ID D7KD54_ARALL Unreviewed; 507 AA.
AC D7KD54;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 08-NOV-2023, entry version 55.
DE SubName: Full=Mov34 family protein {ECO:0000313|EMBL:EFH70392.1};
GN ORFNames=ARALYDRAFT_474017 {ECO:0000313|EMBL:EFH70392.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M67C family.
CC {ECO:0000256|ARBA:ARBA00010981}.
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DR EMBL; GL348713; EFH70392.1; -; Genomic_DNA.
DR RefSeq; XP_002894133.1; XM_002894087.1.
DR AlphaFoldDB; D7KD54; -.
DR STRING; 81972.D7KD54; -.
DR MEROPS; M67.A04; -.
DR EnsemblPlants; fgenesh2_kg.1__3971__AT1G48790.1; fgenesh2_kg.1__3971__AT1G48790.1; fgenesh2_kg.1__3971__AT1G48790.1.
DR GeneID; 9327516; -.
DR Gramene; fgenesh2_kg.1__3971__AT1G48790.1; fgenesh2_kg.1__3971__AT1G48790.1; fgenesh2_kg.1__3971__AT1G48790.1.
DR KEGG; aly:9327516; -.
DR eggNOG; KOG2880; Eukaryota.
DR HOGENOM; CLU_023304_5_1_1; -.
DR OrthoDB; 463685at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0061578; F:K63-linked deubiquitinase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR CDD; cd08066; MPN_AMSH_like; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR044098; STAMBP/STALP-like_MPN.
DR InterPro; IPR015063; USP8_dimer.
DR PANTHER; PTHR12947; AMSH-LIKE PROTEASE; 1.
DR PANTHER; PTHR12947:SF19; AMSH-LIKE UBIQUITIN THIOESTERASE 1; 1.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR SUPFAM; SSF102712; JAB1/MPN domain; 1.
DR PROSITE; PS50249; MPN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 333..463
FT /note="MPN"
FT /evidence="ECO:0000259|PROSITE:PS50249"
SQ SEQUENCE 507 AA; 57313 MW; DD1D3087ADD7C6BA CRC64;
MGSSSEIIDI ATSARRIGVD NRISLKFYFR IADNILKQAD IFRAEKNVID LYVMLLRFSS
LALETIPSHR DYRTSLKSNK EYLRMRLLDV LTELEKLKPV VQKRIDELYP KLKPRYNVQA
HPSNGSLGWS SAVKPSLNSY DPAKVRNPPG HNFGYMGSRG QQFLNAAPLE ERFRKMSVNF
RPNEETLSKH SILGPGGLSA QWQPPKYDTK VQYPSNIDFS PVVIPSFQQF VDSKPMITNG
SNDEPERPIV EPSVASSENI QKNYTEELSS MISFEEPESV NDNNLIRQPS PPPVLAEVQD
LVPALCPEVR EPECIIENSL PDESLRSESP LELHIATTMM DTFMRLAKSN TKKNLETCGI
LAGSLKNRKF YITALIIPKQ ESTSDSCQAT NEEEIFEVQD KQSLFPLGWI HTHPTQSCFM
SSIDVHTHYS YQIMLPEAVA IVMAPQDSSR NHGIFRLTTP GGMTVIRNCD QRGFHAHSSP
EDGGPIYNTC KEVYMNPNLK FDVIDLR
//