ID S7MS79_MYOBR Unreviewed; 1836 AA.
AC S7MS79;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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_10026021 {ECO:0000313|EMBL:EPQ06315.1};
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:EPQ06315.1, 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR629601-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR629601-3};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Alpha-type protein kinase family. ALPK subfamily.
CC {ECO:0000256|ARBA:ARBA00025760}.
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DR EMBL; KE161982; EPQ06315.1; -; Genomic_DNA.
DR eggNOG; KOG3614; Eukaryota.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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:0051262; P:protein tetramerization; IEA:InterPro.
DR CDD; cd16971; Alpha_kinase_ChaK1_TRMP7; 1.
DR Gene3D; 3.20.200.10; MHCK/EF2 kinase; 1.
DR Gene3D; 1.20.5.1010; TRPM, tetramerisation domain; 1.
DR InterPro; IPR004166; a-kinase_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029601; TRPM7_a-kinase_dom.
DR InterPro; IPR041491; TRPM_SLOG.
DR InterPro; IPR032415; TRPM_tetra.
DR InterPro; IPR037162; TRPM_tetra_sf.
DR PANTHER; PTHR13800:SF8; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY M MEMBER 7; 1.
DR PANTHER; PTHR13800; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL, SUBFAMILY M, MEMBER 6; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF18139; LSDAT_euk; 1.
DR Pfam; PF16519; TRPM_tetra; 1.
DR SMART; SM00811; Alpha_kinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR629601-2};
KW Calcium {ECO:0000256|ARBA:ARBA00022568};
KW Calcium channel {ECO:0000256|ARBA:ARBA00022673};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00022568};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR629601-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR629601-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000313|EMBL:EPQ06315.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022568};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR629601-3}.
FT TRANSMEM 915..934
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 946..964
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 985..1004
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1016..1035
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1056..1075
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1137..1160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1598..1828
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 603..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1771
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-1"
FT BINDING 1628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1652
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1724
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1757
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1773
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1781
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1798..1804
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1814
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1816
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1820
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
SQ SEQUENCE 1836 AA; 209941 MW; 79455DFF24EACB02 CRC64;
MKDSASAASA RAELVLRFPW AVPVRRPQLP TPETLPDRWL QAAEEEEEEL LPFRSPPREE
NGQHCIIRIV NSYSQKSWIE STLTKRECVY IIPSSKDPHR CFCGRLVKQH ACFTASLAMK
YSDVKLDDHF NQALEEWSVE KHTEQSPTDA YGVINFQGGS HSYRAKYVRL SYDTKTEVIL
QLLLKEWQME LPKLVISVHG GMQKFELHPR IKQLLGKGLI KAAVTTGAWI LTGGVNTGVA
KHVGDALKEH ASRSSRKICT IGIAPWGVIE NRNDLVGRDV VAPYQTLLNP LSKLNVLNNL
HSHFILVDDG TVGKYGAEVR LRRELEKTVN QQRIHARIGQ GVPVVALIFE GGPNVILTVL
EYLQESPPVP VVICEGTGRA ADLLAYIHKQ TEEGGNLPDA AEPDIISTIK KTFNFGQSEA
VHLFQTLMEC MKRKELITVF HIGSDEHQDI DVAILTALLK GTNASAFDQL ILTLAWDRVD
IAKNHVFVYG QQWLVGSLEQ AMLDALVMDR VAFVKLLIEN GVSMHKFLTI PRLEELYNTK
QGPTNPMLFH LVRDVKQGNL PPGYKITLID IGLVIEYLMG GTYRCTYTRK RFRLIYNSLG
GNNRRSGRNT SSGTPQLRKS HESFGNRADK KEKTRHNHFI KTAQPYRPKI DTAVEEGKKK
RTKDEIVDID DPETKRFPYP LNELLIWACL MKRQVMARFL WQHGEESMAK ALVACKIYRS
MAYEAKQSDL VDDTSEELKQ YSNDFGQLAV ELLEQSFRQD ETMAMKLLTY ELKNWSNSTC
LKLAVSSRLR PFVAHTCTQM LLSDMWMGRL NMRKNSWYKV ILSILVPPTI LMLEYKTKAE
MSHIPQSQDA HQMTMEDSEN NFQNITEEIP MEVFKEVRIL DSNEGKSEME IQIKSKKLPI
TRKFYAFYHA PIVKFWFNTL AYLGFLMLYT FVVLVQMEQL PSVQEWIVIA YIFTYAIEKI
RAIFMSEAGK ISQKIKVWFS DYFNISDTIA IISFFIGFGL RYGAKWNFEE AYKNHVFVAG
RLIYCLNIIF WYVRLLDFLA VNQQAGPYVM MIGKMVANMF YIVVIMALVL LSFGVPRKAI
LYPHEAPSWT LAKDIVFHPY WMIFGEVYAY EIDVCANDST IREICGPGTW LTPFLQAVYL
FVQYIIMVNL LIAFFNNVYL QVKAISNIVW KYQRYHFIMT YHEKPVLPPP LIILSHIASL
FCCICKRRKK DKTSDGPKLF LTEEDQKKLH DFEEQCVEMY FNEKDDKFNS GSEERIRVTF
ERVEQMCIQM KEVGDRVNYI KRSLQSLDSQ IGHLQDLSAL TVDTLKTLTA QKASEASKVH
NEITRELSIS KHLAQNLIDD GPVRPSVWKK QGVVNTLSSS LPQSSLESNN PFLCNIFMKD
EKDPQCNLLG QDLPLIPQRK EFNFPEAGSS CGALFQSAVS PPELRQRLHG VETLKLFSKN
KLGRSPNSIP HLSSPPTKLF VSTPSQPSCK SHLETITKDQ GTVCSKAAEG DIIEFGAFVG
HRDSMDLQRV KETSNKEEIF DQQNDRRNTI LEYSELPKYQ DWLQDRPSDR EIPSEEGTLN
AVERNNLMRL SQSIPFTPVP PRGEPVTVYR LEESSPSILN NSMSSWSQLG LCAKIEFLSK
EEMGGGLRRA VKVQCTWSEH DILKSGHLYI IKSFLPEVVN TWSSIYKEDT VLHLCLREIQ
QQRAAQKLTF AFNQMKPKSI PYSPRFLEVF LLYCHSAGQW FAVEECMTGE FRKYNNNNGD
EIIPTNTLEE IMLAFSHWTY EYTRGELLVL DLQGVGENLT DPSVIKAEEK RSGDMVFGPA
NLGEDAIKNF RAKHHCNSCC RKLKLPGKHF LNQCNV
//
