ID D2HK37_AILME Unreviewed; 2037 AA.
AC D2HK37;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=PANDA_011718 {ECO:0000313|EMBL:EFB25943.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB25943.1};
RN [1] {ECO:0000313|EMBL:EFB25943.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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; GL192938; EFB25943.1; -; Genomic_DNA.
DR InParanoid; D2HK37; -.
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; PF12796; Ank_2; 1.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08477; Roc; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00364; LRR_BAC; 7.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
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; 3.
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};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 655..849
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1265..1548
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 32..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1810..1834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1868..1919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1868..1896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1897..1919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 2037
FT /evidence="ECO:0000313|EMBL:EFB25943.1"
SQ SEQUENCE 2037 AA; 227934 MW; BFE8E65E415E9BC3 CRC64;
MAGMSRRPPS MYWCVGPEGS AVCPERAMET CNGAEDMGSK PSTPSGDPTA QCPGTEGIHA
AYKQGNPSRA QHLLKEACDE STSQLEKGRL LSISAAYGDL ETVRYLLTER RVELPTEPTD
DNPAVVAAHF GHTDVVQELL ESLPGRSEWE QPKLFRGIFP LSCHLLPGPR SPQRLLNWML
ALACQRGHLG LVKLLVLTHG ADPESYAVRK NEFPVIVRLP LYAAIKSGNE DIAIFLLRHG
AFFCSYILLD SPDPSKHLLR KYFIEASALP SSCPGKMALR VKWSHLKLPW VDLDWLIDIS
CQITELDLSA NCLASLPSII PWGLINLRKL NLSKNHLGEL PAVQSSDEII CSRLLEIDIS
SNKLPHLPPG FLHLSKLQKL TASKNYLEKL FEEEGATNWI GLRKLQELDI SDNRLTELPA
LFLHCFKSLS SLNVSRNNLK VFPDAWACPL KCCKASKNAL ESLPDKMALF WKNHLRDVDF
SENALKEVPL GLFQLDALMF LRLQGNQLVA LPPPEKWTCR QLKTLDLSRN QFGKNEDGLK
TKRISFFTTR GRQRSGTETA GVLEFPAFLS ESLEVLCLND NHLDTVPPSV CLLKSLSELY
LGNNPGLREL TSELGQLSNL WQLDIEDLNI NNVPMEIKKE GPKAMLSYLR AQLRKAEKCK
LMKMIIVGPP RQGKSTLLEI LQTGRAPQVV HSEATIRTTK WELQRPAGSR AKVESVEFTV
WDIGGPASMA TVNQCFFTDK ALYVVVWNLA LGEEAVANLQ FWLLNIEAKA PNAVVLVVGT
HLDLIESKFR VERIATLRAY VLALCRSPSG SRATGFPDIT FKHLHELSCK SLEGQEGLRQ
LIFHVTCNMK DVGSTIGCQR LAGRLIPRSY LSLREAVLAE QQRRSLSDDV QYLTDRQLEQ
LVEQMPDNDI KDYEDLQSAI GFLIETGTLL HFPDTSHGLR NLYFLDPIWL SECLQRIFNI
KGSRSVAKNG VIRAEDLRML LVGTGFTQQT EEQYFQFLAK FEIALPVAND SYLLPHLLPS
KPGLDTHGMR HPKANTIQRV FKMSFVPVGF WQRFIARMLI SLAEMDLQLF ENRKNTKSRH
RKVTIYSFTG SQRNRCSTFR VKRNQTIYWQ EGLLVTFDGG YLSVESSDVN WKKKKSGGIK
IICQSEMRDF SAMAFITDHV NSLIDQWFPA LTATESDGTP LMEQYVPCPV CETSWAPHTD
PSEKAEGVQY FDMEDCVLTA IEQDFISCPR HPDLPVPLQE LVPELFMTDF PARLFLENSK
LEHSEDESSV LGQGGSGTVI YRARYQGQPV AVKRFQIKKF KNLANAPADT MLRHLRATDA
MKNFSEFRQE ASMLHALQHP CIVSLMGISI HPLCFALELA PLGSLNTVLS ENAKDSSFMP
LGHMLTQKIA YQIASGLAYL HKKNIIFCDL KSDNILVWSL DVKEHINIKL SDYGISRQSF
HEGALGVEGT PGYQAPEIRP RIVYDEKVDM FSYGMVLYEL LSGQRPALGH HQLQIAKKLS
KGIRPVLGQP EEVQFHRLQA LMMECWDTKP EKRPLALSVV SQMKDPTFAT FMYQLPCGKQ
TTFFSSQGQE YMVVFWDGKE ESRNYTVVNT EKGLMEVQRM SCAGMKLSCQ LKVQNSLWTA
TEDQKIYIYS LKGMCPLNTP QRALDTPAVV TCLLAVPVIK KNSYLVLAGL DDGLVAVFPV
VRGTPDNSCS YLCSHTANRS KFNIPDEDTR QNPYPVKAME VVNSGSEVWY SNGPGLLVID
CAALEISRRL EPYSAPSVVT SVVCSSECRG EEVVWCLDDR ANSLVMYHAA TYQLCARYFC
GDPSPLRDMF PVRPLGPQSP DSHAAGPKEP EGDGIADVSI MYSEELGTQI LTHQDSLTDY
CSMSSYSSNS PHRAPASSSS LPCSPASSSS VPFSTDCEDS DRLHEPAAGS DRSEHDLTPV
DGEAFSQHLQ AVRILAVKDV IWVPRRGGDV IVIGLEKDTG GQRGRVIAVL KARELTPHGV
LVDAAVVAKD TVVCGFENEN MEWCLAVWRG WGTREFDVFY QSYEELGRLE ACMRKRR
//
