(data stored in ACNUC16935 zone)

SWISSPROT: C8VMP1_EMENI

ID   C8VMP1_EMENI            Unreviewed;       604 AA.
AC   C8VMP1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   05-JUL-2017, entry version 50.
DE   SubName: Full=Oxidoreductin (AFU_orthologue AFUA_8G05140) {ECO:0000313|EMBL:CBF85011.1};
GN   ORFNames=ANIA_01510 {ECO:0000313|EMBL:CBF85011.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF85011.1, ECO:0000313|Proteomes:UP000000560};
RN   [1] {ECO:0000313|Proteomes:UP000000560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R.,
RA   Batzoglou S., Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M., Hynes M., Paoletti M., Fischer R., Miller B., Dyer P.,
RA   Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2] {ECO:0000313|Proteomes:UP000000560}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR017205-2};
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DR   EMBL; BN001307; CBF85011.1; -; Genomic_DNA.
DR   STRING; 162425.CADANIAP00008135; -.
DR   EnsemblFungi; CADANIAT00008135; CADANIAP00008135; CADANIAG00008135.
DR   HOGENOM; HOG000158050; -.
DR   InParanoid; C8VMP1; -.
DR   OMA; CPFWNDE; -.
DR   OrthoDB; EOG092C1KNC; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:InterPro.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0006464; P:cellular protein modification process; IBA:GO_Central.
DR   GO; GO:0034975; P:protein folding in endoplasmic reticulum; IBA:GO_Central.
DR   InterPro; IPR007266; Ero1.
DR   PANTHER; PTHR12613; PTHR12613; 1.
DR   Pfam; PF04137; ERO1; 1.
DR   PIRSF; PIRSF017205; ERO1; 1.
PE   4: Predicted;
DR   PRODOM; C8VMP1.
DR   SWISS-2DPAGE; C8VMP1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000560};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR017205-3};
KW   FAD {ECO:0000256|PIRSR:PIRSR017205-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR017205-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    604       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002992242.
FT   ACT_SITE    400    400       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR017205-1}.
FT   ACT_SITE    403    403       {ECO:0000256|PIRSR:PIRSR017205-1}.
FT   BINDING     194    194       FAD. {ECO:0000256|PIRSR:PIRSR017205-2}.
FT   BINDING     196    196       FAD. {ECO:0000256|PIRSR:PIRSR017205-2}.
FT   BINDING     207    207       FAD. {ECO:0000256|PIRSR:PIRSR017205-2}.
FT   BINDING     271    271       FAD. {ECO:0000256|PIRSR:PIRSR017205-2}.
FT   BINDING     274    274       FAD. {ECO:0000256|PIRSR:PIRSR017205-2}.
FT   BINDING     303    303       FAD. {ECO:0000256|PIRSR:PIRSR017205-2}.
FT   DISULFID     96    101       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR017205-3}.
FT   DISULFID    400    403       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR017205-3}.
SQ   SEQUENCE   604 AA;  69010 MW;  44ECEF6C85BA3F1B CRC64;
     MRSAAKFFYL AVFGFMSQAN ADKHGEKSMH GYDTCAIDHN AVVSDACVSY HTIDALNDQI
     YSLLQSITQE TDFFSYYRLN LFNKVCPFWS ESEGMCGNIA CAVNTIDSEE DIPLTWRAEE
     LSKLEGPKAG HPGRQQQHER PRDKPLQGML GEDVGESCVV EYDDECDERD YCVPEDEGSS
     GKGDYVSLVD NPERFTGYAG AGANQVWDAI YRENCFLKPV PELEQSSFTP LGGLQAIQDF
     QNVLQKESKR PDLLPLDNEC VEKRVFHRLI SGMHASISTH LCWDYLNQTT GQWHPNLQCF
     KERLHNHPER ISNLYFNYAL VARAVSKLRK HLEGYTYCLG DPAQDQDTKE KISLLTSTLA
     ERPQIFDENV MFQDPGAIDL KEDFRNRFRN VSRLMDCVGC DKCRLWGKLQ VNGYGTALKV
     LFEYDETKNG ENPPLRRTEL VALINTLGRI SHSIAAVRSF HRAMEVTDGQ VFAIPAGSTA
     GQSRAGGKKV RRLVKNGGST FYYEDDTAED YQYISQQRPW ERQRVKREGD TIIDDFKAEF
     SVVWDTLIFV LKSWVNIPWT FWEIGVLEAN RLWSYWLGLP VPPRAWRIQL PQRPPPPIVV
     RDEL
//

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