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Database: UniProt
Entry: S9WCE6_CAMFR
LinkDB: S9WCE6_CAMFR
Original site: S9WCE6_CAMFR 
ID   S9WCE6_CAMFR            Unreviewed;       438 AA.
AC   S9WCE6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   ORFNames=CB1_002748002 {ECO:0000313|EMBL:EPY73594.1};
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:EPY73594.1, ECO:0000313|Proteomes:UP000030684};
RN   [1] {ECO:0000313|EMBL:EPY73594.1, 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   -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC       from specific proteins to regulate different cellular processes.
CC       {ECO:0000256|RuleBase:RU366025}.
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|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025}.
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DR   EMBL; KB018573; EPY73594.1; -; Genomic_DNA.
DR   RefSeq; XP_006194308.1; XM_006194246.2.
DR   AlphaFoldDB; S9WCE6; -.
DR   Proteomes; UP000030684; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02660; Peptidase_C19D; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
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:SF30; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 27; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU366025};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030684};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW   ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          78..421
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   438 AA;  49619 MW;  BDD57557505169DB CRC64;
     MCKDYVYDKD IEQIAKEEQG EALKLQASTS TEVSHQQCSV PGLGEKYPTW ETTKPELELL
     GHNPRRRRIT SSFTIGLRGL INLGNTCFMN CIVQALTHTP ILRDFFLSDR HRCEMPSPEL
     CLVCEMSSLF RELYSGNPSP HVPYKLLHLV WIHARHLAGY RQQDAHEFLI AALDVLHRHC
     KGDDAGKAAN NPNHCNCIID QIFTGGLQSD VTCQACHGVS TTIDPCWDIS LDLPGSCTSF
     WPMSPGRESS VNGESHIPGI TTLTDCLRRF TRPEHLGSSA KIKCGSCQSY QESTKQLTMN
     KLPVVACFHF KRFEHSAKQR RKITTYISFP LELDMTPFMA SSKESRMNGQ LQLPTNSGND
     ENKYSLFAVV NHQGTLESGH YTSFIRHHKD QWFKCDDAVI TKASIKDVLD SEGYLLFYHK
     QVLEHESEKV KEMNTQAY
//
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