ID   H3B1T2_LATCH            Unreviewed;       643 AA.
AC   H3B1T2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000015853.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000015853.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
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DR   EMBL; AFYH01083495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01083496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7897.ENSLACP00000015853; -.
DR   Ensembl; ENSLACT00000015963.1; ENSLACP00000015853.1; ENSLACG00000013960.1.
DR   eggNOG; KOG1870; Eukaryota.
DR   GeneTree; ENSGT00940000157311; -.
DR   HOGENOM; CLU_004896_0_0_1; -.
DR   InParanoid; H3B1T2; -.
DR   TreeFam; TF352179; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 1.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF86; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF06337; DUSP; 2.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 2.
DR   PROSITE; PS51283; DUSP; 2.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT   DOMAIN          164..643
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   DOMAIN          437..534
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          543..643
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   REGION          280..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..360
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..399
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   643 AA;  72562 MW;  C37220F75BA3A3BA CRC64;
     NIHILTIKKV LKDFNTFQES PTIQMPIVSS VCLHIEAGRE IKMEEPVQIP EASGPISTDK
     GTNLQACVEK KCCYVGCGDS HEDPCAFHLE DTRQSLSTNP TTQQNSYNTQ NSLKLLKSQE
     MLGPLTKDLH IYGRSTLKIP KFSFLEPCTD MEDDDGKKEV KGQTGLMNIG NTCYMNSALQ
     ALANCPPLRE YFFFGSLVQA GKKPSISELY QKLLFNIWHK RKSGYIVPIT MVQGIQTMNP
     IFHKYNQHDV QEFLRFLISQ LHEELKETIL EIEEPLSITM DESNSHQKDS DFNISESCSN
     SNKDESDKVP FKGGHTDDDP LLLVKEGNNQ SLPTDGQEEK DLLNKHHNAC AMEDLDKDNA
     NFSRSNSAEL HKQEAPNEDF DSNLTSSPPK FSTVGSTIKR SAPLSSPKKK LEKIYRSIIS
     DTFDGTILSS VQCLACDSLS QRTENFQDLS LPIPKRKNLA KXEVYISKQW LSKFQTFAEP
     GPISNTDFLC VHGGIPPYKV NKIEGPVVSV PRDTWKHLQR TYSGGPELNH VHVCEVCHTE
     LGDLQNQRKL ELETFIRLNN EFLEQELPEV RHCINMQWMG QWEGFAKAKD NDPSGPINNY
     KLTEKKGGSF SLIKGPDLGY ISKETWKYFH SIYGGGPQVT FCP
//