ID A0AA88Q8K3_9TELE Unreviewed; 3028 AA.
AC A0AA88Q8K3;
DT 27-MAR-2024, integrated into UniProtKB/TrEMBL.
DT 27-MAR-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=Q8A67_008103 {ECO:0000313|EMBL:KAK2903390.1};
OS Cirrhinus molitorella (mud carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Cirrhinus.
OX NCBI_TaxID=172907 {ECO:0000313|EMBL:KAK2903390.1, ECO:0000313|Proteomes:UP001187343};
RN [1] {ECO:0000313|EMBL:KAK2903390.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Prfri {ECO:0000313|EMBL:KAK2903390.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAK2903390.1};
RA Liu H.;
RT "Chromosome-level Genome Assembly of mud carp (Cirrhinus molitorella).";
RL Submitted (AUG-2023) 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:KAK2903390.1}.
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DR EMBL; JAUYZG010000007; KAK2903390.1; -; Genomic_DNA.
DR Proteomes; UP001187343; 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-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; cd00096; Ig; 1.
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; 5.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP001187343};
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 51..197
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1271..1446
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1458..1570
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1647..1712
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1957..2133
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2145..2260
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2483..2548
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2617..2707
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2726..2981
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1610..1645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1731..1895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1908..1945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2280..2353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2419..2485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2569..2598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 736..763
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1620..1640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1731..1752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1793
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1794..1807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1825..1843
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1880..1892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1925..1942
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2283..2295
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2296..2310
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2431..2444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2468..2485
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2575..2598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2755
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 3028 AA; 343148 MW; AAF8D3FD81697082 CRC64;
MSSGEGEDTS KEAADIAAFF KSECSLPKCE PKLEFPSHTG FHRNEDMKAI EVLPILKEKV
AFLSGGRDRR GGPVLTFPAR SNHDRIRQED LRRLIAYLAG IPSEEVSRHG FTVIVDMRGS
