ID D8PX32_SCHCM Unreviewed; 1105 AA.
AC D8PX32;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=SCHCODRAFT_81397 {ECO:0000313|EMBL:EFJ00325.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFJ00325.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
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; GL377303; EFJ00325.1; -; Genomic_DNA.
DR RefSeq; XP_003035227.1; XM_003035181.1.
DR AlphaFoldDB; D8PX32; -.
DR STRING; 578458.D8PX32; -.
DR MEROPS; C19.A59; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02605902; -.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_003532_2_1_1; -.
DR InParanoid; D8PX32; -.
DR OMA; HTAHHRF; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000007431; 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:UP000007431};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 44..176
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 202..521
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1105 AA; 127389 MW; 308434387E7AE07F CRC64;
MDVLDEKTNG APPMDVDNDI VSVRDEVAFA AKHLPDLGQD VKDFKAYHWP LKNWKKLDKK
ITSEEFECGG HSWRILLFPF GNSNAPPNDT VSVYLDYAEP KKAPEGWHAC AQFALVISNI
HDPTIYTVSH AHHRFIAEEC DWGFTRFSEL RKLFNVQEGH SRPIIEEESA MVSVFVRVLE
DPTGVLWHNF VNYDSKKETG FVGLKNQGAT CYMNSLLQSL YCTNYFRKAV YQIPTEEDHP
TESVALALQR VFYHLQTSDQ PVGTTELTKS FGWKSLDSFL QHDVQEFNRV LQDKLESKMK
GTKAEGAIAK LFTGKMKSFI KCVNVDYESS RTEDFNDLQL NVKGMKNLYE SFKDYIQVET
LDGENKYQAE GYGLQDAKKG ITFLSFPPVL HLQLKRFEYD IQRDAMVKIN DRHEFPFEID
LAPFLDESAD KSQSWVYSLC GVLVHSGDLH GGHYFALIKP DKHTRWLKFD DDRVTPVTDK
EVLEENYGGE VMNGTTPAMQ RNQVRTMKRF TNAYMLVYIR QAVVDEILAP FTEEDTPAHL
KRRLDEERMQ IEAKKREREE QHLYLTAKVI TDDTFAKHEG FDLATFDDKN WPPSDLPTFR
VLKQETYATF KERVAKHFGY PVDRIRLWVL VNRQNKTVRP DAIIPDNEPA WTVEIIRNQL
AARTTDLRLY LDVLPDPPKP EPAPQTTIMI FLKHFDTSRQ TLYGAGKAHM LRTAKVADLV
PIINERMRWQ PGTPLKLYEE IKPGMIELMK PRSTFTQSEI QDGDVICFQV DIPDNDRIRD
LESQGLYSNP MQYYDFLQNR VMIIFRPKYE EPDHDHPEFH LVFSKKQNYD VMSQKVGEHL
RHDPIKLRFT TTHPSNGSPK AILKRSLNQS ISEIMQPSYV SSTTTVILYE KLDVSIVELE
TKRSLKIIWT GIHNKEEASF PFLLPKTSAV HELAEHLAKQ VTLTPTGTGK IRIFEISKDY
KTQREFTGSE MIGNIPDPVE LYAEEIPRDE LEASEDDKVI GVFHFSKDLS RTHGVPFRFV
VKRGEKFADT KKRLQARIGV PDKEFAKYRF ALIQASTFKQ PSYIEDDDTI YDHQFAPEDV
LGLDHVDKTG RARAGMAEKA IVIKG
//
