ID A0A7K6PMJ6_9CORV Unreviewed; 3012 AA.
AC A0A7K6PMJ6;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN Name=Trio {ECO:0000313|EMBL:NWW62511.1};
GN ORFNames=IFRKOW_R06477 {ECO:0000313|EMBL:NWW62511.1};
OS Ifrita kowaldi (blue-capped ifrita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Corvoidea; Cinclosomatidae; Ifrita.
OX NCBI_TaxID=461245 {ECO:0000313|EMBL:NWW62511.1, ECO:0000313|Proteomes:UP000542689};
RN [1] {ECO:0000313|EMBL:NWW62511.1, ECO:0000313|Proteomes:UP000542689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-029-41 {ECO:0000313|EMBL:NWW62511.1};
RC TISSUE=Liver {ECO:0000313|EMBL:NWW62511.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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:NWW62511.1}.
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DR EMBL; VZRS01008072; NWW62511.1; -; Genomic_DNA.
DR Proteomes; UP000542689; 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; 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:UP000542689};
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 1..134
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1216..1391
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1403..1515
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1580..1645
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1893..2069
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2081..2195
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2466..2531
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2600..2690
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2711..2965
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1525..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1662..1831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1851..1889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2211..2467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2554..2575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 681..708
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1553..1573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1718..1729
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1730..1743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1761..1779
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1860..1878
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2216..2229
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2230..2247
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2277..2295
FT /note="Polar residues"
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 2441..2453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2454..2467
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2558..2575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWW62511.1"
FT NON_TER 3012
FT /evidence="ECO:0000313|EMBL:NWW62511.1"
SQ SEQUENCE 3012 AA; 340856 MW; 2572295085CCF8B2 CRC64;
SGGRDKRGGP ILTFPARSNH DRIRQEDLRR LISYLACIPS EEVCKRGFTV IVDMRGSKWD
SIKPLLKILQ ESFPCCIHVA LIIKPDNFWQ KQRTNFGSSK FEFETNMVSL EGLTKVVDPS
QLTPEFDGCL EYNHEEWIEI RVAFEDYISN ATHMLSRLEE LQDILSKKEM PQDLEGARNM
IEEHSQLKKK VIKAPIEDLD VEGQKLLQRI QSSDSFPKKN SGSGNADLQN LLPKVSTMLD
