(data stored in ACNUC7421 zone)

SWISSPROT: Q4W9X3_ASPFU

ID   Q4W9X3_ASPFU            Unreviewed;       413 AA.
AC   Q4W9X3;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 105.
DE   SubName: Full=Flavohemoprotein {ECO:0000313|EMBL:EAL84490.1};
DE            EC=1.5.1.34 {ECO:0000313|EMBL:EAL84490.1};
GN   ORFNames=AFUA_4G03410 {ECO:0000313|EMBL:EAL84490.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL84490.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL84490.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00238}.
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:EAL84490.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAHF01000016; EAL84490.1; -; Genomic_DNA.
DR   RefSeq; XP_746528.1; XM_741435.1.
DR   STRING; 746128.CADAFUBP00009685; -.
DR   EnsemblFungi; EAL84490; EAL84490; AFUA_4G03410.
DR   GeneID; 3504053; -.
DR   KEGG; afm:AFUA_4G03410; -.
DR   EuPathDB; FungiDB:Afu4g03410; -.
DR   HOGENOM; HOG000238921; -.
DR   InParanoid; Q4W9X3; -.
DR   KO; K05916; -.
DR   OMA; ADIHYEV; -.
DR   OrthoDB; 696109at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0004155; F:6,7-dihydropteridine reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008941; F:nitric oxide dioxygenase activity; IBA:GO_Central.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   GO; GO:0071500; P:cellular response to nitrosative stress; IBA:GO_Central.
DR   GO; GO:0046210; P:nitric oxide catabolic process; IBA:GO_Central.
DR   Gene3D; 1.10.490.10; -; 1.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR023950; Hmp.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR43396; PTHR43396; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00042; Globin; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4W9X3.
DR   SWISS-2DPAGE; Q4W9X3.
KW   Heme {ECO:0000256|PROSITE-ProRule:PRU00238};
KW   Iron {ECO:0000256|PROSITE-ProRule:PRU00238};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00238};
KW   Oxidoreductase {ECO:0000313|EMBL:EAL84490.1};
KW   Oxygen transport {ECO:0000256|PROSITE-ProRule:PRU00238};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transport {ECO:0000256|PROSITE-ProRule:PRU00238}.
FT   DOMAIN          6..135
FT                   /note="GLOBIN"
FT                   /evidence="ECO:0000259|PROSITE:PS01033"
FT   DOMAIN          149..266
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   METAL           53
FT                   /note="Iron (heme distal ligand)"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00238"
FT   METAL           86
FT                   /note="Iron (heme proximal ligand)"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00238"
SQ   SEQUENCE   413 AA;  45609 MW;  BCB4A40270F79CA0 CRC64;
     MPLTPEQVQF IKATVPVLAE HGTTITTVFY KNMLTAHPEL NNVFNTTHQV TGHQARALAG
     ALFAYASNID NLGALGPAVE LMCHKHASLY IKPDDYKIVG KFLLEAMGQV LGDALTPEIL
     DAWATAYWQL ADIMIGREAQ LYEQAEGWTD FRDFVVALKV PESSEITSFY LKPADGKPLP
     AFQPGQYISV QVHVPELNYL QARQYSLSDM PRSDYYRISV KKESGLNPAE PGAKAHPGHV
     SNILHASVNE GDTIKVSHPF GDFFLSDAKA AHPVVLLSAG VGLTPMTSIL NTLTSQAPER
     KVSFIHGARN ARARAFKNHI TSLEQKLPNL KSTFFTSHPT EEDKEGDDYQ FRGRVDLSQL
     DSNRDLFLDD ATTEYYVCGP DTFMTDMLNV LKSKGVSEDR VKLELFGTGG VPH
//

If you have problems or comments...

PBIL Back to PBIL home page