ID A0A2G4T974_RHIZD Unreviewed; 1186 AA.
AC A0A2G4T974;
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=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=RHIMIDRAFT_310247 {ECO:0000313|EMBL:PHZ17565.1};
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:PHZ17565.1, ECO:0000313|Proteomes:UP000242254};
RN [1] {ECO:0000313|EMBL:PHZ17565.1, ECO:0000313|Proteomes:UP000242254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ17565.1,
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 -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; KZ303842; PHZ17565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G4T974; -.
DR STRING; 1340429.A0A2G4T974; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000242254; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
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 Reference proteome {ECO:0000313|Proteomes:UP000242254}.
FT DOMAIN 32..141
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 303..1111
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1186 AA; 134695 MW; 25C9C0154620CDAF CRC64;
MSDNETDKSP ISTKRARESS MEEDVEERAS KIDPKDQVKI ITQLQQEHLS EGQTWYLVSK
NWFTRWRQYC SRLSSPQHDA RKIGEQTNPG PINNQSILQA NGKLVEGLKL NDTVFAVPEE
AWKDLMEWYG SVTEPIERLM IKGTDGELTV ELYPPHFKLF VVTDSTSTQL TRCPQFTLSE
VSTVNDLVST IKESLDLSQD AELQVWTLED EPTTPIISSN ILQNASQIDI ENGSASLGRS
GQCNIAVAIK GDARFPSDVK QSDTSSVSSA SSIFANGFNN LTTTSSASTP TSSPYSKFTR
GVCGLQNLGN TCFMNSALQC LSNTPELTKW FLADNYKNEL NRDNPLGMKG QVAEAYGELI
EKLWSGHSHS FAPRDFKYTI GKFNSSFYGY QQHDTQELLA FLLDGLHEDL NRIIKKPYME
LPDFDGMKDE EIAKKSWDYH RARNDSVIVD LFQGQFKSRL VCAECKNVSV TFDPFMYLSL
PLPIKKKSKT TIVYVPYDPM KRMQRVVVTL SKDASIAHLQ REIARMMSVE DPSTLLVVEL
FSHKIYKVFP QYEPVATIGS SDTIYVYQLP GPVPPTPKRK VKSYRFGKDD DDDNEDSTSE
HDGQLIVFPV YCATVDKSEQ ATYTSPQQFG DPFVIGIPRK YCTNVDSLYR LLSQHVERYT
HFKLFEEVNG DAEMEDEPPK YEAVVTNGHQ QDMDIDEQQQ QQPIHTAAAV TAAGGKKTEP
MSNLFTIKVF SGGHTYGRHT EDLLPCTHGL TPWTDLRERA EDEQRQREEY ERQQIQPDVN
GNDIEGLPET ENDDTEMEDS IVMSSSMQDE EEVENAAVNF YQNDTITTTY SPIINPATDN
DTESILSNEN NVGSKPESPV LDSFTTPPQL PNSYDTMRHK PTIPVKRKLT CPPSTVIRQG
EGIVLEWTPK RAQQLFGESQ FSSSNGVSGS GWEDIEELGD PEEAKMGPTD AKNKQQITLA
DCLDEFTKEE ELGEEDLWYC PKCKKHQMAT KKFDLWRMPD VMVVHLKRFS HSRTWRDKID
AFIDFPVESL DLTDRVLSID NKEALKEEDR LIYDLYAVDN HYGGLGGGHY TAYAQNFEDK
NWYHFDDSHV SKVNVSDIKT SAAYLLFYKR RKPQNQVNEK CVEDIIQETK EKQQAAEKQN
ETDNMMSDDQ ILSAKEEDQD QTSETNTITN RDELRRSNDD DDIVTD
//
