UniProt: A0A091PKD2

Database: UniProt
Entry: A0A091PKD2_HALAL

LinkDB:  A0A091PKD2_HALAL 
Original site:  A0A091PKD2_HALAL

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (33)   
   InterPro (18)   
   Pfam (5)   
   PROSITE (6)   
   SMART (4)   
All databases (43)   

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ID   A0A091PKD2_HALAL        Unreviewed;      2449 AA.
AC   A0A091PKD2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=N329_08165 {ECO:0000313|EMBL:KFQ07826.1};
OS   Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC   Accipitrinae; Haliaeetus.
OX   NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ07826.1, ECO:0000313|Proteomes:UP000054379};
RN   [1] {ECO:0000313|EMBL:KFQ07826.1, ECO:0000313|Proteomes:UP000054379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ07826.1};
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; KK660394; KFQ07826.1; -; Genomic_DNA.
DR   Proteomes; UP000054379; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0043226; C:organelle; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0030154; P:cell differentiation; 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; cd14068; STKc_LRRK2; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR032171; COR.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR025875; Leu-rich_rpt_4.
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; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR020859; ROC_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR   PANTHER; PTHR48005:SF13; SERINE_THREONINE-PROTEIN KINASE DDB_G0278509-RELATED; 1.
DR   Pfam; PF16095; COR; 1.
DR   Pfam; PF12799; LRR_4; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08477; Roc; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00364; LRR_BAC; 10.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 2.
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; 4.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   PROSITE; PS51424; ROC; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFQ07826.1};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054379};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFQ07826.1}.
FT   DOMAIN          1249..1432
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
FT   DOMAIN          1800..2059
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   COILED          242..269
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         1827
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ07826.1"
FT   NON_TER         2449
FT                   /evidence="ECO:0000313|EMBL:KFQ07826.1"
SQ   SEQUENCE   2449 AA;  277060 MW;  F22A5DA4FDF367EB CRC64;
     VLQMGWSLLC KLIEICPSTL QNIAPKDVGK DWEVLGVHQQ ILKMLTVHKG NINLSVIGLK
     ALNLLLMSDV IAFLLLEEEV DVFSLVFNAM HTFPKNEEIQ QHGCKALHKL FEKVPEEQLT
