ID A0A2K2CW65_BRADI Unreviewed; 960 AA.
AC A0A2K2CW65;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 08-NOV-2023, entry version 28.
DE RecName: Full=USP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=100841955 {ECO:0000313|EnsemblPlants:PNT66262};
GN ORFNames=BRADI_3g09260v3 {ECO:0000313|EMBL:PNT66262.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:PNT66262.1};
RN [1] {ECO:0000313|EMBL:PNT66262.1, ECO:0000313|EnsemblPlants:PNT66262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:PNT66262.1,
RC ECO:0000313|EnsemblPlants:PNT66262};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:PNT66262.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:PNT66262.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:PNT66262}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:PNT66262};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; CM000882; PNT66262.1; -; Genomic_DNA.
DR EMBL; CM000882; PNT66263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K2CW65; -.
DR EnsemblPlants; PNT66262; PNT66262; BRADI_3g09260v3.
DR EnsemblPlants; PNT66263; PNT66263; BRADI_3g09260v3.
DR Gramene; PNT66262; PNT66262; BRADI_3g09260v3.
DR Gramene; PNT66263; PNT66263; BRADI_3g09260v3.
DR Proteomes; UP000008810; Chromosome 3.
DR ExpressionAtlas; A0A2K2CW65; baseline.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02661; Peptidase_C19E; 1.
DR Gene3D; 6.10.140.2220; -; 1.
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 InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF685; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 15; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..125
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT DOMAIN 425..730
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 184..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 106377 MW; C1638F4E83C222F3 CRC64;
MLQPREADVP ALFVVFIVLP VIAYFLLGRW HDAVSKKARV GVLAQKAAEE DFKVETMACP
DVVLPGPSLR PMPYLRSVPS FRPEYHECAT CHGPAKTRCS RCKSVRYCSG KCQIIHWRQG
HKQTCQLWHV NGGSNSGLLP NTEGSEQMPF LSNLNSPLPG GDNHLHDLNF DTVSEPSFAT
TDSYTLGTDA FPTEKSNQNP HSSENGASVA SSEKCNHSVD DETRSSEIAS ANKVSNNSFG
CSDGKNGNPD STYLHNGMVQ HPNSCAPETR KRPKASITVY EPDMGVYLTS DMISSCEGPY
ASATESLQRS NSSGKATGKG NMVHKKPPYP SGKVASSQKS QEVSTSYQYD DHEKNPYSKS
DQRFTKPSVS TSNNLQGSNG TSKLGISKVD VLRKPSKFLK TSLVLFRYED LVKFFQYEVR
GISPRGLFNC GNSCYANAVL QCLMCTKPLM IYLLLRLHSK DCSKNGCLMC ELEQYASTLR
ESGGPVSPSR ILSNLRNIGC RLGGGSQEDA HEFLRHLVMS MQAACLDGLG GEKHVEPSLQ
ETTLIQQMFG GRLKSKVKCL RCLHESERYE NIMDLTLEIH GWVESLQDAL TQFTAPEDLD
GENMYKCGRC CAYVKARKQL SVHEVPNILT VVLKRFQTGK YGKINKCVTF PEMLDMVPFV
TGAGDHPPLY FLYAVVVHVD TENASFSGHY ISYVKDMQGT WLRIDDSEVK AVSPNQVMSE
GAYMLFYLRS FPRPPRIYIE KGLLPVTSSA KRHSSKSSKG SKEEQKLAES LFASNDKICG
VYDFRPDEEG YRQDQHAELR PRNFYHTDDA FAESVSTDFS DATSSEWSLF TSSDESSFTT
ESTRDSFSVV DYSDNAGLDP ITSIFGPYYA PDHPPGNFAS CTRFSPSNPE TRYFSESTGF
VSDSSSLPTH PYGNVHRGRY PDRACASSAE PLASANQRSV YGRYGHSRDG FVQTSGFCHM
//