ID A0A2P5APD5_PARAD Unreviewed; 507 AA.
AC A0A2P5APD5;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 08-NOV-2023, entry version 19.
DE SubName: Full=JAB1/MPN/MOV34 metalloenzyme domain containing protein {ECO:0000313|EMBL:PON38377.1};
GN ORFNames=PanWU01x14_313140 {ECO:0000313|EMBL:PON38377.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON38377.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:PON38377.1}.
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DR EMBL; JXTB01000497; PON38377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5APD5; -.
DR STRING; 3476.A0A2P5APD5; -.
DR OrthoDB; 463685at2759; -.
DR Proteomes; UP000237105; 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:UP000237105};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 333..463
FT /note="MPN"
FT /evidence="ECO:0000259|PROSITE:PS50249"
FT REGION 176..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 57697 MW; 8FA7A584C36FF561 CRC64;
MKPSSEVINI AASAQKLDVD NRISLRYYYR IADNILRQAN IFREEKNIID LYVMLLRFSS
LVSETIPRHR EYRASAKSKK DNLRKGLLNA LSELEKLKPE VQQKINELNR KYAYQTNGWT
HHSQKDSLEW PSVKKQTSTA HDVTKIGRST VCEPIYRNPR AQQFSHASSL EERFKKLSLR
PRPTDETLSR HSILGPNGLN GQWQPPISDK GIRYPSITDL SPLEILSQQP VEEEPTANKD
RDRPEHERLP VESTHTQSSD DNQTSRTEDS LISFETIEAP AHVEIIRQPS PPPVLAEVQD
LVPAVSPQVS ELECGLDTLV TDELVRAETP LQLHISTTMM ENFMKLAKSN TDKQLETCGV
LAGSLKNRKF YITALIIPKQ ESTSDSCQTT NEEEIFEVQD KRSLFPLGWI HTHPTQSCFM
SSIDLHTHYS YQIMLPESVA IVMAPRDTTK NHGIFRLTTP GGMSVIRHCQ QRGFHPHNPP
ADGGPLYKTC TDVYMNPNIN FDVIDLR
//
