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}.
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; 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
//