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uncharacterized protein CAALFM_C603430CA [Candida albicans SC5314].


LOCUS       XP_718045               1600 aa            linear   PLN 18-APR-2022
ACCESSION   XP_718045
VERSION     XP_718045.1
DBLINK      BioProject: PRJNA14005
            BioSample: SAMN02953594
DBSOURCE    REFSEQ: accession XM_712952.2
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 1600)
  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 1600)
  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 1600)
  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 1600)
  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 1600)
  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 1600)
  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 AOW30273.
            
            ##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..1600
                     /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..1600
                     /product="uncharacterized protein"
                     /calculated_mol_wt=177800
     Region          172..834
                     /region_name="Adenylate forming domain, Class I
                     superfamily"
                     /note="This family includes acyl- and aryl-CoA ligases, as
                     well as the adenylation domain of nonribosomal peptide
                     synthetases and firefly luciferases. The adenylate-forming
                     enzymes catalyze an ATP-dependent two-step reaction to
                     first activate a carboxylate...; cl17068"
                     /db_xref="CDD:473059"
     Site            order(333,336..341,343..344)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341228"
     Site            order(336,481..482,502..507,656,678,681,702,818)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Site            order(336,393..394,447,449..450,453,481..482,502..507,656,
                     678,681,696..697,701..702,796)
                     /site_type="active"
                     /db_xref="CDD:341228"
     Site            order(393,449..450,453,481,696..697,701,772,796)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Region          926..1516
                     /region_name="Adenylate forming domain, Class I
                     superfamily"
                     /note="This family includes acyl- and aryl-CoA ligases, as
                     well as the adenylation domain of nonribosomal peptide
                     synthetases and firefly luciferases. The adenylate-forming
                     enzymes catalyze an ATP-dependent two-step reaction to
                     first activate a carboxylate...; cl17068"
                     /db_xref="CDD:473059"
     Site            order(1082,1086..1091,1093..1094)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341228"
     Site            order(1086,1205..1206,1223..1228,1359,1402,1405,1416,1496)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Site            order(1086,1127..1128,1178,1180..1181,1184,1205..1206,
                     1223..1228,1359,1402,1405,1413..1416,1477)
                     /site_type="active"
                     /db_xref="CDD:341228"
     Site            order(1127,1180..1181,1184,1205,1413..1415,1464,1477)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341228"
     CDS             1..1600
                     /locus_tag="CAALFM_C603430CA"
                     /coded_by="XM_712952.2:1..4803"
                     /note="Has domain(s) with predicted catalytic activity and
                     role in metabolic process"
                     /transl_table=12
                     /db_xref="CGD:CAL0000184041"
                     /db_xref="GeneID:3640273"
ORIGIN      
        1 mshsnnninl kvpgnslsgs nsnhgssssd rhnnrhrsvs aaslnpttgt litgelnetd
       61 pstnitpdig gtsgvggdip pdmaillqkl dedflvnkvi dqwtfinrre eimqsinrlh
      121 qkqnddllnl dplklqmpln prmstgdfsk ispdnlidil tyrantykse lafivldakg
      181 kevssiswek lylkavkvay eiqhkltmkn sdsvvllykd gevtefvval fgcfmagvta
      241 ipihqdislt evlniinlts tklllysetv akeldrlsvq nsrinwpskl lrwrttdlgs
      301 arksevshwn akqqklkkdn ktsseqntnl ayvefsrspv gelrgialsh rtifhqmhcl
      361 dlalsslpns ggglqrsykq yradkkvvla tldirfsigi ilgvlftvys gnvhiwapqk
      421 vmeiqglyan liskwrasll ladyfglkrv tydyqqspsa tryfsktqrv dlssvkwalv
      481 naltidgefm eilaerylrp lgcqhpenai ipmltlseyg gmvislrdwi ggkeklgmsm
      541 kdddsndlss vlidkealsr nivkiveinp sanddighdl lrvdafgypl pdatlavvnp
      601 essvlankde lgeiwidspc lsggfyglrk esksifhakc rgsngqldmd flrtgllgft
      661 fngkvyvlgl yedrirqrvs widqalyqkl hrdlvigngs ryhysshlla tlasevkqiy
      721 dctifdifig neylpvaive aevirkqvad etagaeggna kasesvhvsg vplnepvlna
      781 iaqkcfdtly krhflrlycv vvvdcdtlpk llrsggreia nmlckkkfle gslkadfvkf
      841 firksismip hgedviggiw spyvselrsk alanfpdqys tidyreksin dktgapltdf
      901 ktivdilkfr vaksgdsiaf qnvdnnsksk pltwkklenr ayavcqylie kanikagqyv
      961 ilmyslseef viavyaclmc giiavpmlpf dsnrigedfp afvgvirdfd iseilvndev
     1021 ekflkngpia dslkkithkr vkslkikntv kltkvsnmas lnskiasyqa evnfrdentt
     1081 alvwlnftsd hyrvgatlsn kniigvckvf ketcnlssqs aiigcvrhts gigflqacll
     1141 gvflgtttyl sspvnyaenp lsfflllarh kvkdvfvteq mlkyaaikft pkgfnlsnlk
     1201 nmmistenrv eidllrkiak vfsstklsaa smstvynhyf npmissrsym tvapvdlyld
     1261 pialrqgyvs vvnqaevpna lhiqdsgmvp vcteiaivnp etrkickege fgeiwvcsea
     1321 nltaftngpk gpvdhfaqtq frgviadgnp dvtylrtgdl gflynvsitk nkssnsngga
     1381 sgggggggea dgeittfqpl fvlgkiadtf evmglhhfpi dientiesch sdiyrngsci
     1441 fkcgdytivv ceskrtkyfa slvpliinti lskhhlvidi vafikkgefp isrlgtkqra
     1501 rivdawvqgv ipisasygvn ygensmiklv eeidivtrdd pitglknpal syyddnddqg
     1561 dvfsdnretl klnddynyas igqkaefslg nysnsivsed