ID U4KV51_PYROM Unreviewed; 1047 AA.
AC U4KV51;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=PCON_03454 {ECO:0000313|EMBL:CCX04741.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX04741.1};
RN [1] {ECO:0000313|EMBL:CCX04741.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX04741.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX04741.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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 C12 family.
CC {ECO:0000256|ARBA:ARBA00009326}.
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DR EMBL; HF935216; CCX04741.1; -; Genomic_DNA.
DR AlphaFoldDB; U4KV51; -.
DR STRING; 1076935.U4KV51; -.
DR eggNOG; KOG1213; Eukaryota.
DR eggNOG; KOG2778; Eukaryota.
DR OMA; QQCGYAL; -.
DR OrthoDB; 276003at2759; -.
DR Proteomes; UP000018144; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd09617; Peptidase_C12_UCH37_BAP1; 1.
DR CDD; cd21789; Rad21_Rec8_M_SpRec8p-like; 1.
DR Gene3D; 1.20.58.860; -; 1.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR InterPro; IPR006909; Rad21/Rec8_C_eu.
DR InterPro; IPR006910; Rad21_Rec8_N.
DR InterPro; IPR041507; UCH_C.
DR PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR10589:SF16; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR Pfam; PF04824; Rad21_Rec8; 1.
DR Pfam; PF04825; Rad21_Rec8_N; 1.
DR Pfam; PF18031; UCH_C; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCX04741.1};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 6..231
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|Pfam:PF01088"
FT DOMAIN 261..294
FT /note="Peptidase C12 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18031"
FT DOMAIN 309..407
FT /note="Rad21/Rec8-like protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04825"
FT DOMAIN 1010..1044
FT /note="Rad21/Rec8-like protein C-terminal eukaryotic"
FT /evidence="ECO:0000259|Pfam:PF04824"
FT REGION 491..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 690..721
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 491..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1047 AA; 114282 MW; 389E9CE53E8F12B2 CRC64;
MAEHGWNTIE SDAGVFTELV EGLGVKGIQF EELHSVTEAG DVDYLRSLAP VYGAILLFKY
PKKQPENRDG TLDEAASYNL FFANQVIQNA CATQAILSIL LNRTGLDPSD KSHTAGGENP
DPVDADVNIG DMLIAFKEFA KEFPPEDRGL ALSNSVEIRT VHNSFSYSSP FADEGNKPSS
GEGDAYHFIA YTPLNGQLYE LDGLQPAPIS HGPCTKDDFA DKLLPVVTRR MRSDPDGGIS
FVLLAMVKDP RIMAQKIGDE ETIRRENAKR KAWKWENDLR QHNFMGFIHE ALKEVITTKV
KAGDSLATMF YSHEVLTERQ YGIATIWLVA TLGLSRTTLK KLGRKDILAV NLPKACGKVI
EPVAPLALRL QSNLLIGISR VYKQQTEYLY HDVTNAHTTI KKLEISNNLP NIAANLDHER
GGEGRPEQLI LTDDPRLHPD LLLDIDLAGL GELSLTDVDL GDFNDLANSL QSGQMTPSQR
SQITQLSQLF SPGAMVPGSS PSTRSAAAGT GFEPSQHLGH GSSETGMDYE RLELEENPLF
EFDENGEMRE VTPTLPDPFG GDPTTPRGDG DRTPRARVPG THGSEDIEER VRREHDEAGR
PGSEAFQMDQ LPGSDLFPDF PQQMNLGEHP PSAQPVPEDE TSGLSSLTAG SKHLPSEASS
EQIVAEAAAK KTRGPRIKKV IIDDDIELTN HDLKEQHKNY LENMEAARKA METRKLNKEA
KVNAGILVLQ HGISGLLLDP TLKETFSGQA IINSIFSIIP SAMGGESPKK RKRGAIGSDN
EENARTSSRA RTDEPATQPP SEIGRGDGAA DNFSIGFGSE LGMGGNLGQP GTPMYGEMEV
GRDAPPALPS DLGSVKSYRS DGMPWSNVGL PNSPLPGPAG GIPSSSIGYG GVPSSPMARN
TRAMSRMSVA GSVRSMLGIV QEVGEESTFM QDQMGMRDDQ LPEEFQFFDA EAEAQDTQQL
HAAVETEANL FFEYLKNRLV VENERRMEQD EDDEVNFITF DGLIKPGQER REVAAQAFSH
TLLLATKGLL MVSQEEQPFG EIQIGIF
//
