ID S7NU87_MYOBR Unreviewed; 1409 AA.
AC S7NU87;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=D623_10024806 {ECO:0000313|EMBL:EPQ20516.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ20516.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR EMBL; KE164845; EPQ20516.1; -; Genomic_DNA.
DR eggNOG; KOG0587; Eukaryota.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EPQ20516.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EPQ20516.1}.
FT DOMAIN 1..218
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1096..1383
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 213..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..265
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..769
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..843
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1409 AA; 159985 MW; 1B3B4B8A69D7C8F1 CRC64;
MLKKYSHHRN IATYYGAFIK KNPPGMDDQL WLVMEFCGAG SVTDLIKNTK GNTLKEEWIA
YICREILRGL SHLHQHKVIH RDIKGQNVLL TENAEVKLVD FGVSAQLDRT VGRRNTFIGT
PYWMAPEVIA CDENPDATYD FKSDLWSLGI TAIEMAEGAP PLCDMHPMRA LFLIPRNPAP
RLKSKKWSKK FQSFIESCLV KNHSQRPATE QLMKHPFIRD QPNERQVRIQ LKDHIDRTKK
KRGEKDETEY EYSGSEEEEE ENDSGEPSSI LNLPGESTLR RDFLRLQLAN KERSEALRRQ
QLEQQQRENE EHKRQLLAER QKRIEEQKEQ RRRLEEQQRR EKELRKQQER EQRRHYEEQM
RREEERRRAE HEQEYIRRQL EEEQRQLEIL QQQLLHEQAL LLEYKRKQLE EQRQAERLQR
QLKQERDYLV SLQHQRQEQR PVEKKPLYHY KEGMSPSEKP AWAKEVEERS RLNRQSSPAM
PHKVANRISD PNLPPRSESF SISGVQPART PPMLRPVDPQ IPHLVAVKSQ GPALTASQSV
HEQPKGLSGF QEALNVTSHR VEMPRQNSDP TSENPPLPTR IEKFDRSSWL RQEEDIPPKV
PQRTTSISPA LARKNSPGNG SALGPRLGSQ PIRASNPDLR RTEPILESPL QRTSSGSSSS
SSTPSSQPSS QGGSQPGSQA GSSERTRVRA NSKSEGSPVL PHEPSKVKPE ESRDITRSSR
PADLTALAKE LRELRIEETN RPLKKVTDYS SSSEESESSD EEEEDGESET HDGTVAVSDI
PRLISVAINV SGTGLWDLTA LAKELRELRI EETNRPLKKV TDYSSSSEES ESSDEEEEDG
ESETHDGTVA VSDIPRLIPT GAPGGTEQYN VGMVGTHGLE TSHADTFSSS ISREGTLMIR
ETSGEKKRSG HSDSNGFAGH INLPDLVQQS HSPAGTPTEG LGRVSTHSQE MDSGTETSGE
KKRSGHSDSN GFAGHINLPD LVQQSHSPAG TPTEGLGRVS THSQEMDSGT EYGMGSSTKA
SFTPFVDPRV YQTSPTDEDE EDEESSAAAL FTSELLRQEQ AKLNEARKIS VVNVNPTNIR
PHSDTPEIRK YKKRFNSEIL CAALWGVNLL VGTENGLMLL DRSGQGKVYN LINRRRFQQM
DVLEGLNVLV TISGKKNKLR VYYLSWLRNR ILHNDPEVEK KQGWITVGDL EGCIHYKVVK
YERIKFLVIA LKNAVEIYAW APKPYHKFMA FKSFADLQHK PLLVDLTVEE GQRLKVIFGS
HTGFHVIDVD SGNSYDIYIP SHIQGNITPH AIVILPKTDG MEMLVCYEDE GVYVNTYGRI
TKDVVLQWGE MPTSVAYIHS NQIMGWGEKA IEIRSVETGH LDGVFMHKRA QRLKFLCERN
DKVFFASVRS GGSSQVFFMT LNRNSMMNW
//
