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Database: UniProt
Entry: A0A0D9R6F7_CHLSB
LinkDB: A0A0D9R6F7_CHLSB
Original site: A0A0D9R6F7_CHLSB 
ID   A0A0D9R6F7_CHLSB        Unreviewed;      3274 AA.
AC   A0A0D9R6F7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=SMG1 {ECO:0000313|Ensembl:ENSCSAP00000004196.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000004196.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000004196.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000004196.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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; AQIB01118390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01118391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01118392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01118393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01118394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 60711.ENSCSAP00000004196; -.
DR   Ensembl; ENSCSAT00000005986.1; ENSCSAP00000004196.1; ENSCSAG00000007938.1.
DR   eggNOG; KOG0891; Eukaryota.
DR   GeneTree; ENSGT00940000154776; -.
DR   OMA; AFECHFT; -.
DR   Proteomes; UP000029965; Chromosome 5.
DR   Bgee; ENSCSAG00000007938; Expressed in blood and 7 other cell types or tissues.
DR   GO; GO:0033391; C:chromatoid body; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042162; F:telomeric DNA binding; IEA:Ensembl.
DR   GO; GO:0006974; P:DNA damage response; IEA:Ensembl.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:Ensembl.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0032204; P:regulation of telomere maintenance; IEA:Ensembl.
DR   CDD; cd05170; PIKKc_SMG1; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR014009; PIK_FAT.
DR   InterPro; IPR031559; SMG1.
DR   InterPro; IPR035175; SMG1_N.
DR   InterPro; IPR039414; SMG1_PIKKc.
DR   PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR   PANTHER; PTHR11139:SF71; SERINE_THREONINE-PROTEIN KINASE SMG1; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF15785; SMG1; 1.
DR   Pfam; PF17229; SMG1_N; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SMART; SM01345; Rapamycin_bind; 1.
DR   SUPFAM; SSF48371; ARM repeat; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1257..1840
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          2098..2437
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1128..1149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1872..1894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1948..1975
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        12..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3274 AA;  367656 MW;  6544CF4306468E2C CRC64;
     MRFLRTDSAS ADPDNLKYSS SRDRGSSSSY GLQPSNSAVV SRQRHDDTRV HADIQNDEKG
     GYSVNGGSGE NTYGRKSLGQ ELRVNNVTSP EFTSVQHGSR ALATKDMRKS QERSMSYSDE
     SRLSNLLRRI TREDDRDRRL ATVKQLKEFI QQPENKLVLV KQLDNILAAV HDVLNESSKL
     LQELRQEGAC CLGLLCASLS YEAEKIFKWI FSKFSSSAKD EVKLLYLCAT YKALETVGEK
     KAFSSVMQLV MTSLQSILEN VDTPELLCKC VKCILLVARC YPHIFSTNFR DTVDILVGWH
     IDHTQKPSLT QQVSGWLQSL EPFWVADLAF STTLLGQFLE DMEAYAEDLS HVASGESVDE
     DVPPPSVSLP KLAALLRVFS TVVRSIGERF SPIRGPPITE AYVTDVLYRV MRCVTAANQV
     FFSEAVLTAA NECVGVLLGS LDPSMTIHCD MVITYGLDQL ENCQTCGTDY IISVLNLLTL
     IVEQINTKLP SSFVEKLFIP SSKLLFLRYH KEKEVVAVAH AVYQAVLSLK NIPVLETAYK
