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Database: UniProt
Entry: S7PHL8_MYOBR
LinkDB: S7PHL8_MYOBR
Original site: S7PHL8_MYOBR 
ID   S7PHL8_MYOBR            Unreviewed;      2620 AA.
AC   S7PHL8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
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_10026736 {ECO:0000313|EMBL:EPQ07587.1};
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:EPQ07587.1, 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};
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DR   EMBL; KE162248; EPQ07587.1; -; Genomic_DNA.
DR   eggNOG; KOG0584; Eukaryota.
DR   Proteomes; UP000052978; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP 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   CDD; cd14030; STKc_WNK1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1.
DR   PANTHER; PTHR13902:SF46; SERINE_THREONINE-PROTEIN KINASE WNK1; 1.
DR   Pfam; PF12202; OSR1_C; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EPQ07587.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          222..480
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          924..1023
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1270..1362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1698..1731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1781..1802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2058..2087
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2107..2178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2201..2307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2350..2484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..693
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1270..1287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1300..1334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1338..1358
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1714..1731
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2108..2124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2125..2145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2268..2300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2371..2482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2620 AA;  276775 MW;  6D93572BEC7529A8 CRC64;
     MSGGAAEKQG GTPSSLFLSP PAPTPKNGSS SDSSVGEKLG AAGTDAGTGR TEEYRRRRHT
     MDKDSRGAAA TTTTTEHRFF RRSVICDSNA TALELPGLPL SLPQPTVAAV VPQSTPPEPH
     REETLTATVA AQVAQQPSAA VAAPREPAAP GPAASTAPSS ISKDRQIAQP DHVGSKEEPP
     SARSGSGGSS AKESQEERSQ QQDDIEELET KAVGMSNDGR FLKFDIEIGR GSFKTVYKGL
     DTETTVEVAW CELQDRKLTK SERQRFKEEA EMLKGLQHPN IVRFYDSWES TVKGKKCIVL
     VTELMTSGTL KTYLKRFKVM KIKVLRSWCR QILKGLQFLH TRTPPIIHRD LKCDNIFITG
