ID D2V4E1_NAEGR Unreviewed; 648 AA.
AC D2V4E1;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Polyubiquitin {ECO:0000313|EMBL:EFC48371.1};
GN ORFNames=NAEGRDRAFT_78526 {ECO:0000313|EMBL:EFC48371.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC48371.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC48371.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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DR EMBL; GG738851; EFC48371.1; -; Genomic_DNA.
DR RefSeq; XP_002681115.1; XM_002681069.1.
DR AlphaFoldDB; D2V4E1; -.
DR STRING; 5762.D2V4E1; -.
DR EnsemblProtists; EFC48371; EFC48371; NAEGRDRAFT_78526.
DR GeneID; 8862128; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_78526; -.
DR eggNOG; KOG0001; Eukaryota.
DR InParanoid; D2V4E1; -.
DR OrthoDB; 5483783at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR10666; UBIQUITIN; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 56..133
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 337..368
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 204..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 71321 MW; 4E08BF6595E6435C CRC64;
MMNNCSPSED SILCVERMNH SCYNNHHHHH HHLQHLTSTL VSPSSCPKYT HPSPNTQVFI
KTLSGKTMTL LVDLKKDTIL SVKEKIYQKT CIPALKQRLI HRQLQLEDHK KLSDYPTIDK
DSTFHLVLRL VAGVNTKSGK SRSKKTIPIK TEDGADAISN QITSDNSSTS LTPTTAVVVA
DLTIPKPDDG TIDASIINTS STNELVTTSS SSNNNNSTTT PATTRKSRSK SNASTKKSSK
KSTSSSSTTE IKVKEEPMEK DNNTIVLASS DLNSIHSSPS ENSTSPSSST IPSSNSNALE
AYSDESETDE DDSDSEGGGK GKRSGKNKKR GSYTKRACIN CRTAHAACDS GRPCKRCIQL
GKADSCRDAE RKRTKKRTLN EYENAPVFFP SLDSFIPLLS GLQPAPPLET VQKSDDTSNM
STNSETSEKK IKDEFTPKST ARIKKEKESK RKSKNQSSST EQKVERMDIM EISQPEKPLN
SELAAIFAPD TAHSTFLDME SSPTTEQDVQ MFFNDEDISL DKRGGDNLSE AFNTGVVLSP
ESNNSQIEEV LPSTALALVP NNPDNQQLIS ILQSYNGTLP FDLTEAISQS NNNEIVKMLL
YEYLRQSQEL RELKQLVASL QFTLINLNPP QFSPNSSTPL NDISNNTM
//
