ID A0A3L8SNQ5_CHLGU Unreviewed; 2402 AA.
AC A0A3L8SNQ5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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_00005341 {ECO:0000313|EMBL:RLW05197.1};
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:RLW05197.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW05197.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW05197.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW05197.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; 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:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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. {ECO:0000256|ARBA:ARBA00009903}.
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:RLW05197.1}.
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DR EMBL; QUSF01000011; RLW05197.1; -; Genomic_DNA.
DR STRING; 44316.ENSEGOP00005009170; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd05609; STKc_MAST; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR015022; MAST_pre-PK_dom.
DR InterPro; IPR023142; MAST_pre-PK_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF224; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 4; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF08926; DUF1908; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF140482; MAST3 pre-PK domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50106; PDZ; 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW 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 358..631
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 632..704
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 928..1016
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 9..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1608..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1701..1758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1819..2121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2183..2217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2258..2302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2316..2402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1046
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1181
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1722..1746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1831..1871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1904..1923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1924..1948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1969..2003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2062..2077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2189..2217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2281..2302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2345..2360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2375..2402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2402 AA; 262911 MW; 05C47D978BEF1340 CRC64;
MPVNGYVNFK TSSTSLRTGE ENLSGNSPQD SPRNFSPSAS AHFSFARRTD GRRWSLASLP
SSGYGTNTPS STVSSSCSSQ EKLHQLPYQP TPDELHFLSK HFCTTESIAS DNRCRTTAMR
PRSRSLSPGR SPACCDNEII MMNHVYKERF PKATAQMEER LQDIITNHSP ENTLPLADGV
LSFTHHQITE LARDCLDKSH QGLITSRYFL ELQQKLDKLL QEAQERSESG EMAFIKQLVR
KILIVIARPA RLLECLEFDP EEFYYLLEAA EGHAKEGQGI KTDIPRYIIS QLGLNKDPLE
EIAQLANCDS GTAEALEADE SINVSFPVML LLLLNVKKEN LSCNTSLKLQ RKPRESDFET
IKLISNGAYG AVYFVRHKET RQRFAMKKIN KQNLILRNQI QQAFVERDIL TFAENPFVVS
MYCSFETRRH LCMVMEYVEG GDCATLMKNM GPLPVDMARM YFAETVLALE YLHNYGIVHR
DLKPDNLLVT SMGHIKLTDF GLSKVGLMSL TTNLYEGHIE KDAREFLDKQ VCGTPEYIAP
EVILRQGYGK PVDWWAMGII LYEFLVGCVP FFGDTPEELF GQVISDEINW PEKDEAPPPD
AQDLITLLLR QNPLERLGTG GAYEVKQHQF FRSLDWNSLL RQKAEFIPQL ESEDDTSYFD
TRSEKYHHME TEEEDDTNDE DFNLEIRQFS SCSHRFSKVF SSIDRVTQIQ GEEKEDAGDK
TKSVALPSVE SLSWSSEYSE IQQISTSISS EIDSSRQQRN SGLLPKLSVS AEVEQDDSTS
SRGPREEQEK SAFVSDEIVQ DEPEVTTPAS TISSSTLSVG SFSEHLDQIN GRSESVDSPD
NSSKPAGEVA SHVARQRLES TEKKKISGKV TKSLSASALS LMIPGDVFGV SPLGSPMSPH
SLSSDLSSSR DSSPSRDSSI AAASPHQPIV IHSSGKKYGF TIRAIRVYVG DSDIYTVHHI
VWNVEEGSAA YQAGLKAGDL ITHINGEPVH GLVHTEVIEL LLKSGNKVSV MTTSFENTSI
KTGPARRNSY RSRMVRRSKK TKKKESLERR RSLFKKLAKQ PSPLLHTSRS FSCLNRSLSS
GESLPGSPTH SLSPRSPTPS YRSTPDFPSG TNSSQSSSPS SSAPNSPAGS GHIRPSTLHG
LGPKLGGQRY RSGRRKSAGS IPLSPLARTP SPTPQPTSPQ RSPSPLLGHS IGNTKIAQSF
PSKMHSPPTI VRHIVRPKSA EPPRSPLLKR VQSEEKLAPS YGSDKKHLCS RKHSLEVTQE
EVNKELSQRD ITLQSLEENV CDVPSLTRVR PAEQGCLKRP ISRKLGRQES IDELDREKLK
VKVVMKKQDF AEKANAAIHE PSSEPENPNT LRVEERDKKA FQKVLERSNQ FETKIVTVET
QSAGGILKDT LQKNANLRSN DGVALDGQTL CHGPPSNELS HISYDFKRIS PSCTLQDVLP
QSSDKILNGK GENTDKIVPT KEFVKFERLD GKLANIDYLR KKMSVEEKDD SVCPVLKPKM
TSNVHECLQL STGRPVNIQQ DSTAVADGRA FIGSAHATQM NSVSFVPLKT FSGQADMSIE
KSALISSEAP VRKSPSEYKL DGRSVSCLKP IEGTLDIALL SGPQASKTEL PLGVLPEGQS
TSSDGASPKP PVPQGSGGKA EMVSQKEQLL TYPKSSKVNI AEPQALQAGK SSPNPPLISV
ATEAMTEKKV SSLATKGSIS VVEAVQKKDT SPSKQKDHSV EVKSCVTQSQ SFKTTQTYSK
SFAGQNTPEK AVGKEKQIQK ELPVKQPISQ RGCEPISAKV EVIRESSLKV SVSDVLITTC
SKSNEKNCAD FAIPLEVQGK IQPAGPKAQP KDGRESLKQL GKDDSGVSKS FVEREITKQK
AESKKVTTEA KSDGLPSKWS MQLSRDSDHK IEKSAPVSSV QKDCAKDMGK KDQKSHTDIR
LQTSEREQSC QVPRQQLNTS SSPAVKEAVS RHSTIEVHVG VQEHVKPAAT CVESSSNKSR
PASDTSSSKS KSLDKQTLSQ KPCAPTVKEK EIVTQLSASS RKDGKHASKN VLDHLSPAPG
SSRRMNIEHV QAERPVGLDH GSITTLQMSS TAPDTKPKSS AAGPLPAGPE SSKQMQRQEA
AGLGESADQK QLRFSEKQTT APKFSTVKDC LSLNKEAERS PSNEVIVADK RPEVKICTDA
LYVQLDSGKV EPTLCLTASD VRGKGAEKAT MSSKTSQDIK GKAQVNQKQP EDANNQTAIK
HLPAASGQSS CRVAASPGKP LTCSSNFSEC RQEVSVSSVS AKSEASSAKV KPGSSELPAT
CKELSKKSTS STGSSKAEMT KSVSLMALHS ATVVAEAHHP ASNLGGKPGN QEKPLFVNTV
DVKGKDAVLT QQSASRKQNV GKDLPRSAAT PDRPNALSDD KDLARQRRGK EVSRSSAHKK
TC
//
