ID A0A162YD49_PHYB8 Unreviewed; 1115 AA.
AC A0A162YD49;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, 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=PHYBLDRAFT_130323 {ECO:0000313|EMBL:OAD79955.1};
OS Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS 33097 / NRRL 1555).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD79955.1, ECO:0000313|Proteomes:UP000077315};
RN [1] {ECO:0000313|Proteomes:UP000077315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-2015) 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; KV440972; OAD79955.1; -; Genomic_DNA.
DR RefSeq; XP_018297995.1; XM_018429350.1.
DR AlphaFoldDB; A0A162YD49; -.
DR STRING; 763407.A0A162YD49; -.
DR GeneID; 28990256; -.
DR VEuPathDB; FungiDB:PHYBL_130323; -.
DR InParanoid; A0A162YD49; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000077315; 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; 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 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:UP000077315};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 55..183
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 209..527
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1115 AA; 128494 MW; 5DA6E4F983087FA6 CRC64;
MDNQQNPMNE LLPPYDMDRP MPDADQAPSE ISVLDHYEII ARNEMNPVEE EIIELQCQHW
DINNWSSLED RVHGPTFEAG GHQWNVLLFP KGNNQNEFAS LYVEMTDAKT VPDNYCCAQF
VVCLTKPSDP FQYIHHAAQH RFNSEESDWG FTRFIELKQL YSLDEQGNPR FLEDDNVRIT
TILRVIKDPT GVLWHNFNNY DSKKMTGYVG LKNQGATCYM NSLFQSLYCT NLFRKAVYQI
PTENDEPTKS VALALQRVFY NLQFSDVPVG TTEMTKSFGW DSLEAFMQHD VQEFNRVLQD
NLEAKMKNTP ADGAIKRLFV GTMKSYIKCI NVSYESSRTE DFYDIQLNVK GCKNLEESFK
DYIAEEVLEG DNKYMAEGHG LQDAKKGVIF ESFPPVLHLQ LKRFEYDIMR DTMVKINDRH
EFPLEIDLEP YLDPVADRSQ PHKYVLHGVL VHSGDLSGGH YFAFVKPTKD GNWLKFDDDR
VVPTTLKEVL EENFGGDHVS GAMTNGRPSF RGFKRFTNAY MLVYVRESMI DEILANVVEK
DIPSHLSQRL EQERQLQERK AKEKEQQHFY MKAYLVTDNT FMANDGFDFV NLEERSMETS
QLEVRRVLKD QKYGDFKREL SHSMGLPETH IRLWFLVNRQ NRTIRPDAPV PEGEEDCTLE
EIRQKHLANQ PNLRLYVEKS LSPDNERALF PPAPSNTSAN ALIFIKLFDP ELQKIRGIGR
LYINKADKVG SIMEQVNEIA GYEFGTPLVF YEEIKTTMIE EMDLNLTFTK AEIQDGDIIA
VQRNLSDAEI EQLKEAGMYD NVPDFMDYQL HKLDVVFSPK DGNPETEFEL SLHKNMRYDE
VAAKVGAKIG ADPEKIRFLA CGPSGDLKPI RRTPTSLLAD MQNMTYNQNV ARFKLTYEVL
DISLTEFESK RMVKITLCTP TLRDINVVEL LLPKQGKIAD LLKALDAKGA KFESAKGTRR
TRIFEALGNK FNREFLPTDS ISQLSASNYA QLYAEEIPEE EMLMGDDDIF IRVFHFQRDI
SRAHSVPFKF LVKKDEPFEE TKKRLQARTG LNDKDWSKVK FNIVSSYSAV PIEEGDDFKL
SNHLFTQEES LGLEHMDKTP RSARMGAERA LSIRG
//
