SMG1_DICDI
ID SMG1_DICDI Reviewed; 2344 AA.
AC Q553E9; Q86H67;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable serine/threonine-protein kinase smg1;
DE EC=2.7.11.1;
DE AltName: Full=Suppressor with morphological effect on genitalia protein 1;
GN Name=smg1; ORFNames=DDB_G0275845;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16596165; DOI=10.1371/journal.pgen.0020038;
RA Goldberg J.M., Manning G., Liu A., Fey P., Pilcher K.E., Xu Y., Smith J.L.;
RT "The dictyostelium kinome -- analysis of the protein kinases from a simple
RT model organism.";
RL PLoS Genet. 2:E38-E38(2006).
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 upf1 (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 -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000013; EAL69673.1; -; Genomic_DNA.
DR RefSeq; XP_643468.1; XM_638376.1.
DR AlphaFoldDB; Q553E9; -.
DR STRING; 44689.DDB0229297; -.
DR PaxDb; Q553E9; -.
DR EnsemblProtists; EAL69673; EAL69673; DDB_G0275845.
DR GeneID; 8620049; -.
DR KEGG; ddi:DDB_G0275845; -.
DR dictyBase; DDB_G0275845; smg1.
DR eggNOG; KOG0891; Eukaryota.
DR HOGENOM; CLU_229740_0_0_1; -.
DR InParanoid; Q553E9; -.
DR OMA; RVSEDWF; -.
DR Reactome; R-DDI-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-DDI-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DDI-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-DDI-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-DDI-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-DDI-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-DDI-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR Reactome; R-DDI-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DDI-9664873; Pexophagy.
DR PRO; PR:Q553E9; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP 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:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; 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; IPR018936; PI3/4_kinase_CS.
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; 2.
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; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Nonsense-mediated mRNA decay;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..2344
FT /note="Probable serine/threonine-protein kinase smg1"
FT /id="PRO_0000376003"
FT DOMAIN 1136..1552
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 1808..2192
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2312..2344
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1412..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1776..1796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1814..1820
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1933..1967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2059..2067
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2079..2103
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2157..2279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 264..293
