ID A0A669CY15_ORENI Unreviewed; 3028 AA.
AC A0A669CY15;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=trio {ECO:0000313|Ensembl:ENSONIP00000053263.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000053263.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000053263.1}
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 Ensembl; ENSONIT00000064585.1; ENSONIP00000053263.1; ENSONIG00000007788.2.
DR GeneTree; ENSGT00940000154766; -.
DR Proteomes; UP000005207; Linkage group LG22.
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:SF206; TRIPLE FUNCTIONAL DOMAIN PROTEIN-RELATED; 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; 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; 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:UP000005207};
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 21..167
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1259..1434
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1446..1558
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1623..1688
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1939..2115
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2127..2242
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2479..2544
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2613..2703
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2724..2979
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 244..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1573..1618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1715..1877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1894..1927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2262..2481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2565..2585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 721..751
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1595..1618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1791..1805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1848..1877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1900..1925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2262..2276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2283..2308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2397..2416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2452..2481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2753
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 3028 AA; 341345 MW; 1A1BA3452FFA05BE CRC64;
RKVYLWSPVG FRRNEEMRAM EVLPILKEKV AFLSGGRDRR GGPVLTFPSR SNHDRIRTDD
LRRLIAYLAG IPSEEVCKHG FTVIVDMRGS KWDSIKPLLK ILQESFPSCI HIALIIKPDN
FWQKQRTNFG SSKFEFETTM VSLEGLTKVV DPSQLTADFD GSLDYNHEEW IEVRVAFEDF
SGHATQMLAR LEEMQETVSR KDFPQDLEGA RRMIEEHATL KKKVIKAPIE ELDTEGQRLL
QRIQSSESFS NRNGSSGGSS SSGSGVCNAD TQGLVPRITQ LLDKLHSTRQ HLHQAWHVRK
LQLDQCFQLR LFEQDAEKMF DWIMHNKGLF LAGYTEIGNN HPHAVELQTQ HSHFAMNCMN
VYVNINRIMS VGNRLLESGH YASQQIKQIS SQLEQEWKAF AAALDERSTL LEMSAGFHQK
