ID A0A3L8SS13_CHLGU Unreviewed; 1088 AA.
AC A0A3L8SS13;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=DV515_00004122 {ECO:0000313|EMBL:RLW06957.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW06957.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW06957.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW06957.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW06957.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
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:RLW06957.1}.
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DR EMBL; QUSF01000008; RLW06957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SS13; -.
DR STRING; 44316.ENSEGOP00005003307; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
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; cd05597; STKc_DMPK_like; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF31; SERINE_THREONINE-PROTEIN KINASE MRCK ALPHA; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR Pfam; PF15796; KELK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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 Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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:UP000276834};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 83..349
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 350..420
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 550..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 708..820
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 914..941
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 638..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1088 AA; 126233 MW; 15C94704FAD5104B CRC64;
MICIGNEGED LLKYVTACAY ARTFKETIFS NMSPCGRSPV NWCSDVLGSN FLPKTAWLYI
DISPRAKPFT SKVKQMRLHK EDFEILKVIG RGAFGEVAVV KLKNADKVFA MKILNKWEML
KRAETACFRE ERDVLVNGDN QWITTLHYAF QDENYLYLVM DYYVGGDLLT LLSKFEDRLP
EDMARFYLAE MVIAIDSVHQ LHYVHRDIKP DNILMDMNGH IRLADFGSCL KLMEDGTVQS
SVAVGTPDYI SPEILQAMED GKGKYGPECD WWSLGVCMYE MLYGETPFYA ESLVETYGKI
MNHKERFQFP AQVTDVSESA KDLIRRLICS REHRLGQNGI EDFKNHPFFA GIDWDNIRNC
EAPYIPEVSS PTDTSNFDVD DDCLKNSETM PPPSHTAFSG HHLPFVGFTY TNRSCLRLTA
GPPSMDLDAS IQRTLEDSLA TEAYERRIRR LEQEKLELSR KLQESTQTVQ ALQYSTVDGP
ITASKDLEIK SLKEEIEKLK KQVTESGQLE QQLEEASTAR RELDDASRQI KAFEKQVRTL
KQEREDLNKE LAESSDRLKS QAKELKDAHS QRKLAMQEFS EMNERLTDLH SQKQKLARQL
RDKEEEMEVV MQKVESLRQE LRRTERLKKE LEVQAEAAAA EASKDRKLRE RSEQYSKQLE
SEVEGLKQKQ VGRSPGVSSI EHQQEITKLK ADLEKKSVFY EEELSKREMM HANEIKSLKK
ELRDAESQQL ALKKEIMVLK DKLEKTRREN QSEREEFETE FKQKYEREKI LLTEENKKLT
NELDKLTTMF ERLSMNNRQL EEEMRDLADK KESVAHWEAQ ITEIIQWVSD EKDARGYLQA
LASKMTEELE ALRNSSLGAR ATDMPWKMRR FAKLDMSARL ELQSALDAEI RAKQAIQDEL
NKVKASCIST ECKLQESEKK NMELLADIER LKKETEELRS EKGVKHQDSQ NSFLAFLNAP
TSALDQFEIC KIQIIAINFL STDPFFKKMN LFNTFVTSRQ KTRIGRKPGR KKLKQYYRFI
VFFSNQHKQS IIFLLKEHLR RNIGQTEFRR YKAPPLQLDI NLKFACFFPD ANTASSHLAM
KEHNPCCD
//