     LILGEMTCAL NNLLHSLQLP EACSEIKHEA FKNHVFNVDN AKFVVIFDLS ALTTIGNAKN
     SLIGMWALSP TVFALLSKNL MIVHSDLAVH FPAIQYAVLY TLYSHCTRHD HFISSSLSSS
     SPSLFDGAVI STVTTATKKH FSIILNLLGI LLKKDNLNQD TRKLLMTWAL EVAVLMKKSE
     TYAPLFSLPS FHKFCKGLLA NTLVEDVNIC LQACSSLHAL SSSLPDDLLQ RCVDVCRVQL
     VHSGTRIRQA FGKLLKSIPL DVVLSNNNHT EIQEISLALR SHMSKAPSNT FHPQDFSDVI
     SFILYGNSHR TGKDNWLERL FYSCQRLDKR DQSTIPRNLL KTDAVLWQWA IWEAAQFTVL
     SKLRTPLGRA QDTFQTIEGI IRSLAAHTLN PDQDVSQWTT ADNDEGHGNN QLRLVLLLQY
     LENLEKLMYN AYEGCANALT SPPKVIRTFF YTNRQTCQDW LTRIRLSIMR VGLLAGQPAV
     TVRHGFDLLT EMKTTNLSQG NELEVTIMMV VEALCELHCP EAIQGIAVWS SSIVGKNLLW
     INSVAQQAEG RFEKASVEYQ EHLCAMTGVD CCISSFDKSV LTLANAGRNS ASPKHSLNGE
     SRKTVLSKPT DSSPEVINYL GNKACECYIS IADWAAVQEW QNAIHDLKKS TSSTSLNLKA
     DFNYIKSLSS FESGKFVECT EQLELLPGEN INLLAGGSKE KIDMKKLLPN MLSPDPRELQ
     KSIEVQLLRS SVCLATALNP VEQDQKWQSI TENVVKYLKQ TSRISIGPLR LSTLTVSQSL
     PVLSTLQLYC SSALENTVSS RLSTEDCLIP LFSEALRSCK QHDVRPWMQA LRYTMYQNRL
     LEKIKEQTVP IRSHLMELGL TAAKFARKRG NVSLATRLLA QCSEVQLGKT TTAQDLVQHF
     KKLSTQGQVD EKWGPELDIE KTKLLYTAGQ STHAMEMLSS CAISFCKSAK AEYAVAKSIL
     TLAKWIQAEW KEISGQLKQV YRAQHQQNFT GLSTLSKNIL TLIELPSVNT MEEEYPRIES
     ESTVHIGVGE PDFILGQLYH LSSVQAPEVA KSWAALASWA YRWGRKVVDN ASQGEGVRLL
     PREKSEVQNL LPDTITEEEK ERIYGILGQA VCRPAGIQDE DITLQITESE DNEEDDMVDV
     IWRQLISSCP WLSELDESAT EGVIKVWRKV VDRIFSLYKL SCSAYFTFLK LNAGQIPLDE
     DDPRLHLSHR AEQSTDDVIV MATLRLLRLL VKHAGELRQY LEHGLETTPT APWRGIIPQL
     FSRLNHPEVY VRQSICNLLC RVAQDSPHLI LYPAIVGTIS LSSESQASGN KFSTAIPTLL
     GNIQGEELLV SECEGGSPPA SQDSNKDEPK SGFNEDQAMM QDCYSKIVDK LSSANPTMVL
     QVQMLVAELR RVTVLWDELW LGVLLQQHMY VLRRIQQLED EVKRVQNNNT LRKEEKIAIM
     REKHTALMKP IVFALEHVRS ITAAPAETPH EKWFQDNYGD AIENALEKLK TPSNPAKPGS
     SWIPFKEIML SLQQRAQKRA SYILRLEEIS PWLAAMTNTE IALPGEVSAR DTVTIHSVGG
     TITILPTKTK PKKLLFLGSD GKSYPYLFKG LEDLHLDERI MQFLSIVNTM FATINRQETP
     RFHARHYSVT PLGTRSGLIQ WVDGATPLFG LYKRWQQREA ALQAQKAQDS YQTPQNPGIV
     PRPSELYYSK IGPALKTVGL SLDVSRRDWP LHVMKAVLEE LMEATPPNLL AKELWSSCTT
     PDEWWRVTQS YARSTAVMSM VGYIIGLGDR HLDNVLIDMT TGEVVHIDYN VCFEKGKSLR
     VPEKVPFRMT QNIETALGVT GVEGVFRLSC EQVLHIMRRG RETLLTLLEA FVYDPLVDWT
     AGGEAGFAGA VYGGGGQQAE SKQSKREMER EITRSLFSSR VAEIKVNWFK NRDEMLIVLP
     KLDSSLDEYL SLQEQLTDVE KLQGKLLEEI EFLEGAEGVD HPSHTLQHRY SEHTQLQTQQ
     RAVQEAIQVK LNEFEQWITH YQAAFNNLEA TQLASLLQEI STQMDLGPPS YVPATAFLQN
     AGQAHLISQC EQLEGEVGAL LQQRRSVLRG CLEQLHHYAT VALQYPKAIF QKHRIEQWKT
     WMEELICNTT VERCQELYRK YEMQYAPQPP PTVCQFITAT EMTLQRYAAD INSRLIRQVE
     RLKQEAVTVP VCEDQLKEIE RCIKVFLHEN GEEGSLSLAS VIISALCTLT RRNLMMEGAA
     SSAGEQLVDL TSRDGAWFLE ELCSMSGNVT CLVQLLKQCH LVPQDLDIPN PMEASETVHL
     ANGVYTSLQE LNSNFRQIIF PEALRCLMKG EYTLESMLHE LDGLIEQTTD GVPLQTLVES
     LQAYLRNAAM GLEEETHAHY IDVARLLHAQ YGELIQPRNG SVEETPKMSA GQMLLVAFDG
     MFAQVETAFG LLVEKLNKME IPIAWRKIDI IREARSTQVN FFDDDNHRQV LEEIFFLKRL
     QTIKEFFRLC GTFSKTLSGS SSLEDQNTVN GPVQIVNVKT LFRNSCFSED QMAKPIKAFT
     ADFVRQLLIG LPNQALGLTL CSFISALGVD IIAQVEAKDF GAESKVSVDD LCKKAVEHNI
     QIGKFSQLVM NRATVLASSY DTAWKKHDLV RRLETSISSC KTSLQRVQLH IAMFQWQHED
     LLINRPQAMS VTPPPRSAIL TSMKKKLHTL SQIETSIATV QEKLAALEAS IEQRLKWAGG
     ANPALAPVLQ DFEATIAERR NLVLKESQRA SQVL
//
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