ID A0A316VTP4_9BASI Unreviewed; 1556 AA.
AC A0A316VTP4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=IE81DRAFT_367844 {ECO:0000313|EMBL:PWN40949.1};
OS Ceraceosorus guamensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN40949.1, ECO:0000313|Proteomes:UP000245783};
RN [1] {ECO:0000313|EMBL:PWN40949.1, ECO:0000313|Proteomes:UP000245783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN40949.1,
RC ECO:0000313|Proteomes:UP000245783};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; KZ819402; PWN40949.1; -; Genomic_DNA.
DR STRING; 1522189.A0A316VTP4; -.
DR InParanoid; A0A316VTP4; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000245783; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000245783}.
FT DOMAIN 280..394
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 617..1395
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1402..1425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1556 AA; 169877 MW; 195C2AD7A1AF7BBC CRC64;
MPSDSTSQSE QAHQRGSSSK AHQHQTVDST LNAHTLRPQS SFTQHQPLQH TPESSDCATP
DSPRTSARRP CPLSPGRPGI PFRSDYNPDL ALAANTARAS SSSDLAVFSS DDQLDLVPRR
SGGSNYKRAR TASPATTEEL EAEGETEAGA GSDFADSEGN SITSGTAART RLPTPLRVGF
AKQSIGSFAP SPASTSPFHS STRSSNLASR MSPDDQPSRA HLTSQDVEMA DDQSAPLAAP
SAQPRSTHPT IEGSLPTYTD AMQQSVSCHT PAEPGTPAEG TCAEELRKIK KLVEEPLAEG
QRWYLIDAAW WAAWQAYCSA ESSAPAQPLG EAIDSSRASA KPGPISARSL MDIEEELKLQ
LFEGSDFVLL PETAYASLST LYGEAGPQVV REVIKGAASE LRIELYPPRL YLYRLATPAT
LQSSARPPVK ITLSVTSNVS QLKFAAKRAF LSENLPDHAV RFWRIPASAF GNAQTTEPVL
VDAETLKTPG VELVRASEDA QTRTRLSLAE LQLDEPVIHL AVESQSERGA WHFGADGVPV
AVAPSVKNIF AQQPNQDYLS QRFGQFSTSG AAAASTSNTS APPAPPPRPT SSAGRVTRSQ
TAQDRANAAG IGSYGLTGLY NLGNTCFMAS ALQCMSNTKE LKEYFVRGVY KEEINTDNPL
GMGGAVARAF GELLLKLWSS SRGSAVHPRE FKQTLARFAP QFSGFAQQDT QELLAFLLDG
LHEDLNRVKK KPYIEAPDWE GGDEKAMIAF AKRQWEIYKM RNDSVIVDLF QGQYKSTLVC
PECSKVSIKF DPFMYLTLPI PNRKKIIRKV FVRPFASTRP TYEVEVAGPA ELTFGQTKTK
LAEWLGLDTK RLFCVDIFNQ QIFNFIPDYT PLSSITDNDF MTFYELGAEF KHPTREALES
GNAGWNKSKE AGPAPQEEYA TLPVFGVASS SGRARYPDAV GLPLFVTIPK AHANDADFIR
DAILDQYCTY ATPEGRDTLE AHMRSSGSRD AVTAKRDAEE ASPSDLHEQQ MSNAEHDVVQ
HVDLSLSRQD PPDQVAEITS DGVRMVPDSS TSAEVTQASD QDAPNAQRPA RRLFKMTFSN
RLEDNAPMPK KPGSLDDGEE LEARAKRLSE RVPTASDVPL EDASDGGAPF ASRKPDPENE
VDRQGTTWPL VYTGGAIVCS WPEAAYRAVF AGETSNQKVP WGPHETFTDP NLVAEREAAR
ANGGPSKPKL VTIEDCLDEF TKEEKLGAED PWYCPSCKDF RQAAKKFDLW KVPDILVVHL
KRFSAGRMQS RDKIENLIDF PIQGLDLTER VEGAMSVRNL EARGEEVPSV MNMAESIESL
ASDANDDAVA ADAPIYDLYA VDNHFGGLGG GHYTAYAKNP DDGQWHYFDD SSVTPVADPE
SVKTKAAYLL FYRRRTTRPI GGKSREKTEI ASSRAQSEAV EEVHADENDD ALTVVSKAAS
CENLSPALHH LLRQSTSRGL KAAQIGLGLE RWTTTRGAMS LHRVGTARPR LRAPIGGRHC
QSKATLFCRS EIPCHKASLF HTPQKLKVLP RPPSRSCRPI QMTLSFLPTK SKLEGY
//
