ID A0A3Q1H3I0_9TELE Unreviewed; 3057 AA.
AC A0A3Q1H3I0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000034317.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000034317.1}
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 -!- 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; 80966.ENSAPOP00000034317; -.
DR Ensembl; ENSAPOT00000030009.1; ENSAPOP00000034317.1; ENSAPOG00000023620.1.
DR GeneTree; ENSGT00940000154766; -.
DR InParanoid; A0A3Q1H3I0; -.
DR Proteomes; UP000257200; 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-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; 5.
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; 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:UP000257200};
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 42..173
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1274..1449
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1461..1573
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1637..1705
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1951..2127
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2139..2253
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2515..2580
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2647..2739
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 249..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1588..1632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1723..1888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1903..1938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2269..2365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2378..2400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2409..2428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2448..2517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..236
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 739..766
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1588..1608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1609..1632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1723..1741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1803..1817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1818..1837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1860..1888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1906..1937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2278..2319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2348..2365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2381..2395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2488..2517
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 3057 AA; 344372 MW; 19A7D417E0B38478 CRC64;
MSLLSSKCSI LSCVSGFHRN EDMKAIDVLP ILKEKVAFLS GGRDRRGGPV LTFPARSNHD
RIRPEDLRRL IAYLATIPSE EVARHGFTVI VDMRGSKWDS IKPLLKILQE SFPSCIHVAL
IIKPDNFWQK QRTNFGSSKF EFETVMVSLE GLTKIVDPSQ LTADFEGSLE YNHDDWIEVR
LSFETFASDA ARSLARLEEL QETLSQRDLP RDLEGARRLM EEHAALKKRA TKASVEELDT
QGRRLLQRLQ SQTAGGGSSG EGGYGNRGAS GDSNDHHHGF HAHADAHNLV AKVTGLLDKL
HGTRQNLQQL WHMRKLKLDQ CFQLRLFEQD AEKMFDWIMH NKGLFLTSYT EIGGNHQHAV
ELQTQHNHFA MNCMNVYVNI NRIMSVGNRL LESGHYASQQ IQQISGQLEQ EWKAFAAALD
ERSTLLEMSA SFHQKADQYM SKVEPWCKAC GEGELPSELQ DLEDTIHHHQ GLYEHITTAY
SEVSQDGKSL LDKLQRPLTP GSADSLMASA NYSKAVHHVL DIIHEVLHHQ RQLENIWQHR
KVRLHQRLQL CVFQQDVQQV LDWIENHGEA FLSKHTGVGK SLHRARALQK RHEDFEEVAQ
NTYTNADKLL EAAEQLAQTG ECDPEEIYQA AHQLEDRIQD FVRRVEQRKV LLDMSVAFHT
HVKELWTWLE ELQKELLDDV YAESVEAVQD LIKRFGQQQQ TTLQATVNVI KEGEDLIQQL
RDSAISSNKT PHNSSMAHIE SVLQQLDEAQ GQMEELFQER KIKLELFLQL RIFERDAIDI
ISDLESWNEE 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 SSDSNKASKE LQLDIIPASA PGSEVKLRDA
AHELNEEKRK SARRKEFIMA ELIQTEKAYV RDLRECMDTY LWEMTSGVEE IPPGIVNKEH
IIFGNMQDLY EFHHNIFLKE LEKYEQLPED VGHCFVTWAD KFQMYVNYCK NKPDSTQLIL
EHAGPYFDEI QQRHRLANSI SSYLIKPVQR ITKYQLLLKE LLTCCEEGKG EIKDGLEVML
SVPKKANDAM HLSMLDGFDG NIDSQGELIL QESFQVWDPK TLIRKGRDRH LFLFEMSLVF
SKEVKDSNGR SKYLYKSKLF TSELGVTEHV EGDPCKFALW VGRTPTSDNK IVLKASSIEN
KQDWIKHIRE VIQERTVHLR GALKEPIHIP KATTTKHKGR RDGEELDSQG DASSQPDTIS
IASRTSQNTL DSDKLSGGCE LTVVIHDFVA SNGGSNGELT VRRGQTVEVL ERLHDKPDWC
LVRTTDRSPA QEGIVPCSML CIAHSRSSME MEGLFNHKDT LSVSSNDALQ PGSSQTLGPH
SSPGPKRPGN TLRKWLTSPV RRLSSGKADG HVKKLAHKHK KNRDGTRKNM DTIPGSQKDS
DDSAATPQDE TLEERMRNEG LSSGTLSKSS SSGMQSCGEE EGEEGADAVP LPPPMAIQQH
SLLQPDSQDD KSASRLSARP NSSETPSAAE LVSAIEELVK SKMSLEDRPS SLSVEQGDSS
SPSLNPSDNS LLSSSSPIDE LDERKSGFLK RRHYVLLELV ETERDYVRDL GSVVEGYMSR
MKEEGVPDDM RGKDKIVFGN IHQIYDWHKD FFLGELEKCL EDPDRLAPLF VKQERRLHMY
IVYCQNKPKS EHIVSEYIDT YFEDLKQRLG HRLQITDLLI KPVQRIMKYQ LLLKDLLKIS
KKAAVDTTEL EKAVEVMCVV PKRCNDMMNV GRLQGFDGKI VAQGRLLLQD TFMVSDQDGG
LLSRMKERRV FLFEQIVIFS EPLDKKKGFS TPGYLFKNSI KVSWLGLEEN AEDPCKFTLT
SRSSSGNMER YTLHSTSPGV SQVWIHQVSQ ILENQRNFLN ALTSPIEYQR NHVGGGGPSG
PPSSSSSSTA GGGGGGSGGS GGSSSSLCGP RSRPSRIPQP SSRLPQPVHH HHPPGPEGPD
RSAGMWSPCH PQSLSSNSYS DSTTNGELLA SEVPKMRMLD SPHGSNSNNS NRPAVAPLNF
PLKSPRVGTV SPLISPQTPG GKEAFVPSSP AHKGNAFWAI VPAVPPSPAS RPGSFSYPSD
NGGGGDSLGR GSHGTSSHHR HSNSKDIDRM STCSSTSEQS IHSTQSNGSE SSSSSSMSTM
LVTQDYVAVK EDEISVVQGE VVQMLASNQQ NMFLVYRAAN EHCPAAEGWI PGYVLGHTSS
SITPELPEGT IKKSLSWHTA LRIRRKSEKR DKEGRKLENG YRKSQDSLAN KVSVKLLNPN
FIYDAPPEFL VPVIDAACER GENVTLRCKV CGQPRASVTW RGPDNNILSN NGQHSIMYSE
TGEASLRILA VSMEDSGVYT CVATNIAGTV TSSASLRVSG APDDGSEVLW KSNFESHYTE
ISELGRGRFS VTKRCDQRGS KRTVAAKHVN KKLLRREQVL QEIRLLQTLD HPNLVKLLDT
YETANSYVLV LELADQGRFL DYIVSWGNLT EEKVALYLRD ILEALHYLHS WRIAHLDLKP
ENIMVEHASS QPVIKLTDFG DAVQLNPPSS YIHPLLGSPE FSAPELVLGQ PASLMSDLWS
LGVLTYVVLS GASPFLDESL EETCLNICRL DFSFPEDYFQ GVSPAAKDFV GLLLQGEPER
RPSAVSCLQE PWLQPRDVTH LDTSRLISFI ERRKHQNDVR PIGTIKAFLH SRLLNHI
//
