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Ebp1p [Candida albicans SC5314].


LOCUS       XP_714331                407 aa            linear   PLN 18-APR-2022
ACCESSION   XP_714331
VERSION     XP_714331.2
DBLINK      BioProject: PRJNA14005
            BioSample: SAMN02953594
DBSOURCE    REFSEQ: accession XM_709238.2
KEYWORDS    RefSeq.
SOURCE      Candida albicans SC5314
  ORGANISM  Candida albicans SC5314
            Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
            Pichiomycetes; Debaryomycetaceae; Candida/Lodderomyces clade;
            Candida.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Muzzey,D., Schwartz,K., Weissman,J.S. and Sherlock,G.
  TITLE     Assembly of a phased diploid Candida albicans genome facilitates
            allele-specific measurements and provides a simple model for repeat
            and indel structure
  JOURNAL   Genome Biol. 14 (9), R97 (2013)
   PUBMED   24025428
REFERENCE   2  (residues 1 to 407)
  AUTHORS   van het Hoog,M., Rast,T.J., Martchenko,M., Grindle,S., Dignard,D.,
            Hogues,H., Cuomo,C., Berriman,M., Scherer,S., Magee,B.B.,
            Whiteway,M., Chibana,H., Nantel,A. and Magee,P.T.
  TITLE     Assembly of the Candida albicans genome into sixteen supercontigs
            aligned on the eight chromosomes
  JOURNAL   Genome Biol. 8 (4), R52 (2007)
   PUBMED   17419877
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Jones,T., Federspiel,N.A., Chibana,H., Dungan,J., Kalman,S.,
            Magee,B.B., Newport,G., Thorstenson,Y.R., Agabian,N., Magee,P.T.,
            Davis,R.W. and Scherer,S.
  TITLE     The diploid genome sequence of Candida albicans
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 101 (19), 7329-7334 (2004)
   PUBMED   15123810
REFERENCE   4  (residues 1 to 407)
  CONSRTM   NCBI Genome Project
  TITLE     Direct Submission
  JOURNAL   Submitted (15-APR-2022) National Center for Biotechnology
            Information, NIH, Bethesda, MD 20894, USA
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Muzzey,D., Schwartz,K., Weissman,J.S. and Sherlock,G.
  TITLE     Direct Submission
  JOURNAL   Submitted (04-OCT-2016) Department of Genetics, Candida Genome
            Database, Stanford University, Mail Stop-5120, Stanford, CA 94305,
            USA
REFERENCE   6  (residues 1 to 407)
  CONSRTM   Candida Genome Database
  TITLE     Direct Submission
  JOURNAL   Submitted (30-SEP-2016) Department of Genetics, Candida Genome
            Database, Stanford University, Mail Stop-5120, Stanford, CA 94305,
            USA
  REMARK    Sequence and annotation update by submitter
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence is identical to AOW30064.
            
            On Dec 8, 2016 this sequence version replaced XP_714331.1.
            
            ##Genome-Annotation-Data-START##
            Annotation Provider :: CGD
            Annotation Status   :: Full annotation
            Annotation Version  :: A22-s07-m01-r01
            URL                 :: http://www.candidagenome.org/
            ##Genome-Annotation-Data-END##
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Candida albicans SC5314"
                     /strain="SC5314"
                     /host="Homo sapiens"
                     /culture_collection="ATCC:MYA-2876"
                     /db_xref="taxon:237561"
                     /chromosome="6"
                     /haplotype="A"
                     /geo_loc_name="USA: New York"
                     /collected_by="Margarita Silva-Hutner"
     Protein         1..407
                     /product="Ebp1p"
                     /calculated_mol_wt=45958
     Region          27..380
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(47,49,82,124,254,330,354,356..358)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(47,49,82,124,126,133,201,204,206,254,261,330,354,
                     356..357)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(49,126,201,204,206,357)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            206
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
     CDS             1..407
                     /gene="EBP1"
                     /locus_tag="CAALFM_C601180CA"
                     /coded_by="XM_709238.2:1..1224"
                     /note="NADPH oxidoreductase; interacts with phenolic
                     substrates (17beta-estradiol); possible role in estrogen
                     response; induced by oxidative, weak acid stress, NO,
                     benomyl, GlcNAc; Cap1, Mnl1 induced; Hap43-repressed; rat
                     catheter biofilm induced"
                     /transl_table=12
                     /db_xref="CGD:CAL0000199513"
                     /db_xref="GeneID:3644060"
ORIGIN      
        1 mtiestnsfv vpsdtelidv tplgstklfq pikvgnnvlp qriayvpttr fraskdhips
       61 dlqlnyynar sqypgtliit eatfasergg idlhvpgiyn daqakswkki neaihgngsf
      121 ssvqlwylgr vanakdlkds glpliapsav ywdensekla keagnelral teeeidhive
      181 veypnaakha leagfdyvei hgahgylldq flnlasnkrt dkygcgsien rarlllrvvd
      241 klievvganr lalrlspwas fqgmeiegee ihsyilqqlq qradngqqla yislveprvt
      301 giydvslkdq qgrsnefayk iwkgnfirag nytydapefk tlindlkndr tiigfsrfft
      361 snpdlveklk lgkplnyynr eefykyynyg ynsydesekq vigkpla