ID A0A150UXI6_9PEZI Unreviewed; 405 AA.
AC A0A150UXI6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 13-SEP-2023, entry version 24.
DE RecName: Full=SGS-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M433DRAFT_379305 {ECO:0000313|EMBL:KYG42957.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG42957.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG42957.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG42957.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
CC -!- SIMILARITY: Belongs to the SGT1 family.
CC {ECO:0000256|ARBA:ARBA00008509}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYG42957.1}.
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DR EMBL; JPDO01000377; KYG42957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150UXI6; -.
DR STRING; 766039.A0A150UXI6; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR CDD; cd06466; p23_CS_SGT1_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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; PROTEIN SGT1 HOMOLOG; 1.
DR PANTHER; PTHR45862:SF1; PROTEIN SGT1 HOMOLOG; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF05002; SGS; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS51048; SGS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT DOMAIN 177..267
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 301..405
FT /note="SGS"
FT /evidence="ECO:0000259|PROSITE:PS51048"
FT REGION 146..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 405 AA; 44622 MW; 1B517CEF898628E4 CRC64;
MATQAELGKK ALAASNYDEA IKQYTAALQQ FPTSPDYLIQ RSTAYHRANK YPEAVADAEQ
AVLAAHKRAK REAITEAQFR RACALYNLGR YGDAQFVFGI VKRLKPDHKM IDTWVKKSAD
ALNKLADDDE KRKVTVKEVP EVEFGASDSN TLKGDGKSET SAALHSAPTI PPQQTPADKI
RHDWYQNDKN VYYTLLAKGV PEDQAQIQIT ERSMSITFPL LSGSSYDMTL DPLFAAVNPA
ESKFKILPNK IEIVLVKAVP GRWKALEGSD AVINESTSAR VTQEHHEKAE AKESSKPTGP
VYPTSSKSGP KDWDKIAKDL RKADKGSAKS GLVEDDDDDD DEGGGAEHSF FKKLFKNASP
DAQRAMMKSY TESNGTALST DWSEVSKGKV ETCPPNGMEE KKWAT
//
