ID A0A0K9P952_ZOSMR Unreviewed; 613 AA.
AC A0A0K9P952;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=ZOSMA_353G00110 {ECO:0000313|EMBL:KMZ64685.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ64685.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMZ64685.1}.
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; LFYR01001110; KMZ64685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9P952; -.
DR STRING; 29655.A0A0K9P952; -.
DR OrthoDB; 55585at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF687; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KMZ64685.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987}.
FT DOMAIN 259..612
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 613 AA; 67530 MW; D793E08BBFA069A4 CRC64;
MSHNSNVVLF GSFSEEETKK IQMELAMYKK SEQKTYLQFG SLHFKFAVLS TTMKSESKKP
DHSLASESLH NSKKILENQK SMSTHSNGNS DNCSLISKKH PENGEMAKIL NPAASVIEGV
LETEDSSGKS LADVISTTTN KSVENDVLDP YVNLKNGLQK FNFQEIPNSD NCSLISKKHP
ENGEVANVLN PAASVIEGVL ETEDSSGKCL ADVISTTTKR SLENDTLDPC VNLKNKLPSS
IFQEIRNGDA VALNPLLPRG LINSGNLCFL NASLQALLSC SPFVELLQHL RKHDIPKIGF
QTLNAFVEFI SNFDMPRDSS LKKNDTSVIE IGKSFISNSF EAVLKKFTPH SANNTSSRPR
QEDAQEFLTF VMHQMHDELL NLDGNFINSN GHASSMISSA DVAGWATVGP KNKPAVTRTQ
TFTPSELSNI FGGQLRSVVK ARGNQASATV QPFLLLHLDI SSNTVCTIED ALHRFSLPEI
LEGYKAEAGN SASGNAIKAI KIQTVPKILI LHLMRFSYGS RGVAKIHKPV RFSPELVLNY
DLLVYPTLEM GRRYELVASI THHGRDPSKG HYTSDARHSS GKWLRYDDAS VTSVSADAIL
HDQAYVLFYK QKN
//
