ID G0SWX5_RHOT2 Unreviewed; 979 AA.
AC G0SWX5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Proteophosphoglycan ppg4 {ECO:0000313|EMBL:EGU12550.1};
GN ORFNames=RTG_01083 {ECO:0000313|EMBL:EGU12550.1};
OS Rhodosporidium toruloides (strain ATCC 204091 / IIP 30 / MTCC 1151) (Yeast)
OS (Rhodotorula glutinis (strain ATCC 204091)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1001064 {ECO:0000313|EMBL:EGU12550.1, ECO:0000313|Proteomes:UP000006141};
RN [1] {ECO:0000313|EMBL:EGU12550.1, ECO:0000313|Proteomes:UP000006141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204091 / IIP 30 / MTCC 1151
RC {ECO:0000313|Proteomes:UP000006141};
RX PubMed=24526636; DOI=10.1128/genomeA.00046-14;
RA Paul D., Magbanua Z., Arick M.II., French T., Bridges S.M., Burgess S.C.,
RA Lawrence M.L.;
RT "Genome sequence of the oleaginous yeast Rhodotorula glutinis ATCC
RT 204091.";
RL Genome Announc. 2:E0004614-E0004614(2014).
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:EGU12550.1}.
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DR EMBL; AEVR02000003; EGU12550.1; -; Genomic_DNA.
DR AlphaFoldDB; G0SWX5; -.
DR HOGENOM; CLU_303868_0_0_1; -.
DR InParanoid; G0SWX5; -.
DR Proteomes; UP000006141; Unassembled WGS sequence.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006352; P:DNA-templated transcription initiation; IEA:InterPro.
DR CDD; cd07979; TAF9; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR005645; FSH-like_dom.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR003162; TFIID-31.
DR PANTHER; PTHR48070; ESTERASE OVCA2; 1.
DR PANTHER; PTHR48070:SF6; ESTERASE OVCA2; 1.
DR Pfam; PF03959; FSH1; 2.
DR Pfam; PF02291; TFIID-31kDa; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 2.
DR SUPFAM; SSF47113; Histone-fold; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006141}.
FT DOMAIN 285..497
FT /note="Serine hydrolase"
FT /evidence="ECO:0000259|Pfam:PF03959"
FT DOMAIN 710..920
FT /note="Serine hydrolase"
FT /evidence="ECO:0000259|Pfam:PF03959"
FT REGION 25..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 107038 MW; 253047EA44CD398F CRC64;
MVVGEGRGWQ ERLLLFPLEG STLSSTVSKN QGRTKLPAPT RQTPSFSFTM PPQPPQTSQP
VLPRDARLIA LILAAAGAED CEEGVVRMLV EFAHRYTSDV LTDSLLYAEH ARVGSTSTAP
VVPSVEDVRL AVQARTEGAQ VPKEFLLQLA TTVNSVPLPP VPEVYGIRLP PPAQRLTAPN
FSIVPRSAGP PAPPGAEGDL DALAAFDAGH VGAASSEEQK TTRTTTERRN TDRSSALRLH
GLAVPLVFWR RFLQVPAGAP TACAAILLSL PAVRLSRPRL ALLMPNRIRV LALPGHGQSA
SVLEGKLKRH REIWGDEFEV VTMDPPYPLV SGSVSHSTIT DAASTSSCWW DWSSHWRFKP
GEFEGAVRHF RRFYEENGPF DVCFGFSQGA AMAVLVLALL ERPDLHPVWL EGPHRPGVDW
PPRPFKCAVF ASAFGPGDPD YIAWYKKHRP ITPTLHIIGK NDVVADPQHS LDTVARFANA
KVVWHDGGHH IPRKPYFSQL IKDFIVSARD AHDWIDMPTR DGWGSPTESV ASSAGGDNPL
AGTLEGDTPF SPSLSPSRRR RSQRNRLAST DVLVPPAPGA AARYRVSTKT LNDCGDKRGD
DLPYAGAISS QEGRARQEEA GSGWSRPTSR QGSSPRSVEV LPLLSLSLSR FSAACSLSAA
SCIASSHLPT LVILSNPRLD ASFRPHDFRS ASLPFFPSTS TEPSMLATNQ KIRVLGLPGH
AQSAKLLEGK LAAHMHIWGD DIELVTMDPA YSLLMPTLDS SDSTELLNPA FSWWDWSSHY
KYKPGEFDGA LRHLRRFMEE NGPFDAVFSF SQGAAMAVLL LALLENPELH PAWTAGPSKE
GVEWPPAPLK CAVLCSAFGP LDPDFARWFF GRRPLVPTLH VIGKNDVVAD PQLSLDTVAR
FADARVVWHD GGHHIPRKPY YAHLIKEFIL SSCEMHDWRM DEEQSGWGTP TESVSSSVGE
GNEYFPAMPL VAEDVVAHF
//