(data stored in ACNUC16935 zone)

SWISSPROT: Q5BD07_EMENI

ID   Q5BD07_EMENI            Unreviewed;       545 AA.
AC   Q5BD07; C8VN15;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   05-JUL-2017, entry version 94.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBF85140.1};
GN   ORFNames=ANIA_01573 {ECO:0000313|EMBL:CBF85140.1};
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:CBF85140.1, 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   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01103,
CC       ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00692226}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01103}.
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DR   EMBL; BN001307; CBF85140.1; -; Genomic_DNA.
DR   RefSeq; XP_659177.1; XM_654085.1.
DR   STRING; 162425.CADANIAP00008205; -.
DR   MEROPS; A01.015; -.
DR   EnsemblFungi; CADANIAT00008205; CADANIAP00008205; CADANIAG00008205.
DR   EnsemblFungi; EAA64280; EAA64280; AN1573.2.
DR   GeneID; 2875525; -.
DR   KEGG; ani:AN1573.2; -.
DR   HOGENOM; HOG000159040; -.
DR   OMA; GYNSSEA; -.
DR   OrthoDB; EOG092C3KPP; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0031362; C:anchored component of external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd05474; SAP_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom.
DR   InterPro; IPR033876; SAP-like.
DR   PANTHER; PTHR13683; PTHR13683; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5BD07.
DR   SWISS-2DPAGE; Q5BD07.
KW   Aspartyl protease {ECO:0000256|PROSITE-ProRule:PRU01103,
KW   ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00629219};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000560};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01103,
KW   ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00629231};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01103,
KW   ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00629201};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560}.
FT   ACT_SITE     90     90       {ECO:0000256|PROSITE-ProRule:PRU01103}.
FT   ACT_SITE    292    292       {ECO:0000256|PROSITE-ProRule:PRU01103}.
SQ   SEQUENCE   545 AA;  58093 MW;  4C78AE23AD19FF4C CRC64;
     MSVLLVFSLV TFALQGLCSL SLHESDSPHV LQLGLRRNQH NDPVGRDRRR FKRQTGTVAV
     DLHGDSMGGD IYSTNLTIGD PPQAVEVSVD TGSADLWVVY SENPVCNVRG ARCDDSGTYD
     PTASTSFDGL SDEFAIEYGD SSWAEGYYGI DTLTVADAEV SEVQFAVAVE SSIDKGILGI
     GYSTNVVSTY RYPNLPERLV ASNITSSNAY SLWLNRLGSD EGTILFGGVN TAHYTGPLRT
     LPVVRYNGHY IHLWLTLTGM GVESASDDIT KSYSETRSTT GEQEFPFVAL LDSGATLTYL
     PSNIVAQIFS DLDVHLYEPE QFGYVPCDTY LVGREDYNLT FTFSGVTIRV PLRELVLRDA
     ISGPGRDALQ LPNNADEESC LFGILPNTDL FPILGDTFLR SAYVVFDLDN NEISLAQANT
     APGDDRILEI GSGDDAVPEA EDVDDPVTTA TVSLGGSSLI LPTGWTNEPI FPSRTVTTST
     TATSTGTNTG SGEDTEATDS DQGTSGGTGT QAEGPVATDG AVGVGNSPLL AIAMAALVLN
     MVLAL
//

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