SGT1_DICDI
ID SGT1_DICDI Reviewed; 387 AA.
AC Q55ED0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Protein SGT1 homolog {ECO:0000250|UniProtKB:Q08446};
DE AltName: Full=Suppressor of G2 allele of SKP1 homolog {ECO:0000250|UniProtKB:Q08446};
GN Name=sugt1 {ECO:0000312|dictyBase:DDB_G0269292}; ORFNames=DDB_G0269292;
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=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).
CC -!- FUNCTION: May play a role in ubiquitination and subsequent proteasomal
CC degradation of target proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SGT1 family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL71996.1; -; Genomic_DNA.
DR RefSeq; XP_645851.1; XM_640759.1.
DR AlphaFoldDB; Q55ED0; -.
DR SMR; Q55ED0; -.
DR STRING; 44689.DDB0267067; -.
DR PaxDb; Q55ED0; -.
DR EnsemblProtists; EAL71996; EAL71996; DDB_G0269292.
DR GeneID; 8616795; -.
DR KEGG; ddi:DDB_G0269292; -.
DR dictyBase; DDB_G0269292; sugt1.
DR eggNOG; KOG0548; Eukaryota.
DR eggNOG; KOG1309; Eukaryota.
DR HOGENOM; CLU_039532_1_0_1; -.
DR InParanoid; Q55ED0; -.
DR OMA; WDKLVGD; -.
DR PhylomeDB; Q55ED0; -.
DR Reactome; R-DDI-844456; The NLRP3 inflammasome.
DR PRO; PR:Q55ED0; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:dictyBase.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007699; SGS_dom.
DR InterPro; IPR044563; Sgt1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45862; PTHR45862; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF05002; SGS; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS51048; SGS; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..387
FT /note="Protein SGT1 homolog"
FT /id="PRO_0000330903"
FT REPEAT 1..34
FT /note="TPR 1"
FT REPEAT 36..67
FT /note="TPR 2"
FT REPEAT 68..101
FT /note="TPR 3"
FT DOMAIN 193..282
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT DOMAIN 301..387
FT /note="SGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00386"
FT REGION 110..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..144
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 43405 MW; FE7B2486631A88BC CRC64;
MEQLKEGNSY FVDEQYDEAL KCYDKACLEL SNNAEAFFKR SQCHSKLSNL KEALSDINTS
IKLDSNNSKY YLKKGQLCFE LEEFDTALKT FEKGQSIDSE NSSFKTWIRK SKAEIQSNPT
TTTTTTPTPT PTPTPAPQPV TTTTNPTPIP TTSNTTTTTN NNNNNNNNNN NNNNNNNTTT
DSTTTKLPIP SSGNKVRHEW YQTETHVVLT IFAKFVTASN SKINLTSKSV NISFPLANGS
EFLFEMDLFD PIVDKDSTIH YYSTKVEIKM KKSRAIKWDT LEFTDKSGPV GLMDQISSSP
AVPSPYASKK DWDKLPNEPE EKLEGDQALN KIFRDIFSKG SEDQQRAMMK SFTESGGTVL
STNWDEVGSK KVVGEPPKGL EFKQYEK