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Database: UniProt
Entry: A0A024G6A9_9STRA
LinkDB: A0A024G6A9_9STRA
Original site: A0A024G6A9_9STRA 
ID   A0A024G6A9_9STRA        Unreviewed;      1029 AA.
AC   A0A024G6A9;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   08-NOV-2023, entry version 44.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCI42292.1};
GN   ORFNames=BN9_030760 {ECO:0000313|EMBL:CCI42292.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI42292.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI42292.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI42292.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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:CCI42292.1}.
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DR   EMBL; CAIX01000032; CCI42292.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024G6A9; -.
DR   STRING; 65357.A0A024G6A9; -.
DR   InParanoid; A0A024G6A9; -.
DR   OrthoDB; 5474185at2759; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 6.10.140.2220; -; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 1.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR002893; Znf_MYND.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF24; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053237};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00134}.
FT   DOMAIN          46..193
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          299..337
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   DOMAIN          384..1027
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1029 AA;  117755 MW;  A0B991EDBCB56900 CRC64;
     MAKNKKKPSN AQKRAAARRR HNEEHNSRKR NVNAIETNLM AHTLVPLKSQ EREIIFQLLQ
     QAENQSLHVG EKRYLIAFGW WQKWCQMVDF RPNHLIFSSC SMESYGESES NSYEYCKGDN
     EIGEMDNDTL PSIDNGVLLE GMDNTKRDLD DLVGAPLRPN LEENRDFVLV PQEVWDAICC
     WYGGGPTVAR FVVSKCVHER DQSMTINRVQ IYPELEARED DLEEIVGKTK VINNQLAASV
     DESLKIHKYD HSPQHGDAQF PLEEEDHDGD MDTQNVVERQ SLPLRSNTLS DESMRVKSCI
     VCRSVNEAVK RCGRCRRVYY CTVDCQRSHW KYHRIVCSKL EKASVMIHHA DTQEHLIEQE
     LKKLPKEVQV LWRNPIALER RGKVGLRNLG NTCFLNSALQ CLSHMRLLTD YFLSTRFQQD
     LNRGNPLGTG GELALVYNEL IRELWFGSTS QLSPIALKRA IARFAPQFSG YQQQDAQELL
     AYMLDGLHED LNRIKQKPYT EVQESDGKLE DAFVADEAWR RHLLRNDSIF VDHIQGQFKS
     TVVCPVCSKV SITFDPYNCI QLELPTKSTR VLDIIVVSND AVQENELSGC HFTRYAIQVS
     KKQCVQTFYH ALSEVCGIAS NKLVLADVYQ STIFRLIRDT DRISSIGDED RIVAYEMSCI
     PPISLNHKPP GSASPIDIEI DHEGGNIPKN PEMDMASSQY LGFLYHETFS RLAGIPLMFN
     FDENTTCLDA LHHWSRKIST HIVQVRVQLL RYAVFGVQIS PAILASHLFV ASSEGYIFRE
     KSIPATESVL LLEYVHSVDH KHVPVASPHT TNPRGPFFFG LVWSSELLEP NPSTWFRPEI
     DEIKDHKSIQ AFHGTKSSSS SNESITLDAC FKNFIKPETL DDANLWYCAN CKAHRQAHKR
     IEIWKVPDIL ILSLKRFEYR NETLRDKLSV DVDFPLENLD MRPFCLQASA SDTLPHAKKS
     LQYDLFAVSN HYGGMAYGHY TACAKNFCQG EGDDTARWYY FDDGVVDVMP SERVKSNTAY
     ILFYQRKQV
//
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