ID A0A0L0DV25_THETB Unreviewed; 861 AA.
AC A0A0L0DV25;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=AMSG_02059 {ECO:0000313|EMBL:KNC56047.1};
OS Thecamonas trahens ATCC 50062.
OC Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC56047.1, ECO:0000313|Proteomes:UP000054408};
RN [1] {ECO:0000313|EMBL:KNC56047.1, ECO:0000313|Proteomes:UP000054408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC56047.1,
RC ECO:0000313|Proteomes:UP000054408};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL349440; KNC56047.1; -; Genomic_DNA.
DR RefSeq; XP_013761091.1; XM_013905637.1.
DR AlphaFoldDB; A0A0L0DV25; -.
DR STRING; 461836.A0A0L0DV25; -.
DR EnsemblProtists; KNC56047; KNC56047; AMSG_02059.
DR GeneID; 25561770; -.
DR eggNOG; KOG1870; Eukaryota.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000054408; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 6.10.140.2220; -; 1.
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; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:KNC56047.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000054408};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 211..860
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 501..538
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
SQ SEQUENCE 861 AA; 92584 MW; 74D2002A200649E3 CRC64;
MLGAPADEAV DDGVPGVAET VPVIDEVTTA MTAGSGFVAM RKDVREKVDF EVIPEAAWRM
LQEAHGDGSG PELCRKVVAR GSGNLGVELH PLVLHLISYT SRNGFGPRTL VVRPRECAMA
DLVGDVRAVF GWSSETPLAM WRSDEAAPTS ETAMQRAEYT RVALKAATLD DAELLDGALV
VVVSGPLAES GQPPWRAAGT GATVEGRAGL AGLRNLGNTC FMNATLQALS NTPQLVAYFA
SGAFVRDVNV ENKLGTGGAL AAAWADLVRE LWLGPKASVA PSKFKRVLGQ LAPQFSDFKQ
QDAHELFSFV LDGLHEDVNL VTDKPVTEKL ELEDGQDEAW LAGESWATHL QRNKSAVVDL
FHFQLKSTVV CPQCERVSVT FDPACALSVP LPSSGKARIG LTMVFASATS PPLKACLELD
AECNVGHLRH QLACLTGVPS GQIVIGAVDD SRLGSTFGNK KALSKVPRAG GDGPSVVAWE
LAPGSSRALY VLFRRRDTRV CGGCSAPATR LRCKQCKVQY YCSREHQVAD WKYHKKRCGV
ASTPPRARMV IFGTPLVIGH DLAAPQLTGR ALYATIEAAI AGRVSKAWAN GPSSPPPYLL
RLCDADGISC AVCEPEARCR GCAVAWDADE PVAVPKRARV VVDFGGDDGG SSVLLGAAAP
AVEIDESAAR GTGITLGECV AQFEASEVLD EHNEWYCSVC AQHQQATLQM KMWSAPRVLV
VHLKRFRRRG WTGFFGTKVT DAVDFDETLD LRPFVAGDVD PGTGEPFPAS MPYVLYAVVN
HMGNMYSGHY TAYARSPRAN LSQVLAERDA DATAARIGEV ASDPCHEQWW LYNDSTVSRV
SAARVLSDRS HAYMLFYMRA W
//
