ID J4G2D1_9APHY Unreviewed; 1268 AA.
AC J4G2D1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=FIBRA_02696 {ECO:0000313|EMBL:CCM00658.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM00658.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM00658.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM00658.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
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};
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DR EMBL; HE796998; CCM00658.1; -; Genomic_DNA.
DR RefSeq; XP_012179941.1; XM_012324551.1.
DR AlphaFoldDB; J4G2D1; -.
DR STRING; 599839.J4G2D1; -.
DR GeneID; 24095569; -.
DR HOGENOM; CLU_264185_0_0_1; -.
DR InParanoid; J4G2D1; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000006352; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000006352};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 11..38
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 39..66
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 67..92
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 695..996
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 441..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1268 AA; 137825 MW; F9194E47F2116DB2 CRC64;
MAPSTRASQT WNCSVCQRTF SRKYELNRHE VSHANVKPFE CKHCQKCFAQ KTALRTHYNS
HTKLKPHQCV NCSISFGDPS SRSRHRHEMH SGFLGYFCPG CSSSMKRPKN FKIHLEKCDY
VTKYNANIRV YMVYDESSED FKEYFKDRKP PREARIVVGS SKKAVIVNNV PVAIDSSSPP
VAMPSPSATK KAPSITAELS SIGRARRLKT LQRAHPYKKP LSSRRRESAE DINLADIPAD
VLQQSAAHSY TIPTAVAPPV PTEDVFNYVP VDFSYNAADD GILAQAHAQV PDMFLPGPVA
GPSSNPEIAV GYDLGLPPFD VPQIPSGSSV MIPPLVYGQW AGDVPSYTDT GATYEAPISS
QWDYQKYNTH SDYLYGIHGT QVTPHDDYSD LFETIATTPT EAIDAALQSL NTQPHYWPSN
IPTLPAKEAI SPYSPYSDAL SPLSDLTPSP GGTSYSSPGT PADMLSTVGS RGPSPQNEMA
YSLYRPPSSR PQYNWTPKCF CSLVIEGREC RDGARFGSKS GGEKEDAKSR EEQSLTATFF
ALISSPRPTL ALRRVLSGLF LTLPRPPPLS LILSAHTPPF MLASPLVPAS GFADDTAQYR
PAKDLEAFKS LLPPAIEFVE GSSSGTFATD EIKYQPINTT PKANRAEPSD SSMRKALPST
PTKASKSPRA PAVTDKPLYT GSLTTSWPSG TTVGSGLYNT GNTCFLNSAL QCLLHTPPLL
HVLIAHSKVD PCQVRKGAYC MACGLRSVMF DSHQKHRQFS PSQITSNMHV IAKHMRRGRQ
EDSHEFLRYA IDALQKACLA GYPPKLDPKL AETTWVHKIF GGRLRSRVTC LDCGHNSDTF
DSVLDLSIDI LGSSGLKEAL RKFTAVDHLK GADKYKCEKC KKAVTADKQF TVHDAPLVLT
IHLKRFSPIG GKIGQPVKYD ERLSLQSVMS SGQHGPSYVL YAVISHAGGG PNSGHYYAHV
KGSNGQWYEM NDDSVTRHPG APTGMKNAYI LFYIRDKGQA LEAAVNAPAK ILNRDTTPAK
MGIVANMKKR KAVESDDESS LRPKSKTSAP FIGPRLPSPV PASTADTSKA NANAIDPQAE
VLKKKIAAVG QSPSSALLSL AQYDDEDDED IGEKVNEMKT TTPDSELVPS SPVIPPSSST
ASSTQEVQSS TPPPLTASTS TPSVFTTIST SSFYGTKSKG KDESNSKKRK SPEPDPDDPS
ISQWARTPIS PGLSLSTPTV GRRQSGGRSG GIGSGSPFNR IKGSNNLAQR RDAGGPIQQY
GRKKRLIM
//
