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Database: UniProt
Entry: A0A1B6Q6D7_SORBI
LinkDB: A0A1B6Q6D7_SORBI
Original site: A0A1B6Q6D7_SORBI 
ID   A0A1B6Q6D7_SORBI        Unreviewed;      1118 AA.
AC   A0A1B6Q6D7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=SORBI_3003G310900 {ECO:0000313|EMBL:KXG33467.1};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG33467.1, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:KXG33467.1, ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA   Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
RN   [2] {ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=29161754; DOI=10.1111/tpj.13781;
RA   McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA   Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA   Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT   "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT   a transcriptome atlas, and signatures of genome organization.";
RL   Plant J. 93:338-354(2018).
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; CM000762; KXG33467.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B6Q6D7; -.
DR   STRING; 4558.A0A1B6Q6D7; -.
DR   EnsemblPlants; KXG33467; KXG33467; SORBI_3003G310900.
DR   Gramene; KXG33467; KXG33467; SORBI_3003G310900.
DR   InParanoid; A0A1B6Q6D7; -.
DR   OrthoDB; 51419at2759; -.
DR   Proteomes; UP000000768; Chromosome 3.
DR   ExpressionAtlas; A0A1B6Q6D7; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
DR   CDD; cd00121; MATH; 1.
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; IPR029071; Ubiquitin-like_domsf.
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:SF934; UBIQUITINYL HYDROLASE 1; 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   SUPFAM; SSF54236; Ubiquitin-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:UP000000768};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          62..187
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          207..530
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1118 AA;  130600 MW;  B579A11BF8FD36C2 CRC64;
     MAVSGAPEQP QREQPQQDHD EEMLVPHQDA IEGPQQDVVE GPQPMEESAS AVENQLVPDT
     STSRFTWCIE NFSRRNVRKH YSDDFIVGGY KWRVLVFPRG NNGDHLSMYL DVADSNLLPP
     GWSRNAQFSL AVVNQLDSKA SLRKEAIHQF NSRESDWGFT SFMPLLDLYD SSKGYVVNDK
     CIIEAEVAVR KTFDFWNYDS KRMTGYVGLK NQGATCYMNS LLQTLYHIPY FRKAVYHMPT
     TENDTPSGNI PLALQSLFYK LQHCDNSVAT KELTKSFGWD SYDSFMQHDV QELNRVLCEK
     LENKMKGTPV EGAIQKLFEG HHMNYIECIN VDSKSTRKES FYDLALDVKG CSDVYASFDK
     YVAQERLEGD NKYQSEEHGL QDAKKGMLFI DFPPVLQLQL KRFEYDFVRD TMLKINDRYE
     FPLQLDLDRD DGKYLSPDAD RSVRNLYTLH SVLVHSGGVH GGHYYAFIRP KLSDQWYKFE
     DERVTKEDMK RALEEQYGGE EELPHTNGLK NAPIRFTKHS NAYMLVYIRE SDKEKIICDL
     DDEDIPDHLK VRLRKEQEEK ECKKKEKAEA HMFTALKVAR DSDFKEQIGR HMHFDLVDFD
     KVNSFRAPKN MSINDVKEEL SKEFGIPVES QRFWVWAKRQ NFTYRPSRPL TFLEETSAIG
     YLKDAIVAKL PNSEVRLFLE VHLGQENQGI ASGKTKEDIL IFFKLYDPEK EDLRYVGNFF
     VKASGKPSDI VERLNEIAGF PSDEDIELYE EVKFEPAVMC VPIESNISFR SSQIDNGDII
     CYQKRCLPDS MDRYRYPSVP SFFEYIHNRQ VVYFRLLDKP KEEGFSLELS KRSTYDDVVE
     KVARQLRLDD PSKIRLTQHN LSSQQPKPHH IKYRSLNYLS DMLHNHNQMC NILYYDVLDI
     PLPELESTRS LKITFENATN HEMSFHTMRL PKSNTLLDLI EDLKSKVELS CNDAEFRFFG
     VHLHKICKVY QPGDKIDSVN EPLYIEEVPE EEKNAGPHDR LVHVYHFEDN RHVQYFGEPF
     FFLIRDGEAL SDIKVRIQKR LQVPDEQFIK WKFAHVTFSR PEYLQDSDIV LNRFHKQKPV
     YGAWEQHLGL EHTATTPRRS YFGSQNRHSF ERPVKIYN
//
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