ID A0A177CDC1_9PLEO Unreviewed; 797 AA.
AC A0A177CDC1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=CC84DRAFT_1145197 {ECO:0000313|EMBL:OAG05644.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG05644.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG05644.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG05644.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; KV441552; OAG05644.1; -; Genomic_DNA.
DR RefSeq; XP_018036009.1; XM_018176497.1.
DR AlphaFoldDB; A0A177CDC1; -.
DR STRING; 1460663.A0A177CDC1; -.
DR GeneID; 28759983; -.
DR InParanoid; A0A177CDC1; -.
DR OrthoDB; 1353379at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT DOMAIN 115..554
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 89854 MW; E0CC0975ECE7B0D0 CRC64;
MNGVSRFLSR RDKHHEKRSL KHPLGKSRQA PPSVPPELYK VFTNDEKPVD KDAEKRKTLL
QRLQAAGVTS MQEEQVNYAL SWSPDNVDEA YDLLILANET LEGELKEFDA NITMLGAINR
NMVTCYLDAL LFAMFARMDS FEAMLYDEFN DEPRKKLAAI LRLWVNFLRT GRLIRVDFTK
RLQDALAQCG WEEAAEVRQQ DASEAFTFIT GALELPLLTL KMDIYHTGRE DREDDHKFVN
ERLLEVAIPE EDEADKGVTL EDCLENYFNN RIEVKRYLQR QNTLTSIQTG NTDNEKKETL
HIETVELSGP ETPLVATPTT FGPPSPISPV RPLTGRRRGD SIFTERYTVS GATKDYNRFD
EKKHLEEMLN KSSSGRPRSA SLLRKEVMMP AWQFFSLIPW YTDNVPKTDA QVAAHFSSKR
PVLGICLKRY MMLPNGTTKR LNTYVDIPLE IGLPHFISDE RMQEEGPLFG NFKLVLQSVV
CHRGVSVDSG HYISLVRANK PPSQKRPNTS HTEQEDEEDS WLRFDDLSNP RIADIDIHKA
LREESPYLLF YQVQPIDEEL ANRGDPPSYN EAQSVTLSTA PSKETLSSET DATTDTETGE
WEKVSSVEQS ASTVGSITDF EAQGRTSTSS NRRSSIAIED LDNSISNTAR GRPPPTPDEQ
RTGFLSASRR NSKAWLSGNK SRPSSESGEN RLSMTLSRLT GRGSKDKLVA SENVSEEPVI
VVNEAPLSVE STQTIKPQAQ PPASPGKLHK EAGVSRSKSK KHFRSKSREP APSTTDGVQV
KGKHKAKDRP ERECVMM
//
