ID A5E7M7_LODEL Unreviewed; 541 AA.
AC A5E7M7;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Ribosome-associated complex subunit SSZ1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=LELG_05616 {ECO:0000313|EMBL:EDK47435.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK47435.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK47435.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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DR EMBL; CH981534; EDK47435.1; -; Genomic_DNA.
DR RefSeq; XP_001523070.1; XM_001523020.1.
DR AlphaFoldDB; A5E7M7; -.
DR STRING; 379508.A5E7M7; -.
DR GeneID; 5230159; -.
DR KEGG; lel:LELG_05616; -.
DR VEuPathDB; FungiDB:LELG_05616; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_0_3_1; -.
DR InParanoid; A5E7M7; -.
DR OMA; DQVLMDH; -.
DR OrthoDB; 23943at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10232; ScSsz1p_like_NBD; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR45639:SF32; HEAT SHOCK PROTEIN PDR13; 1.
DR PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001996}.
FT REGION 462..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..482
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 58661 MW; 16B8B784EA0989F7 CRC64;
MSVIGITFGN TSSSIAVATQ DGKVDVIANP DGDRSIPSAL SYVGTDEYHG SQAESRLIRN
PENTIVNFRD FVGKKFADIK HDFSYGAKPQ DANGEIAYKI VNDGKTEVLS LNTVVERHFK
QLKLAAEDYI GKPVKNVVLA VPTDFTEHQR EELSKIVGNA GLNVLQLINE PSAALLDHLS
SEEGKLAEDK IYAVADFGGV RSDGAIISVR GGVLTILATA HEYGLGGDNL DAALSEFFAK
EFEKKYKVDP RKTARSLAKL KAESITVRKT LSNVQTSTCS IESLAEGFDF HTSINRLRYE
LTAREPLSKM TAFVEKLIAK AELDPLDIDE VLLVGGCAHT PKLASSISYL FPASTKVIAP
SLVTKASNPS ELVARGAALQ AALIEGFDQE EINESLQPIV VNTQHLLKPI GIKDADGKFV
PILVAETAYP IKRSLEVTNG ENSTVSIQLY EGKRTVKETV VENAHDDEED SEDEDSEEEP
EIEREVVYEA GDLLAELSLS DLKPNAKVEV TVNITQNGVL HLTGRELKQG ATPVKGEISS
Q
//
