ID SMG1_CAEBR Reviewed; 2313 AA.
AC Q61CW2; A8XGG5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Serine/threonine-protein kinase smg-1;
DE EC=2.7.11.1;
DE AltName: Full=Suppressor with morphogenetic effect on genitalia protein 1;
GN Name=smg-1; ORFNames=CBG12735;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Serine/threonine protein kinase involved in mRNA
CC surveillance. Recognizes the substrate consensus sequence [ST]-Q.
CC Involved in nonsense-mediated decay (NMD) of mRNAs containing premature
CC stop codons by phosphorylating smg-2 (By similarity). {ECO:0000250}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of a post-splicing multiprotein NMD complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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DR EMBL; HE600940; CAP31671.3; -; Genomic_DNA.
DR AlphaFoldDB; Q61CW2; -.
DR SMR; Q61CW2; -.
DR STRING; 6238.Q61CW2; -.
DR WormBase; CBG12735; CBP37588; WBGene00033641; Cbr-smg-1.
DR eggNOG; KOG0891; Eukaryota.
DR HOGENOM; CLU_001279_1_0_1; -.
DR InParanoid; Q61CW2; -.
DR OMA; PMQTFAA; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031931; C:TORC1 complex; IBA:GO_Central.
DR GO; GO:0031932; C:TORC2 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IBA:GO_Central.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR CDD; cd05170; PIKKc_SMG1; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
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; IPR014009; PIK_FAT.
DR InterPro; IPR031559; SMG1.
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; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF15785; SMG1; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Manganese; Metal-binding;
KW Nonsense-mediated mRNA decay; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2313
FT /note="Serine/threonine-protein kinase smg-1"
FT /id="PRO_0000229793"
FT DOMAIN 1045..1528
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT REPEAT 1478..1514
FT /note="HEAT"
FT DOMAIN 1746..2091
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2281..2313
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 779..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1752..1758
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1954..1962
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1974..1998
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ SEQUENCE 2313 AA; 264720 MW; 03CD52460EA0CBE3 CRC64;
MLTSKNNDIG NLIEIFRQRD ITYKERKATL QKIEELIPKV PDLEALNTKW IYLLDNAVWP
LIVKSDRMDL KSLAGKVTRH VGALLFDSPF YPEFLLWLGT LLQNTPKKND DARADIVFSV
YYIVGAISQK SENRLGKNDE EYVRKSLEWL IRVIPNSSSA VYNNCLKGII LISNTFRKVT
DDLYESCLRA IVSNFPDFNS HEKNFERLLD TVNLFSDHFS KDPVLAEEMV RIIRPDIKKN
GLRNTRELKK RLKLTMAIVK MAKSQQILVE TNEMMCELQA ELEGNGGKWS SAALITIICD
LLNELLILGK NDAEMRQSVE ESLGNLLKDL NLSKQNTKEK QAFFNSLAKI VKQLPAESDV
KTRIHHIVFN SDTGLFNIQN DDNRIFGHNT IYRDLVNLIS VLLTPTSLSH LQATYTDLRK
IMMESMSKLK QSERWHESIL LLFFSALQGI SCAKSSLIVM IGIRPSIFEL FCDELPLTEY
WLASNHPEVY HIFITILVGH LKAHDFYVSQ SDYLVHGETP TGHAYGQTKR EYVRKQVIAL
HKIIGGFGNR LWKKTRFLIS TWLHSLVVIA RDQKISAESF RLKEWVRLRN TVIQHSVLDW
NNESINQALT VLSTVTNWSA LPLELNKDIT DKTKKATWKE ATTIWESGDF KTYIRQSLST
TYQMSQERQQ KQIGSTSFGA EEFNLVTNFL LKQIVPTTFK KGPYVWMDEV LETAIQGCKN
ISQEKSDVPE TFMEKWDWII NQTANFCIVN KMKTPLGKPM QTFAAFENEI KRLAKEVINR
KSSDKKPKST TEDVPPPATP PLKFSIQWLR VHLLLKLIEV LEKIMISSIR GGSSIFNLTE
IPVTARQFFI MNSSSCEVWL NRVYYPALIV AYFNGYYGLV IRFGSNALNH YARQKGSDEK
MITNGVCTAC LMSLSMAVLG EPMEIVGLRR RVREEFGTEM GQKLMEALGE MASARYEIAL
VQLEAILVVD SSINETLRII IQIAITDMLN RIRLPDAVRY YKKTLFGEDE EAQVAEDFRS
IEMLTKFEKL NYGVAEKRQV VDWSARERLQ LVESAYSQTM KRNELLELQK EMSAMGALAL
SADSSCKLYS DISSTSLVIA NLVDRMTGTS HWKNQLTDVE MFDRAEEGNE GDKLTICRKL
MHWGRHMKHH RGQSFAAHGE IIRFSRKTSN CELAFFHINS AIRGEKLEAW QRLEVERQRL
KLVKSQHFDV RVREMNEVFG SLADVFSTSI EMKQKFQNLD DQTKDLMVAN GYLSDIAKRE
EHMSRASIQL ADFFDTLPTI DTVLTPNLYN TIIWSEIQSR SNSLSCGYAG LVGALYNLSA
DLCPSLAKAH LKMAKWTYEM AKIENFPNIS PFALYQFGQT AQENEELWRS LDATSLVNLE
KQVRKIVPDA MRASVLLSPN NPYLLLWEAA SAHRRKFLCI TVSSYFQFIH NMSGDFECLP
YSKREETTLA TLRILEMLVK HGEVLVDVIN DGLSRTNVHV WKEILPQLFA RLSHPSDHIR
KTLVDLISRV CTAAPHAVVF QVVSGAASST EVSDLEEQQN DDRNRVRACC EQLETKMAQS
YPNLVRDVRQ FVAELERINL LNEEKWSVVL GTMEHEMEKR LALIKAENAK TDFSMHLMPK
QKDEIISKKT KLLTRQIFDV LDELYEKTIV AQPETENEKE FFNTFSEMLT KAHTESKNNR
YNSPEASWAP FKNLVSNFAH RTNKKGMQTF QTADISQYLA TLGKSCVPMP GQESVEFDRV
VSIARVADNV TILPTKTRPK KLGFIGSDGK QLAFLFKGRE DLHLDERVMQ FLRLCNVMLQ
SEKGKSRQIA EYQAHHYAVI PLGPRSGLIK WVEGATPIFH IYRKWQMKEK ALKQATKKNG
ETVPEIEKPT NMYHNMIRQA FTAHNIDAII ASDRSKWPAQ ILEEVFDGLC SKTPTDLISR
EIWMRANDST AWWAVTKRYA RSLAVMSMVG SVLGLGDRHL DNLLVDLKYG HVVHIDYNIC
FDKGKILRIP ETVPFRLSRN MRHALGPSDM YGTFRESCVH VLSTLRSGHQ VLTMLLDAFV
FDPLVDWTSH DNISTSGGVS LALQLAVYGS SWKAKARERL TDTIELFQLR VTELQALWMS
NREDLYHWMK QVTDCLLAEQ SIMGMNGAYA QQRVKAGTEL REAVARHQAL AKEFRPLIRV
IGKEKEEFAD YLKFYKQAFI DPLLKGHSAL RHELDIDTCV QNFNIVMQNI DVVFMSLISL
STMPIDSVSS RASQKQFNAP PGLENVWVLQ QEQQENSQAR EVVRRVERRL NGWLDGSAPD
RKLSPREEAD VLIAEATSSA NLAQMYEGWT AWV
//
