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Database: UniProt
Entry: M9LZ39_PSEA3
LinkDB: M9LZ39_PSEA3
Original site: M9LZ39_PSEA3 
ID   M9LZ39_PSEA3            Unreviewed;       513 AA.
AC   M9LZ39;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=FOG: Low-complexity {ECO:0000313|EMBL:GAC76184.1};
GN   ORFNames=PANT_19d00157 {ECO:0000313|EMBL:GAC76184.1};
OS   Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC76184.1, ECO:0000313|Proteomes:UP000011976};
RN   [1] {ECO:0000313|Proteomes:UP000011976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX   PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA   Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA   Machida M., Kitamoto D.;
RT   "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT   producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL   Genome Announc. 1:E0006413-E0006413(2013).
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DR   EMBL; DF196785; GAC76184.1; -; Genomic_DNA.
DR   AlphaFoldDB; M9LZ39; -.
DR   STRING; 1151754.M9LZ39; -.
DR   OrthoDB; 69173at2759; -.
DR   Proteomes; UP000011976; Unassembled WGS sequence.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd13945; Chs5_N; 1.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 6.20.120.50; -; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR031673; Chs5_N.
DR   InterPro; IPR031669; Fn3_2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR47351; CHITIN BIOSYNTHESIS PROTEIN CHS5; 1.
DR   PANTHER; PTHR47351:SF1; CHITIN BIOSYNTHESIS PROTEIN CHS5; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF16892; CHS5_N; 1.
DR   Pfam; PF16893; fn3_2; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000011976}.
FT   DOMAIN          99..192
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          187..288
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          307..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..415
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..447
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..479
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   513 AA;  54444 MW;  E5CC3E1B419B7524 CRC64;
     MSAHYVGQIA PNYVHSTMQA NSDDDSFTFT VGKLDAGMAI LIGEKASLIE FPSLLLPHGV
     SSGSVVNIRV MRNEQQERRQ KDDFDLLQED ILHTFGQQAP KVPALRLRNV TQTSVTLEWE
     RLSLATATLL SLDIYRNGQR LAPIPNPLHN TSTKLSGLDV NADYTFHLVM KTTAGTFSSP
     LIKTRTHTIN DTSGISVCFG HVHDAEMLEA AKKALASMKA KWSDRIQIDT THYICTDPRN
     PGDVHAQPSA HGNGYTKAML LSIPAVLPHW IFACHDQKKM VGISPFYLDQ DPPNAATIRQ
     SIDQVLGKHS ASAAEPTAAT SAAAAPAQSS NASDAGPPPP PLEKDAKPAS SSATESAPAT
     EPAPATEIEH ETQQEAAAAG SQAEASGSAL GLKLNEDEPA PSPPQPQPQP PTPIITTSAP
     SDDGEDDEAP HASESPAPPP PPQVIVTPTE PEEAAADAQP KAEPASHEDE SGGLNADAHA
     DDDDDGDMDD VSLGGNTNAD DENEVDEADT RRF
//
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