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Reviewed, UniProtKB/Swiss-Prot P78588 (FREL_CANAL)

Last modified June 16, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable ferric reductase transmembrane component
    EC=1.16.1.7
Alternative name(s):
    Ferric-chelate reductase
Gene names
Name: CFL1
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length669 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

2 Fe2+ + NAD+ = 2 Fe3+ + NADH.

Cofactor

FAD Probable.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the ferric reductase (FRE) family.

Contains 1 FAD-binding FR-type domain.

Contains 1 ferric oxidoreductase domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 669669Probable ferric reductase transmembrane component
PRO_0000210151

Regions

Transmembrane122 – 14221 Potential
Transmembrane198 – 21821 Potential
Transmembrane234 – 25421 Potential
Transmembrane281 – 30121 Potential
Transmembrane313 – 33321 Potential
Transmembrane340 – 36021 Potential
Transmembrane499 – 51921 Potential
Domain239 – 373135Ferric oxidoreductase
Domain374 – 492119FAD-binding FR-type
Nucleotide binding437 – 4426FAD Potential
Compositional bias65 – 7713Poly-Ser

Amino acid modifications

Glycosylation201N-linked (GlcNAc...) Potential
Glycosylation521N-linked (GlcNAc...) Potential
Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1521N-linked (GlcNAc...) Potential
Glycosylation5241N-linked (GlcNAc...) Potential
Glycosylation6531N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
P78588-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: E3373CF93EAC2A83

FASTA66974,748
        10         20         30         40         50         60 
MTESKFHAKY DKIQAEFKTN GTEYAKMTTK SSSGSKTSTS ASKSSKSTGS SNASKSSTNA 

        70         80         90        100        110        120 
HGSNSSTSST SSSSSKSGKG NSGTSTTETI TTPLLIDYKK FTPYKDAYQM SNNNFNLSIN 

       130        140        150        160        170        180 
YGSGLLGYWA GILAIAIFAN MIKKMFPSLT NNLSGSISNL FRKHLFLPAT FRKKKAQEFS 

       190        200        210        220        230        240 
IGVYGFFDGL IPTRLETIIV VIFVVLTGLF SALHIHHVKD NPQYATKNAE LGHLIADRTG 

       250        260        270        280        290        300 
ILGTFLIPLL ILFGGRNNFL QWLTGWDFAT FIMYHRWISR VDVLLIIVHA ITFSVSDKAT 

       310        320        330        340        350        360 
GKYKNRMKRD FMIWGTVSTI CGGFILFQAM LFFRRKCYEV FFLIHIVLVV FFVVGGYYHL 

       370        380        390        400        410        420 
ESQGYGDFMW AAIAVWAFDR VVRLGRIFFF GARKATVSIK GDDTLKIEVP KPKYWKSVAG 

       430        440        450        460        470        480 
GHAFIHFLKP TLFLQSHPFT FTTTESNDKI VLYAKIKNGI TSNIAKYLSP LPGNTATIRV 

       490        500        510        520        530        540 
LVEGPYGEPS SAGRNCKNVV FVAGGNGIPG IYSECVDLAK KSKNQSIKLI WIIRHWKSLS 

       550        560        570        580        590        600 
WFTEELEYLK KTNVQSTIYV TQPQDCSGLE CFEHDVSFEK KSDEKDSVES SQYSLISNIK 

       610        620        630        640        650        660 
QGLSHVEFIE GRPDISTQVE QEVKQADGAI GFVTCGHPAM VDELRFAVTQ NLNVSKHRVE 


YHEQLQTWA

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References

[1]"Isolation of the mRNA-capping enzyme and ferric-reductase-related genes from Candida albicans."
Yamada-Okabe T., Shimmi O., Doi R., Mizumoto K., Arisawa M., Yamada-Okabe H.
Microbiology 142:2515-2523(1996) [PubMed: 8828219] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10259 / CBS 5796 / IFO 1060 / JCM 2078.

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Cross-references

Sequence databases

D83181 Genomic DNA. Translation: BAA11834.1.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.16.1.7. 1124.

Family and domain databases

InterProIPR013112. FAD_bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_reduct_TM_N.
IPR013121. Fe_red_NAD_bd_6.
[Graphical view]
PfamPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameFREL_CANAL
AccessionPrimary (citable) accession number: P78588
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: June 16, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Candida albicans

Candida albicans: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents