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Database: UniProt
Entry: S9XJN6_CAMFR
LinkDB: S9XJN6_CAMFR
Original site: S9XJN6_CAMFR 
ID   S9XJN6_CAMFR            Unreviewed;       261 AA.
AC   S9XJN6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=CB1_001675001 {ECO:0000313|EMBL:EPY75381.1};
OS   Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX   NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY75381.1, ECO:0000313|Proteomes:UP000030684};
RN   [1] {ECO:0000313|EMBL:EPY75381.1, ECO:0000313|Proteomes:UP000030684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX   PubMed=23149746;
RG   Bactrian Camels Genome Sequencing and Analysis Consortium;
RA   Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA   Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA   Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA   Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA   Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA   Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA   Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA   Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA   Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA   Bayaer T., Li Y., Meng H.;
RT   "Genome sequences of wild and domestic bactrian camels.";
RL   Nat. Commun. 3:1202-1202(2012).
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};
CC   -!- SIMILARITY: Belongs to the peptidase C64 family.
CC       {ECO:0000256|ARBA:ARBA00005865}.
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DR   EMBL; KB017809; EPY75381.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9XJN6; -.
DR   Proteomes; UP000030684; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR003323; OTU_dom.
DR   PANTHER; PTHR13367:SF9; OTU DOMAIN-CONTAINING PROTEIN 7A; 1.
DR   PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR   Pfam; PF02338; OTU; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030684};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          141..207
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|Pfam:PF02338"
FT   REGION          50..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   261 AA;  29414 MW;  4583BFB623EC2686 CRC64;
     MMRTGAEREA LKRRWRWQQT QQNKESGLVY TEEEWEREWT ELLKLASSEP RTHFSKNGGT
     GGGEGTEFAG QIDCSPQDGP LAHSNRLSPE TTLPRVGLES WGRCVCHRWV VWREAASDAS
     DGRDGWGPGS VDNSEDPVYE SLEEFHVFVL AHILRRPIVV VADTMLRDSG GEAFAPIPFG
     GIYLPLEVPP NRCHCSPLVL AYDQAHFSAL VSMEQRDQQR EQAVIPLTDS EHKLLPLHFA
     VDPGKAWEWG RDDNDNARLA Q
//
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