ID Q5AUF6_EMENI Unreviewed; 1319 AA.
AC Q5AUF6; C8V689;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE SubName: Full=MATH and UCH domain protein, putaitve (AFU_orthologue AFUA_5G01750) {ECO:0000313|EMBL:CBF73830.1};
GN ORFNames=ANIA_08074 {ECO:0000313|EMBL:CBF73830.1};
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:CBF73830.1, 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).
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DR EMBL; BN001302; CBF73830.1; -; Genomic_DNA.
DR RefSeq; XP_681343.1; XM_676251.1.
DR STRING; 227321.Q5AUF6; -.
DR EnsemblFungi; CBF73830; CBF73830; ANIA_08074.
DR GeneID; 2868892; -.
DR KEGG; ani:AN8074.2; -.
DR eggNOG; KOG0229; Eukaryota.
DR eggNOG; KOG1571; Eukaryota.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_002789_0_0_1; -.
DR InParanoid; Q5AUF6; -.
DR OMA; FHPDLDD; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR CDD; cd00121; MATH; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR43215; RADIAL SPOKE HEAD 1 HOMOLOG; 1.
DR PANTHER; PTHR43215:SF14; RADIAL SPOKE HEAD 1 HOMOLOG; 1.
DR Pfam; PF02493; MORN; 4.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00698; MORN; 4.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 148..342
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 386..669
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 1272..1307
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1319 AA; 146929 MW; 099091EF58284983 CRC64;
MDGNSAVMVE QLPVPVPLDT ESSPAEPVTI DTIVQEIPQT PTETVVLQPP HSESEPQQDS
GPDAAATSQE AEVQDSPAAD DSPAAEKEEE DEEHAYWAEE EEDTSAPDEA ELAEIEAQGE
NYNSLDYAYW ESNFHPDLDD PEYRPVEKAR LTWKVKGVRG TKENPNRLKI MRSPPAYIGG
YWWTIKFFPR GNNVSHLSVY IECSSTMPKP DDTLPETEFK VLRGPAETEL DTNKPDLDIK
FDKTKDTEAW TEMFKSQYPA AANQAEPTTE TWRVSAQIGV IVYNPNEPRT GWMQSSCHQF
NPHNLDWGWT NFHGPWDQIH RRQRLQHQAL LRNDTLAFDA YIRIFDDPTR SLWWHPSDSE
PTWDSLGLTG YRPLGDSVIN HSADVAGLAT WLHIAPFSKV IQNVNVLEHL TNCDLKPKPL
CDALQRFLWQ LRRRDQSLQY VDTDTITTTL SNLHEKSSDV CEFWERLRRS LELELAGTPA
ADDLSRLFDS PSPASFPSGA LPTPVHTVPK DFNSRIFVPA DKAKTTSEAF TWYLSAKPGR
WLLPPVLHLE LGRQTLDKAA RQWRLLYNRV DLDEEVDLSP WLLDGQCGKY ILYGYIVHRG
RRTSGKFFSI LRPGGPGTKW LAFDDGSDNR VECLTRKTAL GPHLGLDPDK TPDHKTGHDI
AIAVMYIRSD VIADFLPGPQ GPWEVSDELK HYYETGEVTS QKKNEGKTEV EDIQVEVYSL
EKYDNLSSLF DSYDLMSQAK AANSVMYMSV PRSTNLIEVR KRIGLWASTR SGAEVSPENI
RLWQIGHARD CSATVSLKRV SDLTATVDLP LNPVRYWMQI VSDGDAKYFA MKDPETPVAI
TSKPEEAVVE RPGSETSDDT PTTTSSEGAE PSSSNTGNQN PMDGISGEAG EASPEQPTAE
TVNSTATVAV VVSESEPSPV SADVVAVNAQ APSTTEQNPE DAESPVQIAE SSQPDTSTGA
AASAEATSDE NDAVIAAVIA GDIQQLDEET QETQLPADNQ EQEPNQPPTE DQTSAPAEDQ
TEAPANLEDA APAEPEVVLP VEHVYYYIKV FDIESQSLRT MGSFFSQKEE VIKPAIRKHL
NWPETKDFQV WHQVDGTVVD TLASAETFEI NPADGACFIV GDKLNKAKRT ELSEKGLFSN
PQHLVSYLWA AARNHPTKAF SGTKAVDATF TSDFYSGDFM KGYYHGKGKH ISDSVATYTG
DYVLGKRHGK GFMEYPTGDT YDGDWFEDQC HGQGTFVERK TGNKYVGGYK DGKRHGKGIS
YWEVADEEMD LCQICFGEEQ DALFYDCGHV CACVTCARQV EICPICRKNI LNVVKIYRT
//
