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Database: UniProt
Entry: K7LIW5_SOYBN
LinkDB: K7LIW5_SOYBN
Original site: K7LIW5_SOYBN 
ID   K7LIW5_SOYBN            Unreviewed;      1120 AA.
AC   K7LIW5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=GLYMA_10G120900 {ECO:0000313|EMBL:KRH33404.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH33404};
RN   [1] {ECO:0000313|EMBL:KRH33404.1, ECO:0000313|EnsemblPlants:KRH33404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH33404};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH33404.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH33404}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH33404};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH33404.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH33404.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) 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; CM000843; KRH33404.1; -; Genomic_DNA.
DR   RefSeq; XP_006589035.1; XM_006588972.2.
DR   AlphaFoldDB; K7LIW5; -.
DR   MEROPS; C19.A73; -.
DR   PaxDb; 3847-GLYMA10G23671-1; -.
DR   EnsemblPlants; KRH33404; KRH33404; GLYMA_10G120900.
DR   Gramene; KRH33404; KRH33404; GLYMA_10G120900.
DR   eggNOG; KOG1863; Eukaryota.
DR   HOGENOM; CLU_003532_0_1_1; -.
DR   OMA; DTDWGFA; -.
DR   Proteomes; UP000008827; Chromosome 10.
DR   ExpressionAtlas; K7LIW5; baseline and differential.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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 K02C4.3-RELATED; 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; 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:UP000008827};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          60..184
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          203..527
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        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1120 AA;  130767 MW;  D725F1C83262AAD1 CRC64;
     MTLMTPPPMD QQQQQQEHDE MLVPRSDLPE GPQPMEAQAE IPSTVDAPTV DAPTVDDTPT
     AKFTWTIDNF SSISQKLFSD IFCVGGYKWR ILIFPKGNGA GHLSMYIDVA DSATLPYGWS
     RYAHFNLTVV NQIHSKYSIR KDSQHQFNAR ESDWGFINFM PLAELYDPAR GYLVNDTCIV
     EADISVRKDM DWSYDSKKET GYVGLKNQGA TCYMNSLLQT LYHISYFRKA VYHMPTTEND
     MPSVSIPLAL QSLFYKLQYS DTSVATKELT TSFGWDTYDS FMQHDVQELN RVLCEKLEGK
     MKGTVVEGTI QQLFEGHHMN YIECINVDYK STRKESFYDL QLDVKGCKDV YASFDKYVEV
     EQLEGDNKYH AEHYGLQDAR KGMLFIDFPP VLQLQLKRFE YDCTRDTMVK INDRYEFPLQ
     LDLDMDNGKY LSPDADRSIR NFYTLHSVLV HSSGVHGGHY YAYIRPTLSN QWFKFDDERV
     TKEESKRALE EQYGGEEELP CINPGFDHSP FRFTKHSNAY MLVYVRESDK DKIICNVDEK
     DIAEHLRMRL KKEQDEKELK RKEKAEAHLY TTIKVACDED LREQIGNNIH FDLVDYDKVR
     SFRVQINMPF MVFKEEVAKE FGIPIQYQRF WLWAKRQNNT YRPNRTLTPQ EEAQSVGLLR
     EVSTKANNAA LKLFLELEMG QDLRPIPPPE KSKENLLLFL KLYEPSNEKL RYVGRLFVNS
     SGKPEDILVK LNEMAGYDPD QDIDMFEEIK FVPNVMCERV DKKSTFRESQ LEDGDIICFQ
     KSSPQTGSGE RYRYPDVPSF LEYVHNRLVV RFRTLEKPKE DEFSLELSKL DSYDNVVEEV
     AQHIGLHDPS KIRLTSHNCY SQQPKAQSIK FRGMEHLTDM LIHSNQTSDI LYYEVLDIPL
     PELQCLKTLK ITFHHATKDE VVIHTIRLPR HSTVSDVIND LKSKVDLSHP DAELRLLEVF
     YHKIYKIFRV NEKIENINDQ YCALRAEEIP EEEKNLGSHD RLIHVYHFLK DTTQNQQVQN
     FGHPFLLVIR EGETLAEVKL RIQKKLQVPD EEFSKWKFAF LSFGRPEYLQ DSDIVSTRFQ
     RRDIYGAWEQ YLGLEHIDSA SKRSNTANQN RHEKAVKIYD
//
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