ID A0A0L0DGS0_THETB Unreviewed; 1088 AA.
AC A0A0L0DGS0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=AMSG_07438 {ECO:0000313|EMBL:KNC51539.1};
OS Thecamonas trahens ATCC 50062.
OC Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC51539.1, ECO:0000313|Proteomes:UP000054408};
RN [1] {ECO:0000313|EMBL:KNC51539.1, ECO:0000313|Proteomes:UP000054408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC51539.1,
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 -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; GL349468; KNC51539.1; -; Genomic_DNA.
DR RefSeq; XP_013755941.1; XM_013900487.1.
DR AlphaFoldDB; A0A0L0DGS0; -.
DR STRING; 461836.A0A0L0DGS0; -.
DR EnsemblProtists; KNC51539; KNC51539; AMSG_07438.
DR GeneID; 25566355; -.
DR eggNOG; KOG1863; Eukaryota.
DR OMA; HTAHHRF; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000054408; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00121; MATH; 1.
DR CDD; cd02659; peptidase_C19C; 1.
DR CDD; cd17039; Ubl_ubiquitin_like; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 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|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054408};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 35..160
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 184..501
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1088 AA; 124130 MW; 2BB0152BDB4F85C3 CRC64;
MSDPETDIPI SNDAADGALA EAETESDSAD SDDKTFITHW EIENFSQVTD KKIWSEAFEA
EGRQWRVLCF PKGNEAGHFS LFLECVQDDS VDATWRAQTE FRLQLVNQKN AEDSHFRAAT
HLFVKTSTDW GFSKFMTLDK VLDPDAGFLV DDKLVVECTL EVLEQPFTAY NWWNYDSRKE
TGFVGILNQG ATCYMNSLLQ TLYHTKYFRK CVYQLPTEED KVGASIPLAL QRLFYNMQFA
ESAVSTKELT KSFGWDAMES FYQHDVQELN RVLCDNLETK MKGTEVEGAI GKLFEGKLFN
YIKCLNVDYS STRTESFFDV SLDVKGNKNV YDAFEDYVAE DTLDGENQYS TEDYGKQDAV
KGIRFEVLPP VLQLHLKRFQ YDYQTGAFNK INDRFEFPTV LELDKYLSES ADKSVPQVYD
LFGVLIHSGG VQGGHYYAFV RPSDEPQWLR FDDDKVIKVK DKQALNENFG WTPSAGGNDG
FRSIRMARRY TNAYMLIYVR RADSHWVNEE LTDDVIPEHL RERIERENAE RAEQEKARRE
AHLYVNIRII RDKDLEGHRD VDLVNVTNVE PIKVKKDSTL EGLKKEVEKK WGIPAASQRY
WYWLNRKNKT SRPSRIVPDD KYSARITSLF KSLTACKLFL EVLPESGSFE EITPTKANLF
FKYYDPVAHE LMYVGRKVVE KTTSIAELLP VMREMAGLEA DVPLVVYEEI KTADPIMIDE
VNLSHDLNAA ELGNGDILCF QKAPGGEETG GDVAHPTVPD YFTYIVNRLL IKFVPLEKAA
AKDKSAVTTT LDLTQEDSYS MVVEALGAAT GYSADHIRLT GFNAYTKGPK RQPLRRTPVS
GTELTLFRML YTHYKPLADT LYYEVLDRPL VEIETKRKLS LHLHSLTGER ESTLDLYVEH
AATVADVLNE LRDTLAARAD ADVPAGFDGP LRMLEVSRLA KIVRLFDEGD PVHLIPHYAI
VRVEPVPADE IDVPAGSKAM FFNHFVKSIH HTFGTPFMMY LRPGEPVADL KARVKARFAI
PDEDFAAWKF YLVSFSSPKT LDDAYILNRH KFFNSDYIGI RHANKKVEDI RATPTSTRSS
GHSIKIYN
//
