ID A0A0B7MWM4_9FUNG Unreviewed; 1878 AA.
AC A0A0B7MWM4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=PARPA_00575.1 scaffold 917 {ECO:0000313|EMBL:CEP07294.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP07294.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP07294.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP07294.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) 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; LN719154; CEP07294.1; -; Genomic_DNA.
DR STRING; 35722.A0A0B7MWM4; -.
DR OrthoDB; 1356823at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR018834; DNA/RNA-bd_Est1-type.
DR InterPro; IPR019458; Est1-like_N.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
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; PF10374; EST1; 1.
DR Pfam; PF10373; EST1_DNA_bind; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF48452; TPR-like; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107}.
FT DOMAIN 304..863
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1706..1773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 939..980
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1709..1723
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1759..1773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1878 AA; 215236 MW; ED5442DC69054D74 CRC64;
MDQQKDGSNK KVTAGENSQN KRLKISSSKS RRALPPPAQL ALFERIKAKY TETSSNIKIS
KQWYIQWEAY CLGLSSLPPN PMYLSQIDDP STFIAMHPKA VFYLRDWYGA EDEILQLNLD
LSDHQVPSDN VIFSKKHRPA KGKVYTASIS DDDEEDDKLL RFKIYIVGKP VSEFQYSFSI
SAGSSVSSFQ SSLLNALNNC SYGTNMELWL LNQGNTSFIN KLNNDSRFAL SPDLLRNSDR
FAQRIEPTSV SFESTISSCL SQMSISNKSN KNNTFLLAVE YIKKSSMLPP TPPASSTMTI
LGLVGLQNLG NTCYMNSALQ CLSNTPQLTR YFLNGNYRHD INTSNILGLN GDLAKAYAKL
LREMWAAHSS YRASSLSPKD FKNTFEKFNP HFTGYLQQDS QELLSFLLDG MHEDLNRILS
KPYIEIPDFD GQFRDEEVAD RFWNYHKSRD DSIIVDLFQG QYKSRLVCDE CKKLLVVEIY
LQNIHRIFRE ADSIRTIKPT DAIYVYQLPC PSTEQDDEDW VVFPVYCSTI FDKVDPVSVP
QFGLPIVLAM RAEQLRDTLN LYYTIVSHIE RYCMLKLFEE DNSVPSSPTV PDTATLNVQQ
PIHTTAAVTP AGGRPMVPMP NLFDIHVFGY ENSLASFTFP VGGSQIHWYN TDEPLKQGRG
VIIEWSTSKA RQFFGANLTN SNINTDAWFD YERAEKSKGS ESRSRSNNET SRLITLDDCL
DEFTGDEKLE NEDSWYCPRC KKHQRALKKI DIWKLPEIMI IHLKRFSQVR RWGNKVDTMI
DFPLKELDMT SRVVGHQNEN LIYDLYAVDN HYGGMGGGHY TAFAQNIEDS RWYEFNDTIH
APLYIDNCQL LCIMSWTAIC QALSSVNRTQ LAEERNEEVV FISYIVHTGN ATSVATTTTT
ATTTTTPRRR RRRPRNKRKQ KAAPTDSSTN MPLINQKPIK ELNETLQEKT FNLADLSSEA
HALEKQLAEL QTQLKINYAN MPSKEQGRIA SAIAAEQINT TEEEMLYVRQ SLKKTYREIF
LHDFLYATTH HIEDKLWRHI FYAGIEDVRS KLRKINPDDM EKKNALQKTL LHRIDSAFKF
YRELNNTVKS SYHIDTKILG IDSVHQKTTS DDEKMGILLQ FNYICMGDLA RYHAQQAMAS
KSIKKTVDYW GLAKTCYLKA IDVHRKNGKP YSQLALISMS NGNAMDVVWY YCMSLAVKCP
SSVGRDNLKS FYSKIRFSSK PKDDSLTSMI SHFVESFLFM HRTVMFNQKD SEEFASTLSV
VTQLGAALAA LIHSTVEGKE REDDESTLSK SLITTLHIIR TTLTRSITIL MISVWIAGEK
LREKSNYNVR PAILSSQIHM NTFAFNLLTE AYRSSRQALD QVKETLVLEK FHQLENMIDE
ALLPGLSIWS TFLYTNMTSI SQYCMTAMND VRNREPEKKI LVKSIQSLLS LLISHPSFPD
PVLNVLPPTY PVSEDLVLLG IMPLFGFHSN VDFFKENAYE VDDGKNPEAR KQVRWGRVRN
MIKKMADSSS FDFIQYNQVE QKYSVIDENA KRQQQSRFMK ALATQRLMEQ VSSLEKNVNR
MSLGKRIQNS SENNAPPVKQ NVYTCVIDIT AFLDGLNKVK KWANQTLNVD RRSQDSILEV
IVPLEVIDSL DDHKKGTSHT NMQARESIRF LDQKLLESSN KSETPTTSFL RTQKVTEKLS
DWSEAKAYWI GEESRSNVVD HLISDGEDEN QEVDSDVEIE SDIESTSSNE SLFKQRRRGS
DSGSELETET ESESESESES ESQSQSQSED GNNQKVEEFM YEDEDEGIPY TIEDVPKSYR
AIIGCVLYYH SKLQSRDNNQ PERLVLVTND EDLAWWAELF GDRKSRKRLL IKTVSEWDQM
VSKLDFEKVY EYSWNRNR
//
