ID A0A2U9D0M3_SCOMX Unreviewed; 1447 AA.
AC A0A2U9D0M3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=dual-specificity kinase {ECO:0000256|ARBA:ARBA00013203};
DE EC=2.7.12.1 {ECO:0000256|ARBA:ARBA00013203};
GN ORFNames=SMAX5B_015934 {ECO:0000313|EMBL:AWP21486.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP21486.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP21486.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. Lammer subfamily.
CC {ECO:0000256|ARBA:ARBA00037966}.
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DR EMBL; CP026264; AWP21486.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000003872; -.
DR Proteomes; UP000246464; Chromosome 22.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14215; PKc_CLK2; 1.
DR Gene3D; 2.30.30.140; -; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR040880; DUF5604.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR041292; Tudor_4.
DR PANTHER; PTHR45646:SF6; DUAL SPECIFICITY PROTEIN KINASE CLK2; 1.
DR PANTHER; PTHR45646; SERINE/THREONINE-PROTEIN KINASE DOA-RELATED; 1.
DR Pfam; PF18300; DUF5604; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF18358; Tudor_4; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AWP21486.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1109..1425
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 31..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1074
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1447 AA; 166743 MW; DEAE6EC01FBA9B70 CRC64;
MTPGGSHSTT IGSARPIMLM LASEPQRQLL NERRDMSDSP CESVVSMNEN LGGRTSSAND
SFGQIKKAVV VLTRLPDYKV SALRPPTPPQ FYSEDESLSS SDSDMQWEPE EDSSDSDFSF
SNNKRKVAKL PRADTTKTPA PSTSSNNNDN NNPKVAASTS GHWINDKSKI RPNLPEEEVK
VGMMVLARRM HMRWRRGKVM EIVTKEDGRI KYKVSFEEKG KSLVSGHHIA FDTTPTLEKL
YIGARVVVQC QDNNLWFRPA ILAELPSRKN HLRFLVFMDD HTPTYVGLPI LHLVCRPLED
VVETLPDGHH KCFMRQYLKD WPYPHLTQYK AGESGIVELN GVKQNCDVQV VDCSLMQVLF
QDSQHQEWIH RGSFRLEQHM ARLLQLQDTG GSSESDGDVS AQQLQETRKT PRLKTSPTGT
RMEGDEMEMS KEELQRWIRA KVKNSCLICP DVLKKGNALQ LLLERREKQA ARLLKLCESV
AACEVIVKKQ YSLLGLEYRD TDSDDDDKSS GCGHLPPSPC ESTHSETQVR FSPAANSRTT
LVPKRPDSEN LNRHNPKKSL MKRPVVVLTR LPEWRISALC PLTPPNYSEG EVFGDSDCDQ
QWEPVDDPRN SDFSVTREAS LCIISASSQA PSQATEDPPR VPQGEVSMNM TVLARRRAMS
WQRGKIMDIL SKEDGRLKYK VNFEGKKKSL VSGHHIAFVT SPNVEHLFVG ARVVVKCDAE
QRHFCPAVLA ELACKKNQHR FLVFIDDQTP VYVTLYSIRL VCRPLADPLD DIVDDTHRNF
MKEYMKSWPF QPLTQFLEGK VINAEYNGFQ QECTVLEIDC SLVQVIFQDD QHREWLYRGS
SRLERVIIMK QQMELKKAAG QKNSPTSGNS KTKLQTVEFY FEENEVVRHK SRRLVNTDWA
QGGVTRRQSG PDRAEPTEHT EKRRPSLLAN SAASSDDRAR SKRIKEDTGD VTTDFLWDKR
TGLAAKTREL LQRPRCLHEA PLPPCYLRQP LVFRSFDNRS TEHRPFDRRY CERDRDRERE
PHGAAESYYP RNFSPTMYDY RRGRERERER DESYRRKGSR RKHKRRRRRT RSYSHSSSRS
NSRTRALSVR DDEEGHLICR SGDVLQERYE IVSTLGEGTF GRVMQCIDHR RGGAHVALKI
IKNVEKYKEA ARLEINVLEK INEKDPDNKF LCVQMYDWFD YHGHMCISFE LLALSTFDFL
KENNYLPYSI GQVRHMAYQI CLAVKFLHDN KLTHTDLKPE NILFVNSDFT MSFNVEKKRE
ERTVKSTAVR VVDFGSATFD HEHHSTIVST RHYRSPEVIL ELGWSHPCDV WSIGCILFEY
YLGFTLFQTH DNREHLAMME RILGPVPSRM IRKTRKQKYF YRGRLDWDES SSAGKYVREN
CKPLRRYLLS EAEEHHQFFD LIESMLEYEP SKRLVLADSL KHPFFESSGA GEAAGSKTWE
GNRDISR
//
