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}.
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; 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
//