ID   A0A1D6KLH0_MAIZE        Unreviewed;       649 AA.
AC   A0A1D6KLH0;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   08-NOV-2023, entry version 35.
DE   SubName: Full=Ubiquitin carboxyl-terminal hydrolase 17 {ECO:0000313|EMBL:ONM03743.1};
GN   ORFNames=ZEAMMB73_Zm00001d031832 {ECO:0000313|EMBL:ONM03743.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM03743.1};
RN   [1] {ECO:0000313|EMBL:ONM03743.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM03743.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; CM007647; ONM03743.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6KLH0; -.
DR   ExpressionAtlas; A0A1D6KLH0; baseline and differential.
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   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:SF874; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 16; 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; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ONM03743.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          148..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..370
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   649 AA;  70485 MW;  6246B9C96B25A23B CRC64;
     MEEAAESSSA AAAAALVLAL VALVVVPAVA LLVRGRWRRA AARREEVRRL ARLAAEESEL
     AERESALAYY SELFPGVVHA AGAPEWGPPP VAVPVPAQEE FDAQPQPSVG AKGVCAVCFR
     PTTFRCKQCK AVKYCSFKCQ IAHWRQGHKD ECHPPSVNTR PDDEEEKAEV GKSAKENASV
     GVKQDAQMNK PAVGSETSDA NHDLKSSNGK SKHMPSEAVC TSAEIPGGHK SNSTVEIDQN
     IQSVDSSKMG SSIKHANFVE DGSSTVDLNE ALPCNSHSSS PNINGHSSFV NEEFCNHSKE
     HQRAKDASVV EDCSQTSSTR ELEDSSIPHA AASVVLESKS SRTPIHVELE RSKTKSAGND
     SIQSTKPVPS ALTVDKATSV RGSLSITPNN SSKVADSLPD RSFKPSDRSG STTNNLATSL
     KKMVRQQTAP KVVRHYPSES TLFPYELFVK LYSKVELHPF GLHNLGNSCY ANAVFQCLMF
     TRPLTTYLLE GLHSKNCSQN GWCFMCEFEK LIVEGKRRKI ALSPTGILSH LNDIGSSFGP
     GKQEDAHEFL RYAIDAMQSV CMKEARKGGV LQSAEETTLV QLIFGGYLRS KIKCSRCHVS
     SEQCEPMLDL TVEIDGDISS LGEALVRFTS TEVLDGENKY HCSRFCYGS
//