ID A0A068RW90_9FUNG Unreviewed; 1115 AA.
AC A0A068RW90;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=LCOR_05269.1 {ECO:0000313|EMBL:CDH53970.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH53970.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH53970.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDH53970.1}.
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DR EMBL; CBTN010000020; CDH53970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068RW90; -.
DR STRING; 1263082.A0A068RW90; -.
DR VEuPathDB; FungiDB:LCOR_05269.1; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000027586; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 55..186
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 212..529
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1115 AA; 128631 MW; F7A311145F4B8A83 CRC64;
MDERMSDAGP VEDVINECDK TMTEAEPAPT LSIIDDYEQI AEKELAPQDE ETVETKVFHW
NIENYKDLPE RVQGPVFEVG GHKWNILLFP RGNNQNELLS VYLEYAELRE NPSPDVYACA
QFVIALSPPS DPTRFVSQVS HRRFCAEETD WGFTRFMDLR RIYQGDAQTG TAPFIENDSL
RISVIVRVIA DETGVLWHNF INYDSKKMTG YVGMKNQGAT CYMNSLFQSL YCTNYFRKAV
YQIPTENDDP NNSIALALQR LFYNLQFNSN SVGTTELTRS FGWTSSDAFM QHDVQEFNRV
LQDALEAKMK DTPADGAIKK LFLGKMKSYI KCINVDYESS RSEDYYDIQL NVKGCKNLEE
SFKDYIAEET LEGDNKYMAE GHGLQDAKKG VIFEDFPPVL HLQLKRFEYD MMRDTMIKIN
DRHEFPLEID LEPFLDSNAD KSQPHKYALH GVLVHSGDLS GGHYFAFVKP TKDGRWLRFD
DDRVTPATLK EVLEENYGGE PLNGFGMGRP APRVYKRFTN AYMLVYIRES MRDEILGDVS
ENDIPPHLIK RIEEERLARE KRNRERAEQH LYMRVVLATD ESFEANTGFD FVRLDDRLRV
EDTHVQALRV RKDQTYGEFM QELAESTGVQ LGHFRLWLLV NRQNRTIRPD QPLSDSPEEL
ELTMEKIQEK YVTDSQNTLR LYMETAKVVE DDVPVFPPPS TANGQSVLVF IKLFDPKTQL
IRGVGHVYAP CNGKVSSITE ELNMIAGFEP ETPLRLFEEI KPTMIEEMDQ SITFNDAEIQ
DGDIICIQQQ LSDEEIIALK EQGLYSTVPE YMDYQNNKLN VLFVPRDKDP NGEVALEMHK
NTKYDDVSAK LAEKIGADAD KIQFFVPNTT TTDEPRHPYA RDPNDTLESM LYTQRLGRPF
VNGKLFYEVL DVSLSELESK RLIKVTTCIP TLKDGETSKL WISKQARITD LLKELQIGSN
PSVRVFEAIN NRFHREFMST DALAQVSDSH AAQLYIEPIP EEERNMGDED FFIRVFHFQH
NQHRTHSVPF KFLVRKDEPF EETKKRLQAR TGMADKEWSK VKFSIVSQYS AAPIDEDDYK
LSDHQFNRED SLGLEHIDRT KTNRSGFEKG LSIRA
//