FT /evidence="ECO:0000255"
FT COILED 378..405
FT /evidence="ECO:0000255"
FT COMPBIAS 230..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2157..2249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2252..2273
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2344 AA; 266637 MW; 41708EB6B1E124DF CRC64;
MNDSNSSNDS CNTENNTLTA TKNSINNTTT TTTTPNNNVN CLKTSGSIKL SASSVPFIPG
SSASLPSILS NQYKLAASNN VSNNIMMIST PIISSAQQQQ QQVPPPQQTT TTTTATATAI
TPTPITTSQS TSSSMLNLPL KVGKESIETL FRNRFHPKNN IRETVLSSLQ SILIPDLSDT
INNTKENIEY FYNMIIDENN YILKLLLLNI INDTKRNLVV YNYNQQHQLP IQNTSSPNTP
SSTTTTTTTS TKPSKRGDKE RERGRRNKDK INEKQLQQQQ LQQLQLQQQL DHEGSSLYLP
FSSLLSFIKP DKQQQPQQSQ QSQLNEIDQM VRPKSLPKDD NDSDNFNIRV LEYNLKLLIK
IYFKVSMYQD SIKTHIFDLY IQINQAISEQ QRQLQEKEKE SKTSKPIPQP IISLVIPTVL
VSIGDIIKYK YATPSPPNLT PTTTTKMEEE ERIINTILIN EFKKTDVSII ESNLYLFECI
LSISVSNEPT IVVPNTTTAT TATTATTSNT STAAAATTTT PTLSTSSSSL SPPASTQSSL
SLSSSSSAVI APTTVGYIFK FNKELFRKLI ALVYSTVVQH QITLSTVFTT LVLKGYLNED
QIQKLLNITL FKLSDPSEQV KLSYLTLLSK MVSYFDLNHQ KNLNHKVNDI SLPYKLLIMG
STSQPFFNGQ IFKKIFDWIM GIGKDQPSFD SLTKYLIDLF DSFNVISILF NEQNKILSQQ
YLAAQSTMIT PPLSLHQIDD RRKFETLISK SDELIWFWTV WECSKFCIAN RLKSPYGSAF
QTFEIFEKLL LQLNKDRRDF KKIKILLHFM ESMEKLIFST VNGSVLVQSL NNKETQFFRH
NVRVCEDWFS RIRVNLLKAS ILSSSTPDII RHASLRVQDI QANRFVLDSN TAHFELEFCI
LHLANALQQL NETESLQGLS NWSDINLNNS DNNNNNNNKN NNNNNNSTFF NNGNINKYTL
KLPWMKGVIL RSKQKFEESI SSLLSVPPML ESNSISFPFV LEQIIKSYLD ISNFTEVEQF
LQNYQNQIQQ QSNSLIIYKD TFIKTLGSFY RGEMEEAHAF AKRTESQNHI LQREQLGLGL
LGNQIMTDEL LLSIMVNQKD LFNNTNIINN NNSGGSSSGT ATATAVTTTT TTTTTTTTTT
TTTTNTNNDI IGFSNNINSM LKLTKNNILK ALNYLGLESN VQTFQYLTQL KIMDEIENGV
YNSRVVPINN QIGFLERLRR VRGHISNTKQ RSDILLSNIP LTEKMIKLSR KFENYKFSSK
LLDTILESHS SSYYLERCKL KYLNGKQTEA TLDLIKYAHR DITIPSSSTT TTTTTTTTTP
PSTSSNTATT TNNINIDELS TQKFKVYTEI IKYLNSNPSI ITELSSSNYS IPQEQLNPEY
YFKKATLTKP ENSKLWITYA DWILNEKSNI SEQNDEESLN GGGSGGNENS SNEMLRLKNT
NTNELKTAVE AYFQFLKYSM LDGNSNGGLN IRATLKILNI LVCSGNKLVE TFERCLNELT
STRPFTIIIP QLFARLSHPD TFVQKYVVEI LNRIGRDNPN KIVYQTIVGS LNFTNTNNNN
NSSCAAATTD DGLDIELLQK QYPNYLQILN IKENLLKHSE LLVKETETLI YQLGKLTTLW
DDNWQYFIEQ IQGWVYINTK QWNDDYQQLK ATIKNPTILK HTLKKKNQEL LQPIYEKLKR
LTAATVLSVC KTPHEKWFTK CHFETINKTI RAFEKQNKPT SPFDVLHDLI AEFQQYRLIS
LSLSSVNPSL ALFRPTITQM PGTDLNYFNI NHIHHHHHHH NHHGNNNNQH STSSGNLPIQ
NQVTIQLIKP TIYLLPTKTK PKKMAMLGSD GNLYYYLLKG REDLHLDERI MQLLNVVDQL
LMNDKKPTLK LLRTRNYSVI PLSQSSGLIQ WVEGAVPLFS IYKNWYKNDQ VYKQQQQQQQ
QLQQQQQQQQ QQQQQQPQPQ QQPQQQPQQQ PQQQPQPQQN STTTSNIVNK PIIARPVDIF
YAKITPLLEK AGLNFMTPRS EWPKEILIQV LNELMQETPK WILQRELWFS SSSSSELFLK
TQSYSRSLAL MSVIGYMIGL GDRHLDNILL DLKTGEIVHI DYNICFEKGA ELKIPERVPF
RMTQIFEYAL GLTGVQGTFR ETSIQIMHLL RKNKDILLNL LETFIYDPLF DWKHSNKQTN
NNNNNNNNNN MNQAAGEQES IEKKQSSNNS SNPIISTPTK LQQQQKLPNS PLSISSNNTN
STNNNNNNNN NNNNNNNNNN NNNNKDQDSD SSQSQEDEDN NVVEGEGGEG GEGDIDELNL
VQDSSNGKDA FKSIQGLTVV NQVRLKLEGT EKKLSIPDQI DLIIRESMNV ENLSSTYEGW
SPWV
