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Database: UniProt
Entry: A0A200PZL7_9MAGN
LinkDB: A0A200PZL7_9MAGN
Original site: A0A200PZL7_9MAGN 
ID   A0A200PZL7_9MAGN        Unreviewed;       849 AA.
AC   A0A200PZL7;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   08-NOV-2023, entry version 25.
DE   SubName: Full=Ubiquitin carboxyl-terminal hydrolases family 2 {ECO:0000313|EMBL:OVA03663.1};
GN   ORFNames=BVC80_1097g1 {ECO:0000313|EMBL:OVA03663.1};
OS   Macleaya cordata.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Macleaya.
OX   NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA03663.1, ECO:0000313|Proteomes:UP000195402};
RN   [1] {ECO:0000313|EMBL:OVA03663.1, ECO:0000313|Proteomes:UP000195402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC   TISSUE=Root {ECO:0000313|EMBL:OVA03663.1};
RX   PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA   Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA   Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA   Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA   Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT   "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT   Benzylisoquinoline Alkaloids Metabolism.";
RL   Mol. Plant 10:975-989(2017).
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:OVA03663.1}.
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DR   EMBL; MVGT01003607; OVA03663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A200PZL7; -.
DR   STRING; 56857.A0A200PZL7; -.
DR   InParanoid; A0A200PZL7; -.
DR   OrthoDB; 227085at2759; -.
DR   Proteomes; UP000195402; Unassembled WGS sequence.
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:SF677; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 18; 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   Hydrolase {ECO:0000313|EMBL:OVA03663.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195402};
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        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          76..113
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   DOMAIN          171..477
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          562..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   849 AA;  94245 MW;  7CF3A7220606467F CRC64;
     MHISGLPLDL YSFLQFLFTA FLFCIGLLYL VKNTASKYFF VDATFDEGGG GVVLTGEERR
     RSREDMLSVA GVDDCCASCG DSATKKCSGC KAVRYCSQIC QSKHWKGGHN LECKEFKRGN
     LNSTSIFSQR GRNFGCGGTS STVRQLSKKI IFPYEEFVKL FIWDKPGFPP CGLLNCGNSC
     FANVVLQCLS CTRPLVAYLL EKGHREECRR NDWCFLCELQ IHVERAIQSS HPFSPINILS
     RLPNIGGNLG YGKQEDAHEF MRFAIDTMQS VCLDEFGGEK ALHPSSLETT LIQHIFGGHL
     QSQVTCTECN KISNRYENMM DLTVEIQGDA ASLEDCLDQF TVKEWLDGDN MYKCDGCNDY
     VKAWKRLTVC QAPNVLTIAL KRFQSGRFGK LNKRVTFPET LDLGPYMSEA GEGTDLYRLY
     AVVVHVDMLN ASFFGHYICY TKDFDGNWYR IDDCKVTSVE LDEVLAQGAY MLLYSRNTVR
     SHCVKPLKPS TEEYRQPVEV AEEAQECLPK PVVSFDIAES MDLVETSTST AYDISQHAEE
     SGSKNDSLDN MDLEDPFKVN LRPPREIPQD MDTSNNSHDC DNEHSCTAEI ISASSSKGTL
     PIELEFPETN SDAECSSRVG NGEMNGCNTE YMSSKSSVDS YLSGQNGIYE MAETSAIPVV
     ELTSTRETVG GENSASFPRL LNSRLENLVA VKSGMGSISA QGIEVKTTKS TGDKNTCSGE
     KPKPLFSRGF LDKSTRYRSL NGNGKAQMES SEAGPSYKVN SNCNGFVRKP DFLHQNSSEY
     NDHDRLDCDS LLKSSFIEKK SEKFLGEDEV ANGGCNSSES SHGAELGFHA ELVHREVPIS
     ASLEETPIN
//
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