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
//