ID A0A074XV95_AURPU Unreviewed; 1532 AA.
AC A0A074XV95;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=M438DRAFT_350913 {ECO:0000313|EMBL:KEQ89513.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ89513.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ89513.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ89513.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584974; KEQ89513.1; -; Genomic_DNA.
DR STRING; 1043002.A0A074XV95; -.
DR HOGENOM; CLU_001060_9_0_1; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000030706; 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 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:UP000030706}.
FT DOMAIN 217..342
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 555..1333
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 60..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1457..1532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..943
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1102
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1457..1472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1476..1504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1532 AA; 169260 MW; C548E6D06B9F9AF0 CRC64;
MTTPQVPEAD QNFYVRTKPP GALLHQNLYR TSFPPDNAHR HCPPSCRRIL YIRPFHSTEL
PFSGGSPSVK TASSKKQKVA HPVADDPRHA YHQAVHDPDR QPSSPQSSSS PSSNQAAHTP
SSPPRYIPPH LHADSRASSP SDAYAQLNLA EDMSHSSAQG DTDAPNPTQR PASPAKRSAA
TMEGIESAAD PVTSNESQQA PPSYDAHQQD ASPSFTPSFE EQVTRIQAML NVPVEDGSKV
FIVAAKWFHR VMARTADADQ KVFDPEMLEG EVGNIDNSSL VAPGAFDDPL AFPGKPDLPY
VPLRADVERE THFEVFTEEA WRQIVEWYGV SDCQLPILRF AHNVAPEGSP SSNIIYELSP
PVFTIRKVPS APQSAQADAA AVKVVASRSE RFQSFLARAK EAASIPMQHK VKIFKQLNPT
LISGDMPNTA QPGIPSPPTS RNPSPSPSTS SKLVIDRSTF TRWTVGTNFE PVDGQDHTTN
EKYNGKSTLE ILGLIADQTL ILEEQQRGEY ASDASKKQKN SNPQTQDTNR RTSPAPTAPT
TRGRTRKDGR TRGSIGLTNL GNTCYMNSAL QCISRVEELA VYFLHHKHKP EINADNPLGY
NGKIANAYAN FLAGLYSDNA TSAYRPGGFK GALSMAQPMF SGYGQQDSQE FLSFLVDALH
EDLNRIQKKP YIENPDSDDK TVHDPEAIRQ LGDKYRENHH ARNDSIAMDL FNGFYKNTMV
CPDCEKVSVT FDPYSLLTLQ LPIENTWQGK IMFMPVTGYP SAFEMDVEKN ISVKALKDIF
VSKIGRGLTR ERLIFAEMFS HRFYKIAYDS QTLSELEFSS SDILCMYELS EVPTNAAFMP
RKQMGYRSIY HDPPEDLPGM DSPLAETMAI PVFHSKVERR VSSPALNPTL ITVTKEEAKN
YDAILKRVLA AVTTMTTKRL LEEIPKEEAP DSATDHDNDA DISMRDGSQT PSKQLLDALQ
PGRFICPELR NMFELKYVQA SGDMFLTGTG TINNASPMQA RVRAVERRRG SISSVASNTS
VRSQDSGYDG QGRESCDSDQ ADPMVESFRA SGQDTFTGDV QSDDESGMGS LEQLSAKDNR
RRKFNKNKAR KTYSRKGRRP NNKNPVRSNL PRATAADEPK DGNEFYVKLG EGIVIEWQED
AFESLFGGGD GNGQYTFNHK EVPLVDDAEL QLRRNKRMQR KKNGITLDDC FSETGKTEVL
SEDNAWYCGR CKELRRASKT LELWTVPDIL VVHLKRFSGE RFRRDKVDVL VDFPIEGLDL
TKRVGCKEEG KEYIYDLFAV DNHYGGLGGG HYTAYAKNFY DGNWYDYNDS SVSRQNPEGV
VSTAAYLLFY RRRSQTPLGP AYLQELVLKA RNPEEASDGE DESGEGERLG DHSSASSRLP
GSSNAGAVGA GAAITGTPQQ GANAGGPGRG VSQAVMPTSE FNDDEGISLN DELYDSNTTA
ATLANQEASW GFEVLGEDDN TTSVNTPADT ASDRPDAGSD AGDRLMELVN DEHEKDRYGD
NDSPPPLMDD ETMIEEGQEQ FDGPNASTHD YE
//
