ID M5BWA2_THACB Unreviewed; 1118 AA.
AC M5BWA2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=BN14_01988 {ECO:0000313|EMBL:CCO27997.1}, RSOLAG1IB_00352
GN {ECO:0000313|EMBL:CEL51817.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO27997.1, ECO:0000313|Proteomes:UP000012065};
RN [1] {ECO:0000313|EMBL:CCO27997.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Isolate 7/3/14 {ECO:0000313|EMBL:CCO27997.1};
RA Jelonek L.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCO27997.1, ECO:0000313|Proteomes:UP000012065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065},
RC and Isolate 7/3/14 {ECO:0000313|EMBL:CCO27997.1};
RX PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA Schlueter A.S.;
RT "Establishment and interpretation of the genome sequence of the
RT phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL J. Biotechnol. 0:0-0(2013).
RN [3] {ECO:0000313|EMBL:CEL51817.1, ECO:0000313|Proteomes:UP000059188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL51817.1};
RA Wibberg Daniel;
RL Submitted (NOV-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; CAOJ01002707; CCO27997.1; -; Genomic_DNA.
DR EMBL; LN679100; CEL51817.1; -; Genomic_DNA.
DR AlphaFoldDB; M5BWA2; -.
DR STRING; 1108050.M5BWA2; -.
DR HOGENOM; CLU_003532_2_1_1; -.
DR Proteomes; UP000012065; Unassembled WGS sequence.
DR Proteomes; UP000059188; 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; PF00917; MATH; 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, ECO:0000313|EMBL:CCO27997.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000059188};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 56..187
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 213..531
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 128588 MW; DC66590081C5A68E CRC64;
MSVLQQQQQP EAMETLDEKA GPSNLAMEVD EPVSVRDHEA FAAKQLPDLG HEVEDFQVFT
WRLSKWRQLE KKITGPEFDC GGHRWRILLF PAGNSNSPPN DTVSIYLDYA NPKNAPEGWH
ACAQFALVMS NTQDPTNFVC SHAHHRFIAE ECDWGFTRFH DLRKLFNGIE GRKPIIENDE
ADITVFVRVL KDPTGVLWHN FVNYDSKKET GFVGLKNQGA TCYMNSLLQS LYCTRYFRRA
VYQIPTEEDI PSESVALALQ RVFYHLQTSD QPVGTTELTK SFGWKSLDSF MQHDVQEFNR
VLQDKLESKM KGTPAEGAIN KLFLGKMKSY IKCVNVDFES SRVEDFYDIQ LNVKGMANLY
ESFKDYVAVE TLEGDNKYQA EGLGLQDAKK GVIFQEFPPV LHLQLKRFEY DIQRDAMVKI
NDRHEFPFEI DLAEFLDDTA DKTQPWVYKL HGVLVHSGDL HGGHYFALIK PDRDTRWLKY
DDDRVTPVTD REVLEENYGG ELSNGLVNNQ RNPVRQLKRF TNAYMLVYIR ESAIDEVLAP
FTDKDTPLHL KQRLEEERQA SELKKKEREE QHLYLTARII TDKTFSNHQG FDLATFDDKN
APQSDFHSLR ILKTDSYAMF KSIVAKTLHY NEAHIRLWVL VNRQNKTIRP DTHIPEDEAT
LRESVESIRN TMAARQTDLR LYLDVIADAN GQLLPEANSP NSIMVFLKYF DVSKQTLSGI
GKVYVQKNSK VGDLIPIINE RMRWQPTTPV RLYEEIKPGM IEVMKPKLTF AQNEIQDGDI
VCFQAELSEK EISDLEAQGL LSTPIQFYDL LQNRVLIKFK PRFEDVGQEE FDLVLSKKMN
YDTLATKVGE HLRHEPIKLR FTTSSNTGQP RQVLKRALNQ TIAEILQPSY GTAPIPILFY
EMLEVSIVEL ETKRNLKVIW TGSHNREETT VSFLLPKTSM VHELCEQLAK HEQIKLTPGE
SGKIRVFEVT KDGKHQHEFN ANEMLGNLPE TDIYAEEITA EELSAGENDK VISVFHFTKE
STRWHGVPFR FVVKPNEKFV DTKKRLQKRM GITDKEIAKY KFSLIQSALF RQPNPIEEGD
IIFDHKFLPE DVLGLDHIDK TGKAGRSGPG EKAIVIKG
//
