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Database: UniProt
Entry: A0A2G9HNY7_9LAMI
LinkDB: A0A2G9HNY7_9LAMI
Original site: A0A2G9HNY7_9LAMI 
ID   A0A2G9HNY7_9LAMI        Unreviewed;       510 AA.
AC   A0A2G9HNY7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   08-NOV-2023, entry version 22.
DE   SubName: Full=SMAD6 interacting protein AMSH, contains JAB/MPN/Mov34 domain {ECO:0000313|EMBL:PIN19234.1};
DE            EC=3.4.19.12 {ECO:0000313|EMBL:PIN19234.1};
GN   ORFNames=CDL12_08087 {ECO:0000313|EMBL:PIN19234.1};
OS   Handroanthus impetiginosus.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC   Handroanthus.
OX   NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN19234.1, ECO:0000313|Proteomes:UP000231279};
RN   [1] {ECO:0000313|Proteomes:UP000231279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX   PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA   Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT   "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT   Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT   forest tree.";
RL   Gigascience 7:1-16(2018).
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:PIN19234.1}.
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DR   EMBL; NKXS01001312; PIN19234.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G9HNY7; -.
DR   STRING; 429701.A0A2G9HNY7; -.
DR   OrthoDB; 463685at2759; -.
DR   Proteomes; UP000231279; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
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:SF18; AMSH-LIKE UBIQUITIN THIOESTERASE 3; 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   Hydrolase {ECO:0000313|EMBL:PIN19234.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          336..466
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
FT   REGION          308..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   510 AA;  57603 MW;  6346ECB18AC0DD0D CRC64;
     MRRPAYSSPS INFSAVTRKI EVDNRISLRN YYRIADNLLK QANIYREEKN LIDLYVILLR
     YSSLVSETIP YHQDYQTLCP KERTFYKKKL PSVLDELETL KPQVRRQLDE QEKVNTATQV
     RQFDGPNKFA SSVNNKASLS YSNKQMLQPS TAPSSSLKQN NEFNRFSSSN SIDSQFQKLS
     LSLPLPKQET LSRHSFLGPN GLRGQWLAPS AEIKVSYPTN IVMDTSEFSS LNQVGQQEPM
     AIQDCETKVE KSSMESVLSL DDGRWLAEES GLPQGNEIEN NAFQLSNIRQ PSPPPVLAQV
     QPELLPISPS RVADPRPGPP KLSPDALSSS NSYQDLHIPV RILEDFLRVA RENTTKNLET
     CGVLAGSLRN RVFHITTLII PKQESTSDSC QTLNEEEIFD VQDKRSLFPL GWIHTHPTQT
     CFMSSVDLHT HYSYQVMLPE AIAIVMAPTD TSSPHGIFHL SDPGGVSVIR NCQQRGFHPH
     EEPEGGSPIY EHCSHVYMNS NLKFDVVDLR
//
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