CDQYMSNVDS WCKACGEVDL PSELQDLEDA IHHHQGLYEH ITAAYSEVSQ DGKALLDKLQ
RPLTPGSADS LTATANYSKA VHHVLDIIHE VLHHQRQLEN IWQHRKVRLH QRLQLCVFQQ
DVQQVLDWIE NHGEAFLSKH TGVGKSLHRA RALQKRHEDF EEVAQNTYTN ADKLLEAAEQ
LAQTGECDPE EIYQAAHQLE DRIQDFVRRV EQRKVLLDMS VAFHTHVKEL WTWLEELQKE
LLDDVYAESV EAVQDLIKRF GQQQQTTLQV TVNVIKEGED LIQQLRDSAI SSNKTPHNSS
INHIESVLQQ LDEAQAQMEE LFQERKIKLE LFLQLRIFER DAIDIISDLE SWNEELTGQM
NDFDTEDLTL AEQRLQHHAD KALTMNNLTF DVIHQGQELL QYVNEVQASG VELLCDRDVD
MATRVQDLLE FLHEKQQELD LAAEQHRRHL EQCVQLRHLQ AEVKQVLGWI RNGESMLNAG
LITASSLQEA EQLQREHEQF QHAIEKTHQS ALQVQQKAEA LLQANHYDMD MIRDCAESVA
SHWQQLMLKM EDRLKLVNAS VAFYKTSEQV CSVLESLEQE YKREEDWCGG ADKLGPNCET
DHVTPMISKH LEQKEAFLKA CTLARRNADV FLKYMHRNSV NMPGMLSHVK APEQQVKNIL
NELLQRENRV LHFWTMKKRR LDQCQQYVVF ERSAKQALEW IHDTGEFYLS THTSTGSSIH
HTQELLKEHE EFHITAKQTK ERVKLLIQLA DGFCEKGHSH AGEIKKWVTA VDKRYRDFSL
RMDKYRCSLE KALGISSDSN KSKDLQLDII PATAPGSEVK LRDAAAHELN EEKRKSARRK
EFIMAELIQT EKAYVRDLRE CMDTYLWEMT SGVEEIPPGI LNKEHIIFGN MQDLYEFHHN
IFLKELEKYE QLPEDVGHCF VTWADKFQMY VNYCKNKPDS TQLILEHAGN YFDEIQQRHR
LANSISSYLI KPVQRITKYQ LLLKELLTCC EEGKGEIKDG LEVMLSVPKK ANDAMHLSML
EGFDENIESQ GELILQDSFQ VWDPKTLIRK GRERHLFLFE MSLVFSKEVK DSNGRSKYIY
KSKLFTSELG VTEHVEGDPC KFALWVGRTP TSDNKIVLKA SSIENKQDWI KHIREVIQER
TIHLRGALKE PIHIPKTATT KHHKGRRDGE DLDSQGEGSS QPDTISLASR TSQNTLDSDK
LSGGCELTVV IHDFMASNSN ELTVRRGQTV EVLERCHDKP DWCLVRTTDR SPAQEGLVPC
SMLCIAHSRS SMEMEGIFNH KDTLSVCSND SIMPGSSATL QPGHGIGSHT SPGPKRPGNT
LRKWLTSPVR RLSSGKADGH VKKLAHKHKK SREVRKSGEM TIGSQKDSDD SAATPQDETL
EERVRNEGLS SGTLSKSSSS GMQSCGEEEG EEGADSVPLP PPMAIQQHSL LQPDSQDDKT
SSRLSVRPSS SETPSAAELV SAIEELVKSK MALEDRPSSL SVEQGDSSSP SFNPSDNSLL
SSSSPMEEMD ERRASILKKR HFILLELVET ERDYVRDLGL VVEGYMSRMK EEGVPDDMKG
KDKIVFGNIH QIYDWHKDFF LRELEKCLED PDRLGPLFLK QERRLNMYVV YCQNKPKSEH
IVSEYIDTYF EDLKQRLGHR LQITDLLIKP VQRIMKYQLL LKDFLKHSKK AGLESPDLEK
AVEVMCIVPK RCNDMMNVGR LQGFDGKIVA QGRLLLQDTF MVSDPDGGLL GRMKERRVFL
FEQLVIFSEP LDKKKGFSLP GFLYKNSIKI SCLGLEENVE GDPCKFILTS RSASGAVESF
VLHSSHPGVR EVWTLQISQI LESQRNFLNA LTSPIEYQRN HVGASSAPSI GAPGGGNSGS
SAAPGGGGGS SQSSSIPSGP QGGSRRPSRI PQPSRLPQPL RHHPGADPDG SNKMSGLSPR
PVPPPLLPVG GSPQGKRPIH TTEDQAYTPI PRATVGPLPS TPTSKPRPGA VSPMASPMAT
PSGSGFWSSM PGSPASRPGS FTFPGEAGET PVRQSSNQSQ THRHSTHSKE ADRMSTCSSA
SEQSIQSTQS NGSESSSSSS VSTMLVTQDY TAVKEDEISV IQGEVVQILA SNQQNMFLVF
RAATEQGPAA EGWIPGFVLG HTSTIVPDCP EGSIKKSSSW HTSLRIRKKS EKKEKEAKKE
TKLENGYRKS RDGLANKVSV KLLNPNYIYD VPPEFLVPLS DVTCDNGESV TLRCKVCGRP
RATVSWKGPN QSNLTNNGHF SIAYSDTGEA TLRIIGVASE DDGVYTCVAT NELGSVTSSA
SLRVLAVSTD GVRVSWKDNF ESHYTEVVEL GRGRFSVVKR CDHRGTKRTV AVKHVNKKLM
RRDRVTQELN LLQRLQHPHI VTLIDTYETP SSYALVLEMA DQGRLLDYIV SWGNLTEEKV
ACYLRNVLEA LHYLHNCRIA HLDIKPENLL VSHTASGQPI VKLTDFGDAV QLNSAHYVHP
LLGSPEFASP ELVLGEPVSL TSDLWSLGVV TYVLLSGASP FLDESAEETC LNICRLDFSF
PRDYFQGVSQ AARDFVCLLL KTDPGRRPPA GLCLQEPWLQ AGQGDGRAEG CLDTSRLISF
IDRRKHQTDA RPIGGVRSFI HGRLQPRV
//
