ID A0A1W5D8H5_9LECA Unreviewed; 1594 AA.
AC A0A1W5D8H5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Lasallia pustulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC Lasallia.
OX NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM39345.1, ECO:0000313|Proteomes:UP000192927};
RN [1] {ECO:0000313|Proteomes:UP000192927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma R., Thines M.;
RL Submitted (MAR-2017) 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};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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; FWEW01003499; SLM39345.1; -; Genomic_DNA.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000192927; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR CDD; cd17039; Ubl_ubiquitin_like; 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; IPR029071; Ubiquitin-like_domsf.
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 SUPFAM; SSF54236; Ubiquitin-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 Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 155..280
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 525..1357
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1375..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1503..1531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1594 AA; 174208 MW; A5D6682959AB71EE CRC64;
MAQPADPRAQ GGSLLPDRSS TSATKRRASD MGRANTGMQG EDVEMVGSQS ADLPTVPATA
NTVLDATPPI QVGSAQNPEA RHNREVSVDM LAYDQGVSSK TSSKTTASET VSESTSSAAY
MTPHSGIPSS NSLNGAPEVL DASERQAVVS APDLPPIDEQ IKRVKDLASV PMQAGQKGYV
VSMKWLSRVL SRGSHDNGKD TYGKEAKEGP IGPVDNTGLN VIRDPLFGDF EDEAGEPYIP
LRPGLQLPED FEIVPQEAWE LIIKWYGLSK GSPIITRYIH NTSTGAMENL QYEIHPPVFT
ILKLPDSHGT GTTVQALKEK QRDAIPVRVL ASRHEGFQHF LKRVKAMAGI ELKTKVRIWR
ILAGLGTGPS SGMITPAQSR SASPAPNVIV PVDPGNRLVL DVHSFAALQV GSQREMLDAR
DETANVYYNG HMNLDLVGLR QDEVIVLEEQ IGGPAGGEWV SDAVGKQLSK NNVPINLTKS
GTSTGPDKLK PGSFTAGGRA SPTPGSSGMI TRGRQQKTGK ARGTVGLNNL GNTCYMNSAL
QCVRSVEELT QYFLMEKYKA ELNPGNPLSH NGNVAKAYAS LLHELYSENA VSSFAPRNLK
NTIGKYGPSF SGYGQQDSQE FLLFLLDGLQ EDLNRIHKKP YIEKPDSTDQ MVHDPLALRE
MADKCWDIYK ARNDSVITDL FAGMYKSTVV CPVCDKVSII FDPFNNLTLQ LPIENVWTKQ
IFFFPLNSRP IQVRVEINKN ASFMALKEYI CKRTKVDPKR TVLAEIYKNR IYKMFDDNAS
ISDERIQDGD SIALYEVEDV PSNYPPPKKK GQKIRSMLYT SYSNSDEEED VPEGDSPLAE
KMLIAVFNRQ IKDGGHSRYQ QRALVGVPFY VIITRDEAKD YDAILRKILA KIATMTSLDI
LGDENSSDTE STQHEDSDTV LMARDDGDSS SDSKVQARSV ESEDGMVDIS MRDAGEKSDG
VPHLSSPPEN CGKRRTPHVL EPGAFIKPEL RTLFDMKYFS GTEMIPTGWS TLNDENKNYP
SIASRIPQPV AQPISRPMAN KLARRLQGNA SSSSSDEDVD DLPPLVGNNA LINPGSDSDS
DGLPLVEELH QPVQGFNAPG FSRFNKHTPR TKRGLITYSR KGKHFPVDAD LQASEPGSNT
ESTPLIRLGE AIVLDWDTQT FESLFSVSER DNDNDMRGSA TWDNVPLMPD PELENKRQLR
LSRKKNGVSL DDCLDEFGRP EILSENDAWY CPRCKEHRRA SKTFELWKSP DILVVHLKRF
SAQGRLRDKL DVFVDFPVEG LDLSSRVAMQ EDGKSPIYDL FAVDNHYGGL GGGHYTAFAK
NFYDNNWYEY NDSSVSRRPN PQAVVTSAAY LLFYRRRSPQ PLGGPFFEKI ISAASSLDSE
PQPDSRATSP AGEGKRLGDF SRNGSSSALL GVGAAHQAGS GGLADDELQA RNVANADDVL
PGYSMDLRAG EQTLESMEMD EESGAGIHSS LGTSFGPTNW SFAGLPNGDG EHGMAGISQV
TVLPPGSDQG DDEDLFDGAS NKAASSAGLS DDEGTRILTD FADDAGTTHG AFGTPLISRE
GTPVQEVPPA LEMVESDNEP AAEVRLHEDV FEME
//
