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Database: UniProt
Entry: A0A0L0G8S3_9EUKA
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Original site: A0A0L0G8S3_9EUKA 
ID   A0A0L0G8S3_9EUKA        Unreviewed;      1118 AA.
AC   A0A0L0G8S3;
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=SARC_02497 {ECO:0000313|EMBL:KNC85314.1};
OS   Sphaeroforma arctica JP610.
OC   Eukaryota; Ichthyosporea; Ichthyophonida; Sphaeroforma.
OX   NCBI_TaxID=667725 {ECO:0000313|EMBL:KNC85314.1, ECO:0000313|Proteomes:UP000054560};
RN   [1] {ECO:0000313|EMBL:KNC85314.1, ECO:0000313|Proteomes:UP000054560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP610 {ECO:0000313|EMBL:KNC85314.1,
RC   ECO:0000313|Proteomes:UP000054560};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Young S.K., Zeng Q., Gargeya S., Alvarado L., Berlin A.,
RA   Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Howarth C., Mehta T., Neiman D.,
RA   Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., White J., Yandava C., Burger G., Gray M.W., Holland P.W.H.,
RA   King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Sphaeroforma arctica JP610.";
RL   Submitted (FEB-2011) 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; KQ241709; KNC85314.1; -; Genomic_DNA.
DR   RefSeq; XP_014159216.1; XM_014303741.1.
DR   AlphaFoldDB; A0A0L0G8S3; -.
DR   STRING; 667725.A0A0L0G8S3; -.
DR   EnsemblProtists; KNC85314; KNC85314; SARC_02497.
DR   GeneID; 25903001; -.
DR   eggNOG; KOG1863; Eukaryota.
DR   OrthoDB; 51419at2759; -.
DR   Proteomes; UP000054560; 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   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   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:UP000054560};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          56..190
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          215..528
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1118 AA;  127904 MW;  86E0D377B735FF86 CRC64;
     MTFPQVTQQV EMDVEVGQDS DEYLPDASDG TSSAKDDPLS IADRPTLLLP EDIVEEHCFT
     FEVDGLFDNP DPNCKIKSRV PEVFSGCEWR FLIFPRGNNN NYEHQSISVF LECAYIDANE
     GAEWKKSVFF TLALLSVYPE KSHMKDSHHV FQSRDKESDW GFSSFTTISE VQDANNGFSV
     NNKYTFEARV VIAKGISSIW STLPGYDSKM ATGCVGLKNQ GATCYMNSML QALFFTNKLR
     KAVYSLPSNE TDTSVSLALQ RVFFDLQTLD EPVGTTQLTR SFGWNTADAF MQHDVQEFNR
     VLCDNMESKM KGTDAEGTIA SLFEGRMKSY VKCINVDYES SRSESFYDIQ LVVKDKQSLY
     DSFDEYVVEE TLDGDNKYLA EGHGLQDAKK GCIFEKLPPV LHLQLRRFEY DIDADAMVKI
     NDRHEFDERI NLDKYLHNPG SEPADYTLYS VLVHSGDIHS GHYVAYIKPK IDGSWCKFDD
     DKVTNVSTEE ALDGNFGVDK VNGQIRMGSK GDKTKKFTNA YMLVYIRDSC VNEVMVPVED
     DDMRNTLREQ LLNERQKDHR KIVDAAEAHK YMMFQIIQDK EIAENHGFHL FSSDTAWTEM
     KVHKLSTVDD FLAQAGEVFG LEPHQMRFWK FVHRQNGTMR PHAEVLGLEG QGHRRITELE
     NWNALKGSNE KLYMETPREG ETALPQVFIH EKRDDRTRHN DDVMIYLKDY DAVKGQLTYI
     GSCVFPKDEL MAAAEPVMRQ WAGIPDGVPL VVYEEIKPLR IDMVNTERTF RQGELASGDI
     LTFQVQTRAD KHCKWPTVKD YYEYLAHRIT ITFNCIDESR NEPSIELELR TDMKHDEVAQ
     MLGSLLPLDD GDQVDPATLR FHLPDGEKSS RPVFRGNGEI MLETMIDSMT IDPANANTLL
     YEYLDVNIVE LESKVPLSIW WRSASGEETE QRLLLEHGTT VSNVLEDQRH NPMIKLAPGG
     SGKLRLLEIY DHRILRVYQE NEACEKIRQD DRRARLEEVP LDQLNADNFL NVVHFHREAK
     KLHGSPFLLA VHEREIVKDL KKRLQAASTA TPCEFEKWKV AILDAEGYNS KPKYLKDEDS
     VQELLSNELY PRIGLDHPGR PSNYRSNDAQ AGAVVIRN
//
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