RLHSTRQHLH QMWHVRKLKL DQCFQLRLFE QDAEKMFDWI THNKGLFLNN YTEIGTSHPH
AMELQTQHNH FAMNCMNVYV NISRIMSVAN RLIESGHYAS QQIKQIASQL EQEWKAFAAA
LDERSTLLDM SSIFHQKAEQ YMSNVDSWCK ACGEVELPSE LQDLEDAIHH HQGIYEHITL
AYSEVSQDGK SLLDKLQRPL TPGSSDSLTA SANYSKAVHH VLDVIHEVLH HQRQLENIWQ
HRKVRLHQRL QLCVFQQDVQ EVLDWIENHG EAFLSKHTGV GKSLHRARAL QKRHEDFEEV
AQNTYTNADK LLEAAEQLAQ TGECDPEEIF QAAHQLEDRI QDFVRRVEQR KILLDMSVSF
HTHVKELWTW LEELQKELLD DVYAESVEAV QDLIKRFGQQ QQTTLQVTVN VIKEGEDLIQ
QLRDSAISSN KTPHNSSINH IETVLQQLDE AQSQMEELFQ ERKIKLELFL QLRIFERDAI
DIISDLESWN DELSQQMNDF DTEDLTIAEQ RLQHHADKAL TMNNLTFDVI HQGQDLLQYV
NEVQASGVEL LCDRDVDMAT RVQDLLEFLH EKQQELDVAA EQHRKHLEQC VQLRHLQAEV
KQVLGWIRNG ESMLNAGLIT ASSLQEAEQL QREHEQFQHA IEKTHQSALQ VQQKAEAMLQ
ANHYDMDMIR ECAEKVASHW QQLMLKMEDR LKLVNASVAF YKTSEQVCSV LESLEQEYKR
EEDWCGGADK LGPNSETDHV TPMISKHLEQ KEAFLKACTL ARRNADVFLK YLHRNSVNMP
GMVTHIKAPE QQVKNILNEL FQRENRVLHY WTMRKRRLDQ CQQYVVFERS AKQALEWIHD
NGEFYLSTHT STGSSIQHTQ ELLKEHEEFQ ITAKQTKERV KLLIQLADGF CEKGHAHATE
IKKCVTAVDK RYRDFSLRME KYRTSLEKAL GISSDSNKSS KSLQLDIIPA SVPGSEVKLR
DAAHELNEEK RKSARRKEFI MAELIQTEKA YVRDLRECMD TYLWEMTSGV EEIPPGIVNK
EHIIFGNMQE IYEFHNNIFL KELEKYEQLP EDVGHCFVTW ADKFQMYVTY CKNKPDSTQL
ILEHAGAYFD EIQQRHGLAN SISSYLIKPV QRITKYQLLL KELLTCCEEG KGEIKDGLEV
MLSVPKRAND AMHLSMLEGF DENIESQGEL ILQESFQVWD PKTLIRKGRE RHLFLFEMSL
VFSKEVKDSS GRSKYIYKSK LFTSELGVTE HVEGDPCKFA LWVGRTPTSD NKIVLKASSI
ENKQDWIKHI REVIQERTIH LKGALKEPIH IPKTAPTTKQ KGRRDGEDLD SQGDGSSQPD
TISIASRTSQ NTLDSDKLSG GCELTVVIHD FTACNSNELT IRRGQTVEVL ERPHDKPDWC
LVRTTDRSPA AEGLVPCGSL CIAHSRSSME MEGIFNHKDS LSVSSNDASP PASVTSLQPH
MIGAQSSPGP KRPGNTLRKW LTSPVRRLSS GKADGHVKKL AHKHKKSREV RKSADAGSQK
DSDDSAATPQ DETVEERGRN EGLSSGTLSK SSSSGMQSCG EEEGEEGADA VPLPPPMAIQ
QHSLLQPDSQ DDKTSSRLLV RPTSSETPSA AELVSAIEEL VKSKMALEDR PSSLLVDQGD
SSSPSFNPSD NSLLSSSSPI DEMEERKSSS LKRRHYVLQE LVETERDYVR DLGYVVEGYM
ALMKEDGVPD DMKGKDKIVF GNIHQIYDWH RDFFLGELEK CLEDPEKLGS LFVKHERRLH
MYIVYCQNKP KSEHIVSEYI DTFFEDLKQR LGHRLQLTDL LIKPVQRIMK YQLLLKDFLK
YSKKANLDTT ELEKAVEVMC IVPKRCNDMM NVGRLQGFDG KIVAQGKLLL QDTFLVTDQD
AGLLPRCKER RVFLFEQIVI FSELLDKKKG FSMPGFLFKN SIKVSCLSLE ENVDSDPCKF
ALTSRTGDVT ETFILHSASP GVRQLWIHEI NQILENQRNF LNALTSPIEY QRNHSSGGGG
SGSSSGNSGG PSSCSGIPSS SRSRPSRIPQ PVRHHSPVLV SSAASAQAEG DKMSGMSIHN
HSLPHYNTSL ETGLSQPDRH PPSAEPDGPQ REAEQIPKMK VIESPRKTAG NISGSADGAQ
KDSRGISEDS RTRNSIGSLT LGKPRPGAIS PMNSPLSTTF PSPFGKETFP PSSPLQKGSF
WSSIPASPAS RPGSFTFPGD NDSLQRQVHR HSSHSKDTDR MSTCSSTSEQ SVHSTQSNGS
ESSSSSNIST MLVTHDYTAV KEDEINVYQG EVVQILASNQ QNMFLVFRAA TDQCPAAEGW
IPGYVLGHTS AIIIDNPDGT IKKSTSWHTA LRLRKKSEKK DKDGKREGKL ENGYRKSREG
LANKVSVKLL NPNYIYDVPP EFIIPLSEVT CETGETIVLR CKVCGRPKAS VTWKGPDHNT
LSNDGHHSIS YSDLGEASLK IVGVTAEDDG IYTCIAANDM GSVSSSASLR VLGPGSDGIM
VIWKDNFDSH YSEVAELGRG RFSVVKKCDQ KGTKRAVATK FVNKKLMKRD QVTHELGVMQ
NLQHPQLIGL LDTFETSTNY ILVLEMADQG RLLDYVVRWG NLTEGKIRLY LGEILEAVQY
LHNCRIAHLD LKPENILVDQ SSTKPTIKLA DFGDAVQLNT TYYIHQLLGN PEFAAPEIIL
GNPVSLTSDV WSIGVLTYVL LSGVSPFLDE SVEETCLNIC RLDFSFPDDY FKGVSQKAKD
FVCFLLQDDP AKRPSAALAL QEQWLQLGNS KSSDSIDISR LTSFIERRKH QNDVRPIRSI
KNFLQSRLLP RV
//