KWDSIKPLLK ILQESFPSCI HVALIIKPDN FWQKQRTNFG SSKFEFETIM VSLEGLTKVV
DPSQLTPDFE GSLDYDHEEW IEVRVAFEDF TSNAARILSR LEELQDLVSQ RELPSDLDGS
RRAMEEHASL KKKVTKAPVE ELDTEGQRLL QRIQCGEKGR GDIQGLAPKV QALLDKLHAT
RQHLHQSWHM RKVKLDQCFQ LRLFQQDAEK MFDWIVHNKG LFLTTYTEIG ANHQHVLELQ
TQHNHFAMNC MNVYVNISRI MSVGNRLLES GHYATQQIQQ ISGQLEQEWK AFAAALDERS
TLLEMSANFH QKTDQYMSNM DSWCKACGEG ELPSELQDLE DTIHHHQGLY EHITAAYSEV
SQDGKALLDK LQRPLTPGSA DSLTASANYS KAVHHVLDII HEVLHHQRQL ENIWQHRKLR
LHQRLQLCVF QQDVQQVLDW IENHGEAFLS KHTGVGKSLH RARALQKRHE DFEEVAQNTY
TNADKLLEAA EQLAQTGECD PEEIYQAAHQ LEDRIQDFVR RVEQRKVLLD MSVAFHTHSK
ELWTWLEELQ KELLDDVYAE SVEAVQELIK RFGHQQQTTL QVTVNVIKEG EDLIQQLRDS
AISSNKTPHN SSMAHIESVL QQLDEAQAQM EELFQERKIK LELFLQLRIF ERDAIDVISD
LESWNEELSQ QMKEFDTEDL TLAEQRLQHH ADKALTMNNL TFHVIHQGQE LLQYVTEVQA
SGVELLCDRD VDMATRVQDL LDFLHEKQQE LDTAAEQHRR HLEQCVQLRH LQAEVKQVLG
WIRNGESMLN AGLITASSLQ EAEQLQREHE QFQHAIEKTH QSALQVQQKA EALLQANHYD
MDMIRDCAEK VASHWQQLML KMEDRLKLVN ASVAFYKTSE QVCSVLESLE QEYKREEDWC
GGTDKLGPNS ESDHVTPMIS KHLEQKEAFL KACTLARRNA DVFLKYLHRN SVNMPGMLAH
VKAPEQQVKN ILNELLQREN RVLHFWTMRK RRLDQCQQYV VFERSAKQAL EWIHDTGEFY
LSTHTSTGST IHHTQELLKE HEEFQITAKQ TKERVKLLIQ LADGFCEKGH AHASEIQKWV
ASVDKRYRDF SLRMDKYRSC LEKALGLSTD SNKASKDLQL DIIPASAPGA EVKLRDANHE
LNEEKRKSAR RKEFIMAELI QTEKAYVRDL RECMDTYLWE MTSGVEEIPP GIVNKEHIIF
GNMQDLYEFH HNIFLKELEK YEQLPEDVGH CFVTWADKFQ MYVNYCKNKP DSTQLILEHA
GAYFDEIQQR HRLANSISSY LIKPVQRITK YQLLLKELLT CCEEGKGEIK DGLEVMLSVP
KRANDAMHLS MLEGFDENIE SQGELILQES FQVWDPKTLI RKGRERHLFL FEMSLIFSKD
VKDSNGRSKY LYKSKLMTLE LGVTEHVEGD PCKFALWVGR TPTSDNKIVL KASCIENKQD
WIKHVREVIQ ERTIHLRGAL KEPIHIPKAT ATKHKGKRYV NNSHQSYSIS IDGEDLDSQG
DASSQPDTIS IASRTSQNTL DSDKLSGGSE LTVVIHDFMA SNGSELTVRR GQTVELVERP
QDKPEWCLVR TTDRSPAQEG LVPSSMLCIA HSRSSMEMEG IFNHKDTLSV SSNEGGLSGS
ATLQPGHLQS SPGPKRPGNT LRKWLTSPVR RLSSGKADGH VKKLAHKHKK SRDVRKNADA
GSQKDSDDSA ATPQDETIEE RMRNEGLSSG TLSKSSSSGM QSCGEEEGEE GPDSVPLPPP
MAIQQHSLLH QDSQEDKATS RLSGRPSSSE TPSAAELVSA IEELVKSKMS LEDRPSSLPV
ERGDSSSPSC NPSDNSLLSS SSPIDEMDER KTGFLKRRHY VLLELVETER DYVRDLGAVV
EGYMSRMKEE GVPDDMKGKD KIVFGNIHQI YDWHKDFFLG ELEKCLEDPD RLAPLFVRQE
RRLHMYIVYC QNKPKSEHIV SEYIDTYFED LKQRLGHRLQ ITDLLIKPVQ RIMKYQLLLK
DLLKFSKKAG LDTVDLEKAV EVMCVVPKRC NDMMNVGRLQ GFDGKIVAQG RLLLQDTFLV
SDQDGGLLSR MKERRVFLFE QIVIFSEPLD KKKGFSMPGY LFKNSIKVSW LGLEESPDND
PCKFILTSRS SAGSTEHYVL HSSNRAVCQA WIQQISSILE NQRNFLNALT SPIEYQRNHV
GASGLGGPSS SGLPGGSSSS AMGPSCGSRS RASRIPQPSS RLPQPVQHHH APAPDDRTSG
TCPLPDQDLN GEVPRMRVLE SPLKDLREDT QSGTPIPRAA VAPLSLTLTK PRLRVPSPIL
SPLNPQNFTV QKGSPFWASM PVSPTGRPGS YTEQSDTLSR NQCQTRRHST HSKELDRIST
CSSTSEQSLH STHSNGSESS SSSSVSTMLV TQDYVALKED EISVYQGEVV QILASNQQNM
FLVFRAATEQ GPAAEGWIPG YVLGHTSTII PDYPDGTLKK SSSWHTALRI RRKSEKRDKE
GRKESKPENG YRKSRDGSAN KVSVKLLNPN YIYDVPPEFV IPLNEVVCDR GDSVTLRCKI
CGQPKASVCW RGPDQSTLSN GGKYTLTHSE TGEVTLRISP ATLDDSGTYT CIASNDVGSV
TSSAYLRVLA TSCDGILWKD NFESLYTEVM ELGRGRFAVT KWCEQRGSRR SVAAKLVNKK
LMRREQVVQE LGVLQCLQHP HLVGLLDTYE TPASYVLILE IADQGRLLDY IVSWGNLTEE
KVSLYLRDIL EALHYLHTCR IAHLDLKPEN VLIEQTSTQP LVKLTDFGDA AHLSNAPYIH
PLLGSPEFSA PELVLGEPAA LASDLWSLGV LAYVMLSGAS PFLDESVEET CLNICRLDFS
FPEDYFRGVS QAARDFICVL LQGEPCRRPS AQVCLHEEPW LKLNAASGAA RLDTSRLISF
IERRKHQNDL RPVASFRAFL HSRLLSQT
//
