ID A0A2I0MW96_COLLI Unreviewed; 3009 AA.
AC A0A2I0MW96;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 28-JAN-2026, entry version 38.
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|EMBL:PKK33947.1};
GN ORFNames=A306_00001754 {ECO:0000313|EMBL:PKK33947.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Columbimorphae; Columbiformes;
OC Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK33947.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK33947.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK33947.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK33947.1}.
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DR EMBL; AKCR02000001; PKK33947.1; -; Genomic_DNA.
DR STRING; 8932.A0A2I0MW96; -.
DR InParanoid; A0A2I0MW96; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
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-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: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 CDD; cd14113; STKc_Trio_C; 1.
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; 2.30.29.30:FF:000091; 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; 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; 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; 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};
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872};
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 5..151
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1233..1408
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1420..1532
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1597..1662
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1910..2086
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2098..2212
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2463..2528
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2597..2687
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2708..2962
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1542..1592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1679..1848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1868..1906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2228..2254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2289..2464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2551..2572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 698..725
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1570..1590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1679..1705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1746
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1747..1760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1778..1796
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1877..1895
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2297..2326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2339..2352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2371..2381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2394..2405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2438..2450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2451..2464
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2555..2572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3009 AA; 340616 MW; FB799A120270B49C CRC64;
MKAMEVLPIL KEKVAYLSGG RDKRGGPILT FPARSNHDRI RQEDLRRLIS YLACIPSEEV
CKRGFTVIVD MRGSKWDSIK PLLKILQESF PCCIHVALII KPDNFWQKQR TNFGSSKFEF
ETNMVSLEGL TKVVDPSQLT PEFDGCLEYN HEEWIEIRVA FEDYISNATH MLSRLEELQD
ILSKKEMPQD LEGARNMIEE HSQLKKKVIK APIEDLDVEG QKLLQRIQSS DSFPKKNSGS
GNADLQNLLP KVSTMLDRLH STRQHLHQMW HVRKLKLDQC FQLRLFEQDA EKMFDWITHN
KGLFLNSYTE IGTSHPHAME LQTQHNHFAM NCMNVYVNIN RIMSVANRLV ESGHYASQQI
KQIASQLEQE WKAFAAALDE RSTLLDMSSI FHQKAEQYMS NVDSWCKACG EVELPSELQD
LEDAIHHHQG IYEHITLAYS EVSQDGKSLL DKLQRPLTPG SSDSLTASAN YSKAVHHVLD
VIHEVLHHQR QLENIWQHRK VRLHQRLQLC VFQQDVQQVL DWIENHGEAF LSKHTGVGKS
LHRARALQKR HEDFEEVAQN TYTNADKLLE AAEQLAQTGE CDPEEIYQAA HQLEDRIQDF
VRRVEQRKIL LDMSVSFHTH VKELWTWLEE LQKELLDDVY AESVEAVQDL IKRFGQQQQT
TLQVTVNVIK EGEDLIQQLR DSAISSNKTP HNSSINHIET VLQQLDEAQS QMEELFQERK
IKLELFLQLR IFERDAIDII SDLESWNDEL SQQMNDFDTE DLTIAEQRLQ HHADKALTMN
NLTFDVIHQG QDLLQYVNEV QASGVELLCD RDVDMATRVQ DLLEFLHEKQ QELDVAAEQH
RKHLEQCVQL RHLQAEVKQV LGWIRNGESM LNAGLITASS LQEAEQLQRE HEQFQHAIEK
THQSALQVQQ KAEAMLQANH YDMDMIRECA EKVASHWQQL MLKMEDRLKL VNASVAFYKT
SEQVCSVLES LEQEYKREED WCGGADKLGP NSETDHVTPM ISKHLEQKEA FLKACTLARR
NADVFLKYLH RNSVNMPGMV THIKAPEQQV KNILNELFQR ENRVLHYWTM RKRRLDQCQQ
YVVFERSAKQ ALEWIHDNGE FYLSTHTSTG SSIQHTQELL KEHEEFQITA KQTKERVKLL
IQLADGFCEK GHAHATEIKK CVTAVDKRYR DFSLRMEKYR TSLEKALGIS SDSNKSSKSL
QLDIIPASVP GSEVKLRDAA HELNEEKRKS ARRKEFIMAE LIQTEKAYVR DLRECMDTYL
WEMTSGVEEI PPGIVNKEHI IFGNMQEIYE FHNNIFLKEL EKYEQLPEDV GHCFVTWADK
FQMYVTYCKN KPDSTQLILE HAGAYFDEIQ QRHGLANSIS SYLIKPVQRI TKYQLLLKEL
LTCCEEGKGE IKDGLEVMLS VPKRANDAMH LSMLEGFDEN IESQGELILQ ESFQVWDPKT
LIRKGRERHL FLFEMSLVFS KEVKDSSGRS KYIYKSKLFT SELGVTEHVE GDPCKFALWV
GRTPTSDNKI VLKASSIENK QDWIKHIREV IQERTIHLKG ALKEPIHIPK TAPTTKQKGR
RDGEDLDSQG DGSSQPDTIS IASRTSQNTL DSDKLSGGCE LTVVIHDFTA CNSNELTIRR
GQTVEVLERP HDKPDWCLVR TTDRSPAAEG LVPCGSLCIA HSRSSMEMEG IFNHKDSLSV
SSNDASPPAS VTSLQPHMIG AQSSPGPKRP GNTLRKWLTS PVRRLSSGKA DGHVKKLAHK
HKKSREVRKS ADAGSQKDSD DSAATPQDET VEERGRNEGL SSGTLSKSSS SGMQSCGEEE
GEEGADAVPL PPPMAIQQHS LLQPDSQDDK TSSRLLVRPT SSETPSAAEL VSAIEELVKS
KMALEDRPSS LLVDQGDSSS PSFNPSDNSL LSSSSPIDEM EERKSSSLKR RHYVLQELVE
TERDYVRDLG YVVEGYMALM KEDGVPDDMK GKDKIVFGNI HQIYDWHRDF FLGELEKCLE
DPEKLGSLFV KHERRLHMYI VYCQNKPKSE HIVSEYIDTF FEDLKQRLGH RLQLTDLLIK
PVQRIMKYQL LLKDFLKYSK KANLDTTELE RAVEVMCIVP KRCNDMMNVG RLQGFDGKIV
AQGKLLLQDT FLVTDQDTGL LPRCKERRVF LFEQIVIFSE LLDKKKGFSM PGFLFKNSIK
VSCLSLEENV DSDPCKFALT SRTGDVTETF ILHSASPGVR QLWIHEINQI LENQRNFLNA
LTSPIEYQRN HGSGGGGSGS SGSRPSRIPQ PVRHHSPVLV SSAASAQAEA DKMSGMSIHN
LSLPHYTTSL ETGLSQPDRH PPNAEPDGPQ REAEQIPKMK VIESPRKTAG NISGSADGAQ
KDSRGSSEDS RSRNSIGSLT LGKPRPGAIS PMNSPLSTTF PSPFGKETFP PSSPLQKGSF
WSSIPASPAS RPGSFTFPGA PEGPAPRHSS HSKDTDRMST CSSTSEQSVH STQSNGSESS
SSSNISTMLV THDYTAVKED EINVYQGEVV QILASNQQNM FLVFRAATDQ CPAAEGWIPG
YVLGHTSAVI IDNPDGTIKK STSWHTALRL RKKSEKKDKD GKREGKLENG YRKSREGLAN
KVSVKLLNPN YIYDVPPEFI IPLSEVTCET GETIVLRCKV CGRPKASVTW KGPDHNTLSN
DGHHSISYSD LGEASLKIIG VTAEDDGIYT CIAANDMGSV SSSASLRVLG PGSDGIMVIW
KDNFDSLYSE VAELGRGRFS VVKKCDQKGT KRAVATKFVN KKLMKRDQVT HELGVMQNLQ
HPQLIGLLDT FETSTNYILV LEMADQGRLL DYVVRWGNLT EGKIRLYLGE ILEAVQYLHN
CRIAHLDLKP ENILVDQSSA KPTIKLADFG DAVQLNTTYY IHQLLGNPEF AAPEIILGNP
VSLTSDVWSI GVLTYVLLSG VSPFLDESVE ETCLNICRLD FSFPDDYFKG VSQKAKDFVC
FLLQDDPAKR PSAALALQEQ WLQLGNSKSA DSIDISRLTS FIERRKHQND VRPIRSIKNF
LQSRLLPRV
//
