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Database: UniProt
Entry: E4UUY3_ARTGP
LinkDB: E4UUY3_ARTGP
Original site: E4UUY3_ARTGP 
ID   E4UUY3_ARTGP            Unreviewed;      1471 AA.
AC   E4UUY3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   SubName: Full=MATH and UCH domain-containing protein {ECO:0000313|EMBL:EFR01100.1};
GN   ORFNames=MGYG_04104 {ECO:0000313|EMBL:EFR01100.1};
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN   [1] {ECO:0000313|Proteomes:UP000002669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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DR   EMBL; DS989824; EFR01100.1; -; Genomic_DNA.
DR   RefSeq; XP_003173930.1; XM_003173882.1.
DR   STRING; 535722.E4UUY3; -.
DR   GeneID; 10029217; -.
DR   VEuPathDB; FungiDB:MGYG_04104; -.
DR   eggNOG; KOG0231; Eukaryota.
DR   eggNOG; KOG1571; Eukaryota.
DR   eggNOG; KOG1863; Eukaryota.
DR   HOGENOM; CLU_002789_0_0_1; -.
DR   InParanoid; E4UUY3; -.
DR   OMA; PAYIGGY; -.
DR   OrthoDB; 383715at2759; -.
DR   Proteomes; UP000002669; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
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; 1.
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; 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; 3.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00698; MORN; 3.
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; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002669};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN          260..474
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          1424..1459
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          965..1078
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1090..1184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..207
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        976..990
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1017..1037
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1129..1143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1144..1172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1471 AA;  164056 MW;  56D236BAF3CB287C CRC64;
     MEVAVEAQRA SLSHQPAPPY TSSPQTHASE ESEPQPESRD RHQDEQTQDQ PLQNGIMPTL
     ENAPPSSATH SSATETESSA PDRPVVETLA PVSTETTEQS VNTQVVEVIE TPAADAPVVN
     GEPDTMETDT AANGGQAPAD GQIQSQNENT PVNGTTEQDD RSHPRENEEP SEESSPSTAS
     DGSTDSSEST ERTGEDYDEE DENDEPAYWA EYKEDTSVAE GDELKEIESG DADHSAHEYD
     YIEKSFYHEL DDPEYKPIEK ARITWKITGI RGTKEKPNRA TIIRSPPAYI GGYYWTLKFF
     PRGNSVGSLS VYLECSPTPP VQDKVVLETE FRVLKGAPDA VLSDLTPDQE IKLAATVTPP
     PKPATPEESA SKNQEKDREE LPEVDSEEKT ECESPSKPKP DFRISAQIGV VLYNPEEPRT
     GWTQSSCHQF NSHNFDWGWT HFHGPGPWNT IHLRQHGQRQ ALLRNDTLCF DAYIRLFDDP
     TKSLWWHSSD SEPIWDSYSL VGLRPMGDVS VNYCQHTAGL VPWLLLTPFR DIVKSIGVMD
     HLDHIAARPK PVCEALQVIV HEMTAENIAS VRTEGVRRAL RYLLEGSGDV VEFWERLRRS
     LQIELAGTDA IEKLASIFDS PHDDSKMSDE SLNMLPRDFN SRIRITSENT ESIQCGVTEY
     LKSREGKWSL PPVLQVELAR QKFDKKARQW KFLVNRVHRN EELDLSNFVD SEAQGKYTLF
     SFIAHKGHRT SRWYYPLVRP GGQGTHWLAF KGEDPYRIEC LTAKTAAESY EGLDIAEVGN
     GEPVNAEIAV AFIYIRNDLQ DQFLTPKLDS WTPPPAWHRY MQAISPDKSA VKPDEQIPVA
     FYGLNGVSKD ARNPAAAYDV IDHLNSEKDT TTMTVPVSTT VGELRAKLAA QISTEEKPVT
     SERIRMWTVG APHEVRLFNF SMEPLVSMGS QLLSLGWNAL RIWVQILNEE DVKYFSIPEF
     VPPPPVPNEA NETKDDVPAP PPPPPVQNEE QPQPTQEAQP PSQDEDVEMN DASPEEIPIQ
     PPQNQDGQEQ QSDNLPSAPE PPEHEMSDNA PDQPETNGVE PTPAPEGQTD EQAANEAIIA
     SIIAQDLALL DESQEMDTSE GYTDANAIPP PPPAVVEEVS TNSAGNEAEE GREAQEHHSG
     SEDSQMEGSP IVESRNNVPE ETNAQTSQEE AQREEPAVPE PPVIKSDLIL PCDQVYYFVQ
     EFDADRQTVE TVGAFFARSS CNVREEVRKT LGLSEDQGYN FWSRRKAVAS VHSVSSSHRF
     RDLMNDVGCI IFGKTIPKRR QTELVEAGCF LSPDRLLEYL WAVARQHPIK SFTGKKTVEA
     ILNGEYYSGD LCKGYYHGSG THISEAGDTY SGDFVQGRRQ GTGTIEHSSG DTYTGDWFED
     QPHGQGTWVE HKTGNKYVGG YRNGKRHGKG VSYWEVADEE MNLCQICYTE EQDSLFYTCG
     HVCACGTCAR QVEICPVCRE KVISVVKIFR C
//
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