     EFVESKDHMI ILKVFKEFPE KEEVILPALY SLHSLAGPSS NVEVLMSGNV RCYNIIVEMM
     KSFPNSETVQ EVSCCLLHKL TLGNFFNILV LHKVPEVIVK AAKTYPENAK LQAAALSCLA
     LLTETIFLNQ DLEERKEEEE EEKLCWLEAC YRALELHRRN TDVLEAACWA LKNLFLYQRN
     LHEKIGDGDN QFPIDRAVML SMLMHSSSKE VFQAAASTLA ILSQQNVNIR KTLLAKGIHM
     NVLDIMRKHP HSPEVAESAC RILNRVFEGS FPHLDIMTVA VSEVVKAMRK HEKSLSLQLE
     ALRVLLHFMM PDMKNEHQNG SSRDVGDAAF VLTVKVIKSQ CLLEGTHSLV LNALNRFIGN
     PSIQKCGLKL LASVAECTGA LEILTQQGAT DTVLHTLQMY PDEQDIQCLG LSLLHSLITR
     KSLCIATMHV LSTVLVSALR RFKEVTEIQM HGFHTILSIL GLSPCFAKLL VHESFDTVIF
     HQMSMCFTDQ RDRQFQSLCC KCFAKIAEND DIKNMMLEKA CIEYNSIMAE CLLLLGADIN
     KKTKTNSLIY QVCEKGNNPK LVELLLANGA REQDVRSALA ISIKRGDSQI ISLLLKRLSL
     DVANSSICLG GFGIGRLEPS WLIPLFPDKL TPLRKQNAGS ALARMVLKFQ MKNISEDRSR
     ASSDLNFSED SVDKNYDWNF ISDPLVDSVF PFSDDIDSEG SEGSLFTKKK SNSIAVADWE
     MAFQRGSPTL PRHSYSVGPG SDYEPLMKQR RKFLPSDESP SISKFSPHIR PSDSLSSLIS
     EKEYIKSLDL SSNELENIDA ISQNSCLTSH LEHLEKLELH QNALTNIPEQ LCENLKCLTY
     LDLHSNRFTS FPTYLLKMNC IANLDISRND IGPSFALDPY LRCPTLKQLN LSYNQLVCTP
     EFLTNVAENL EQLLLEGNKI SCLCSPICLK ELKILNISKN NISSLAENVF MGCTKLEQFN
     ARMNALEIIP DLSSSITTLK LSQNHFINVP EAILLLPHLR SVDLSQNKII SLPGPMHWKS
     LNLRELLFNY NQIDVLDLSE KACAWSRLEK LHLSHNKLKE IPPQIGFLEN LTSLDVSHNP
     DLRFFPDEMG RLSKIWDLPL EGLHLNLDFK HVGFKARDII RFLQQRLKKA VPYNRMKLMI
     VGNTGSGKTT LLQQLMKCKR TELGSPKATV GIDVKDWIIQ GKGKMKKELI LNVWDFGGQE
     EFYSTHPHFM TQRALYLAVY DLSKGQAEVD AMKPWLFNIK ARASTSPVIL VGTHLDVSDE
     MQRKACMSKI TRELLNKRGF PAIQDYHFVN ATEESDSIIR LRKIIIKESL HFKIRDQPVV
     GQLIPDSYLE LEKRILLERK NVPVEFPVID QKRLLELVQE SQLQLDENEL PHAVHFLNES
     GVLLHFQDPA LQLRDLYFVD PKWLCKIMAQ ILMVKVEGFS KYPKGIVKRS DVEKFLLKKS
     RFPKIYMSQY FKLLEKFQIA LPLGEDQLLI PSSLSDHRPV IELPHCENSE IIIRLYEMPY
     FPMGFWSRLI NRLLEISPYM LSGRERALRP NRMYWRQGIY LNWSPEAYCL VESAVFDNNP
     DSFLKITAPS CRKGCILLGQ VVDHIDSLME EWFPGLLDID VCGEGETLLK KWALYSFQDG
     EEHQKILLDD LLKKAEEGDL LVNPDQPRHT IPIAQIAPDL ILADLPRNIM LNNDELEFDE
     APEFLLGDGG FGSVYRASYG GEEVAVKIFN KHTSLRLLRQ ELAVLCHLHH PSLVSLLAAA
     IRPRMLVMEL ALKGSLDRLL QQDNASLTRT LQHRIALHVA DGLRYLHSAM IIYRDLKPHN
     VLLFTLYPNS AVIAKIADYG IAQYCCRMGI KTSEGTPGFR APEVARGNVI YNQQADVYSF
     GLLLYDILTG GGRIMEGLKF PNEFDELAIQ GKLPDPVKEY GCAPWPKVEN LIRKCLKENP
     QERPTSSQVY EILNSAELIC LMRYVSIPST STAECMVAAN QSCKKAGVWI GNGNTEKAQL
     SFVNLNTDGH TCEDIADSKI LSLALVTLPT EKENWIVAGT QSGSLWAVNT EDETRRHRLQ
     KMSDSITCLY CNSLSKQSKQ KNFFLVGTAD GRLAVFEDKA VKCKGATPLK ILTVGNVSTP
     LMCLNESSYL SEKNIIWGGC GTKIIALTSD FSVQKLIETK TSQLFCHNAY SDANIISIAI
     DKSIYLAKKN SHFVEIWDKK TEKLSELIDC AHFLKDKVEK LNKESKHKLA YSGRVKTICL
     QKNTALWIGT GGGHILLLDL STRRPVRVID NFCDSVRVMI TAQLGSLKNV VLVLGYRYKS
     DTEDNKYHKE LQSCVSVWDI NLPHEVQNLK KHIEMRQELA EKMKSFSLD
//

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