SVPLPPPMAI QQHSLLQPDS QDDKTSSRLS VRPSSSETPS
AAELVSAIEE LVKSKMALED RPSSLSVEQG DSSSPSFNPS DNSLLSSSSP IEEMDERRNS
ILKKRHYILL ELVETERDYV RDLGLVVEGY MSRMKEEGVP DDMKGKDKIV FGNIHQIYDW
HKDFFLRELE KCLEDPDRLG PLFLKQERRL NMYVVYCQNK PKSEHIVSEY IDTYFEDLKQ
RLGHRLQITD LLIKPVQRIM KYQLLLKDFL KHSKKAGLES MDLEKAVEVM CIVPKRCNDM
MNVGRLQGFD GKIVAQGRLL LQDTFMVSDP EGSLLGRMKE RRVFLFEQLV IFSEPLDKKK
GFSLPGFLYK NSIKVSCLGL EDNVEGDPCK FILTSRSTNG AVESFVLHSA HPGVREVWTL
QISQILESQR NFLNALTSPI EYQRNHVGAS SGPCVPSMGA PGGGSSGSSV APGVGGGSSQ
GSSIPSGPQG GSRRPSRIPQ PSRLPQPLRH HPGADPDGPN KMSGSSPRPV PPPLLPPGGS
PQGKRPVHIP EDQAQTPTPA SAVTPIPRAT VGPLPSTPSS KPRPGAVSPM SSPMSTPAFG
KDALPPPPPS PGQKSGSGFW SSMPGSPASR PGSFTFPGEA GESPVRQSSN QIQTGSGSQT
HRHSTHSKEA DRMSTCSSAS EQSIQSTQSN GSESSSSSSV STMLVTQDYM AVKEDEISVI
QGEVVQILAS NQQNMFLVFR AATEQGPAAE GWIPGFVLGH TSAIVPDCPE GSINRKSSSW
HTSLRIRKKS EKKEKEAKKE TKLENGYRKS RDGLANKVSV KLLNPNYIYD VPPEFLVPLS
DVTCDNGESV TLRCKVCGRP RATVTWKGPN QSNLTNNGHF SIAYSDTGEA TLRIIGVASE
DDGVYTCVAT NELGSVTSSA SLRVLAVSAD GVRVSWKDNF ESHYAEVVEL GRGRFSVVKR
CDHRGTKRTV AVKQVNKKLM RRDRVTQELN LLQRLQHPCI VSLMDTYETP SSYALVLEMA
DQGRLLDYIV SWGNLTEEKV ACYLRNVLEA LHYLHNCRIV HLDVKPENLL VAHTASGQPT
VKLIDFGDAV QLNSAHYVHP LLGSPEFASP ELVLGEPVSL TSDLWSLGVV TYVLLSGASP
FLDESAEETC LNICRLDFSF PRDYFQGVSQ AARDFVCLLL RTDPGRRPPA GLCLQEPWLQ
AGLGDGRARA EGCLDTSRLI SFIDRRKHQT DARPIGGVRS FIQSRLQPRV
//