     PTGSVKIGDL GLATLKRASF AKSVIGTPEF MAPEMYEEKY DESVDVYAFG MCMLEMATSE
     YPYSECQNAA QIYRRVTSGV KPASFDKVAI PEVKEIIEGC IRQNKDERYS IKDLLNHAFF
     QEETGVRVEL AEEDDGEKIA IKLWLRIEDI KKLKGKYKDN EAIEFSFDLD RDVPEDVAQE
     MVESGYVCEG DHKTMAKAIK DRVSLIKRKR EQRQLVREEQ EKRKQEESSF KQQVDQQSSA
     SQAGIKQLPS ASTGIPTAAT TSASVSTQVE PEEPEADQHQ QLQYQQPSIS VLSDGTVDSG
     QGSSVFTESR VSSQQTVSYG SQHEQAHSTG TLPGHTASVV QAQSQPHGVY PPSSMPRRGR
     SMSVCVPHLS AVPSLSRISP SAPSTPPPVQ SAPLSPPLLR TAPEETFAEK LCKALESVLP
     MHSASQRKHR RSSLPSLFVS TVAISQRRKS TSFLEAQTHH FQPLLRTVGQ NLLPPGGSPA
     NWTPEAVVML GTTASRITGE PCEIPVNPLF EPPQVYSDCR PGLVLSEEAH SFVPQEALYL
     AGVQYQAQVA EQYEGIPYNS PVLSSPMKQI PEQKPVQGGP TSRSVFEFPS GQAFLAQGQS
     QGQPSSSIVT GVSSSQPIQH SQQQQGIQQT APPQQTVQYS LPQTTTSSEA TTAQPVSQPQ
     ASQVLPQVSA GKQLPVSQPV PTIQGEPQIS VATQPSVVPV HSGAHFLPMG QPLPTSLLPQ
     YSVSQIPISA PHVSAAQTGF STLPITIAAG INQPLLTLAS SATASVIPGG STLASSQLPT
     LLQPVTQLPS QVHPQLLQPA VQSMGLPANL GQAAEVPLPS GDVLYQGFPP RLPLQYPGDS
     NIAPSSSVAS VCIPSTVLSP PMPTEALATP GYFPTVVQPY MESNLVVPVG SIGGQVQVSQ
     PAVSLAQAPT TSSQQAALES TQGVSQVAPP EPVPITQPQP TQPTTLVSSI DSAHSDVASG
     MSDGNENVPS SSGRHEGRTA KRHYRKSVRS RSRHEKTSRP KLRILNVSNK GDRVVECQLE
     THNRKMVTFK FDLDGDNPEE IATIMVNNDF ILATERESFV DQVREIIEKA DEMLSEDVSV
     EPEGDQGLES LQGKDDYGFS DSQKLEGEFK QPLPASSMTQ QIGIPTSSLT QVVHSAGRRF
     IVSPVPESRL RESKVFTGEI SDTVAASTSH GAGMNLSHSA SSLSLQQAFS ELKNAQMTEG
     PNTAPPNFSQ TGPTFPVVPP SMGSIAGVPT TAATTLSVSV PVTSCPLNDI STSVIQSEIT
     VPTEKGITTC TSVTSSELCI PPVSEESPVL SSMVSGITIP AVVSTSATSQ SVLAPTSGSV
     VSSIGTLPSR PVSTTSASAV SSAAAPGANP PPALSQPSAG STTTGAATLT SVSNTTPFPS
     IASQPSLQLS SSTSAPTLAE TVVVSAHSLD KISHSSTAGL ALSHSAPSSS SSPGAAVSSS
     ISQPGGVHPL VIPSVIASTP VLAQAAGPTS TPLLPQIPTI PPLAQPVASV PAVQQTLIHS
     QPQPALLPNQ PHTHCPEIDA DTQPKAPGID DIKTLEEKLR SLFSEHSSSG TQHASVSLET
     SLVVETNATP GIPTTAVAPS KLMTSTTSTC LPPTSLPLGT TGLPVIPVVT PGQVSTSVSY
     VSAPVSTTPG VKPATAPSKL PLTKAPVVSV GSELLAGIPS SEQLPPFPGP SQTQQPLEDL
     DAQLRRALSP ETIAVTSAVG PGSMVPPTAV TEAGAQPQKD VSQVTAASSG TGVFKTGRFQ
     VSVAMDDAQK EGKNKSEDAK SVRFESSTSE SSVLSSSSPE STLVKPEPNG MTIPDISSDM
     PDGAHKTPAS EAKSEIGQPT KVGRFQVTTT ANQVGRFSVS RTEDKVTEAK KEGPMASPFM
     DLEQTVLPAA IPKKEKPELS DPSHLNGPSS DLEAAFLSRD VDDGSGSPHS PPQLSSRSLP
     IQNLSQSLSN SLNSSYMSSD NESDIEDEDL KLELRRLREK HLKEIQDLQS RQKHEIESLY
     TKLGKVPPAV IIPPAAPLSG RRRRPTKSKG SKSSRISSLG SKSPQLSGNL SGQSAASGLH
     PQQTLQPPGN IPETGQNQLL QPLKPSPSSD NLYSAFTSDG AISVPSLSAP GQGTSSTNTV
     GGTVNSQAAQ TQPPAMTSSR KGTFTDDLHK LVDNWARDAM NLSGRRGSKG HMNYEGPGMA
     RKFSAPGQLC ISMTSNLAGP APISAASATS LGHFTKSMCP PQQYSFPAPP FGTQWSGTGG
     PAPQPLGQFQ PVGTASLQNF NISNLQKSIS NPPGSNLRTT
//
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