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Database: UniProt
Entry: C8VKH9_EMENI
LinkDB: C8VKH9_EMENI
Original site: C8VKH9_EMENI 
ID   C8VKH9_EMENI            Unreviewed;       980 AA.
AC   C8VKH9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=WD repeat protein (AFU_orthologue AFUA_2G04360) {ECO:0000313|EMBL:CBF85744.1};
GN   ORFNames=ANIA_01879 {ECO:0000313|EMBL:CBF85744.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF85744.1, 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., Batzoglou S.,
RA   Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA   Dyer P., 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., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; BN001307; CBF85744.1; -; Genomic_DNA.
DR   RefSeq; XP_659483.1; XM_654391.1.
DR   AlphaFoldDB; C8VKH9; -.
DR   STRING; 227321.C8VKH9; -.
DR   EnsemblFungi; CBF85744; CBF85744; ANIA_01879.
DR   GeneID; 2874995; -.
DR   KEGG; ani:AN1879.2; -.
DR   eggNOG; KOG2276; Eukaryota.
DR   HOGENOM; CLU_008535_0_0_1; -.
DR   InParanoid; C8VKH9; -.
DR   OMA; HATVCVD; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR   GO; GO:0006751; P:glutathione catabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR017149; GSH_degradosome_Dug2.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR   PANTHER; PTHR43270:SF8; DI- AND TRIPEPTIDASE DUG2-RELATED; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   Pfam; PF00400; WD40; 2.
DR   PIRSF; PIRSF037237; Peptidase_WD_repeats_DUG2; 1.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW   WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT   REPEAT          93..134
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          247..275
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          377..403
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        823..837
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..900
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   980 AA;  106519 MW;  C02423D70CB64FBC CRC64;
     MDNTGLAESD SPSDIDEQTK AWESDPRSVR AHLAQTDGVD DAVPQIECGI GHRVQASRSV
     LALVVDEDCV FAGLQGGDIV AWSLDNYDLV LSVRAHQESV LDLYLSEKGD LLFSSGGDSV
     VNVWSTRTFE RLYSIHSHHD VGDLFAVSYS PSLNTIYCGA QNTSIQWCNL SQSGAASTQQ
     SAAHLSKRTH RFFDSKGPDG TRAPRADGNS VADGGQVLTF KRDHHNLFAH HGYVYTMTLV
     RGLLESSPND EVLLTGAGDG VVKLWRLEQG KPDSAPALMA RLHNTDPVLS VAVEGSFLYC
     GLSGGALNIW NLDSHQLVKR IAAHTGDLWA VDIIHGMAVC GDSNGIVKKF NSRFEEVGSW
     AAHEGTMLAS AAGKFKDRHI YATGGNDNTV GIWDLTDVSL SASEKPPIDN DEMVSCLAKL
     VAFKTISASP KFAGECNQGA AFLRRHCIYL GAKTKLLTTG EDTNPIVFAR FSAISPETTN
     KTILFYGHYD VVGADANRQR WKTDPYQLTS MDGFLYGRGV SDNKGPILAA LYAAAGLARQ
     KTLRCNVVFL LEGEEESGSQ GFHETVRKHK QQIGPVDWIL LANSYWLDDY NPCLTYGQRG
     VVHANLIVTS DHPDLHSGID GSSLLDEPLK DLTMLLGTLV GPKGKVNLPG FQDPVLPLTD
     VERERYGAIA EILLKQHPQI KDAGALIDSL MHRWREPSLT IHSVEVPGSS KSTTTTISRK
     AKASLSIRIV PNQSADEVAA ALTLYAQEQF DQLESQNELT VEITGTSDPW LGDPDNEIFE
     TLSEAITAAW TPDQQSLKHQ YSLPRRAIGD RTASPRGAKD TVTSALRRQD SEDSLASHID
     RIIMSTTTSK TTTRHRSSLS TTVPTSSTLT GQSNKQTADS TTASPPGPAA TSSALSPTGT
     DGPAEVSREK IGVRPIYIRE GGSIPTIRFL EKEFCAPAAN LPCGQASDNA HLYNERLRVE
     NLYKSREIFS YVFSRLPEKT
//
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