ID A0A2G4STL3_RHIZD Unreviewed; 827 AA.
AC A0A2G4STL3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=RHIMIDRAFT_251906 {ECO:0000313|EMBL:PHZ12113.1};
OS Rhizopus microsporus ATCC 52813.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ12113.1, ECO:0000313|Proteomes:UP000242254};
RN [1] {ECO:0000313|EMBL:PHZ12113.1, ECO:0000313|Proteomes:UP000242254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ12113.1,
RC ECO:0000313|Proteomes:UP000242254};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KZ303850; PHZ12113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G4STL3; -.
DR STRING; 1340429.A0A2G4STL3; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000242254; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 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|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000242254};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 27..126
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 243..820
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 827 AA; 97381 MW; 35FD8108D19B0D94 CRC64;
MTNEKRKRLI DSMKTRDEHY KKQKYELSKE DQFNYIKEIK NSTRLEQEEK WFLISTKWYN
DFKAYCRGDV DRLSTIDNSS LFDKDYKVKG NLICGKDYIL LPKRAWESLM EWYGINDERF
IVKRSVKSLY HFEVYQMHQK PSQRKTFNID CGATVKDFYQ ALVSALNLSA SISRVWILKR
PIESNTFITE SLLDTLAAKT IHPSTIPTHV LITTYLPNKD EKRYSLAIKT ESTTVSTVTR
GLRGLNNLGN TCYMNSAIQC LSNTPKLTYW LLKDLYKKDI NRYNPLGLRG ELAESYASLI
KSIWRIGHSS SISPYEFKKT FERFNSHFSG YEQQDSQEFL GFLLDGLHED MNRVHHKPYV
QMHDYEDESR QEEIADQLWK YHKSRNNSVI VDLFQGQFKN KLRCNECNKV SITFDPFMHL
SLPIPVSICK LNITFIYYHK PRQCKFTVSL TKQSRTIADL KQAIMNKLKD SKHFLITRMF
QSKICTLYKD SDPLSAIQPT DIIYIYEIPF AYPDPSWILF PVYFQLIDND NTHFNMFGYP
SILAFDTSKG YPDLYTSISL RVQRYTAKTL INEDGMPIEQ DMFTIKTFIN KESADTHFPL
LEPPTDVSFM PDEHDPNTIQ QGQAVLTQWK KEKAFGIFGS APKRNNPDVL TINTGLWRAF
DNLANGNQQD RPDIYACLRE FTKEEHLTDD DLWYCPRCKK QQRATKKLDL WRLPEIMVIH
LKRFSQVRMW RNKLNTFVDF PISGLDMTDY VIDVKDDDRL MYDLYAIDNH YGDMGGGHYT
AYAQNAIDKH WYDFDDTSVT KIDERRIKTS AAYVLFYKRR RRRSNVD
//
