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Database: UniProt
Entry: A0A091Q5V6_LEPDC
LinkDB: A0A091Q5V6_LEPDC
Original site: A0A091Q5V6_LEPDC 
ID   A0A091Q5V6_LEPDC        Unreviewed;      2021 AA.
AC   A0A091Q5V6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
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   ORFNames=N330_02680 {ECO:0000313|EMBL:KFQ15587.1};
OS   Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX   NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ15587.1, ECO:0000313|Proteomes:UP000053001};
RN   [1] {ECO:0000313|EMBL:KFQ15587.1, ECO:0000313|Proteomes:UP000053001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ15587.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; KK688442; KFQ15587.1; -; Genomic_DNA.
DR   PhylomeDB; A0A091Q5V6; -.
DR   Proteomes; UP000053001; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043226; C:organelle; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR   CDD; cd14067; STKc_LRRK1; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR   Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR032171; COR.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR020859; ROC_dom.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR48055; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE EMS1; 1.
DR   PANTHER; PTHR48055:SF13; LEUCINE-RICH REPEAT SERINE_THREONINE-PROTEIN KINASE 1; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF16095; COR; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08477; Roc; 1.
DR   SMART; SM00248; ANK; 4.
DR   SMART; SM00364; LRR_BAC; 8.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS51450; LRR; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS51424; ROC; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFQ15587.1};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFQ15587.1}.
FT   DOMAIN          644..838
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
FT   DOMAIN          1254..1537
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1853..1883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ15587.1"
FT   NON_TER         2021
FT                   /evidence="ECO:0000313|EMBL:KFQ15587.1"
SQ   SEQUENCE   2021 AA;  226056 MW;  D3F07E0ABAC178A3 CRC64;
     SQLQPRMYWC VGTDEAAVCR GSNMEPQNGT VDMGGKQSTV GEVSIIQTPV TESIQDAYKA
     GDTSKAQELI KLSCEETALQ VEKCQLLGIA AAYGDLQAVR YLLKEALVVL PTEPNDDNAA
     VVAAYFGHKD VVKELLDSLR GKPIGLPLPV LKLFGSCPST CQQLLNWMLA IACQQGHLDV
     VKLLIRAYSA DPESCAVRKN EFPVLIRLPL YAAIKAGNED VAVFLLRNGA FFCSYILMDS
     PESSKHLLRK YFIETSPLPG SAPAKTALCV NWSNLKLPWV DLDWLIDISC QITELDLSAN
     CLVSLPSVIP WGLINLRKLS LADNQLTELP SVQSSDEIIC TRLLEVDVSS NRLSTLPSGF
     LHLKNLKKLI ASKNYMEKLF DEENTTNWIG LRKLQEFDVS DNRLVELPTV FLYCFKSLNI
     LNVSRNQLKV FPDPWACPLK CCKASRNSFE FLPDALTIFW KNHLREVDFS ENSLKEVPPG
     LFQLEALVSL KLLGNQLVTL PSQDKWNCKQ LKSLDLSKNQ LGKSDEGFKT KRIPFFTTKS
     RVRCGPEAGP FLEFPAFLSD SLEVLYLNDN QLDSVPQSVC LLKGLTELYL GNNPGIRELP
     PELGQLANLW QLDIEELNIS NVPAEIRKEG PKTVLAYLRA QLRRAEKCKL MKMIVIGPPR
     QGKSTLIEIL QTGKVPQMMH SDATIRTTKW ELPKPVGHKA KVDSVEFNVW DIGGPASMST
     VNQCFFTDKA LYIVVWNLAL GEEAVANLQF WLLNIEAKAP NSAVLVVGTH LDLIETKFRV
     ERIATLRAYV LALCRSPSGS RATGFPDITF KHLHELSCRT LEGLDGLRQL IFHVTCNMKD
     VGSSICSQKL AGRLIPRSYL SLQEAVLSEQ HRRSQSDDVQ YLTDRQIELI IEQTPGNDIK
     DYEDLQTAIN FLIETGTLLH FPDTSHGLRN LYFLDPVWLS ECLQRIFNIK SSKSVAKNGV
     IRAEDLRMLL VGTGFTEQTE EQYFQFLAKF EIALPVANNS YLLPHLLPTK PALDIHGFCH
     QTTNTVQRVF KMSFVPVGFW QRFIARMLIS LAEMDLQLFE NKKNTKTRNK KVTIYSFTGT
     QRNRCSTFRV KRTHTVYWQE GLFVTFDGGY LSVESSDVNW KKKKSGGIKI ICQSEVRDFS
     AMAFITDHVN SLIDQWFPAL TAMESDGTLL MEQYVPCHIC AASKPEENEC GEKAEDAQYF
     NMEDCVLTAI ELDYIMCPNH PDIPVSLQEL VPELFMTDFP ARLFLENSKL ECSENENNVL
     GQGGSGTVIY RARYQGKPVA VKRFQIKKCK GSPTSAADTM LKHLRAMDAM KNFSEFRQEA
     SMLHSLQHPC IVSLIGISIH PLCFALELAP LGSLTTVLSE NSKGSSFVPL GHMLTHKIAY
     QIVTGLAYLH KKNIIFCDLK SDNILVWSLD VKEHVNIKLS DYGISRQSFH EGALGVEGTP
     GYQAPEIRPR IVYDEKVDMF SYGMVLYELL SGQRPVLGQH QLQIAKKLSK GIRPVLGQPE
     EVQLYRMQAL MMECWDTKPE KRPLAISVVG QMKDPTFATF MYLLSCGKQS SFFSSQGQEY
     TVVFWDGKED TRNYTVVNPE KGVIEVERMS CPGMKLCCQL KFQNALWAAT EDQKISVYGL
     QGMCPLKTPQ KGLDTPATVS CFLVMPVVKK NAYVVLAGLS DGLVAVFSVS QGIPGDSCSY
     LCSHTANRSK FNIPDDDPRQ NPYPVKAMEI ANSGAEVWYS NGPGVLIIDC ATMEISRRLE
     PFSPPSVITS IACNSECHGE EVVWCLDDKS NFLVMYHVTT YQLCARYFCG DCSPLRDMFT
     IQQPSAAIPA TAPVNPRAME SHPPGDMSII YSPEVGTQIL NHQDSLTDYC SVSSYSSSPP
     DRITRCPSSL PSSPMSSSSG PVSTDFESFD KFHELKPSLD HDAMPVGDDT QHLQAVKILP
     VKDLIWIPRR GGDIIVIGLE KESGTQRGRV IAVLKAGELA PYGALVDAAL IAKDTVVCCF
     ENENMEWCLA VWRGWSARDF DVFYQAYEEL GRLETCMRKR R
//
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