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SMG1_CAEBR
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   03-AUG-2022, entry version 99.
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.CBG12735; -.
DR   PRIDE; 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; 26975at2759; -.
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: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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR   CDD; cd05170; PIKKc_SMG1; 1.
DR   Gene3D; 1.10.1070.11; -; 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   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; SSF48371; 1.
DR   SUPFAM; SSF56112; SSF56112; 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
 
 
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