ID M5GGB2_DACPD Unreviewed; 1352 AA.
AC M5GGB2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EJU05183.1};
GN ORFNames=DACRYDRAFT_103677 {ECO:0000313|EMBL:EJU05183.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU05183.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJU05183.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU05183.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(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; JH795856; EJU05183.1; -; Genomic_DNA.
DR STRING; 1858805.M5GGB2; -.
DR HOGENOM; CLU_005874_0_0_1; -.
DR OMA; YLGQEKW; -.
DR OrthoDB; 6206at2759; -.
DR Proteomes; UP000030653; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01795; Ubl_USP48; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR044743; Ubl_USP48.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF722; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 48; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030653};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 169..466
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 943..1055
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 1165..1234
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1352 AA; 150436 MW; 78B96DD39EEA6CB6 CRC64;
MPPKGKRKGA PKPRPLSPVL ARKRKHPDNE EPTPPSRWSW VKLDGKVAEQ ITPKHMIWAC
GFSEESGLPV CPNIWSKDVK EGDEKGKGRA VDTGAYDASV SGKSQKAEVI DLTLPTLCSK
KKCRDNPNCL NYLGQDAWED EDEARAAFLQ VARLGYDPRE LNRDPEIPVG LRNLGATCYA
NAFIQVWFQD LAFRAGVYAC KPTAPEGKQL EDAPLFQLQA TFAALQQCRQ NIYNPIKLVE
SLGLRTSEQQ DATEFSKLFM NLLGEQFKLQ EAPSVKTLLR DQFEGHLTYC TTCKGCGHTS
ERDSEFLELE LNLGSKSHLE ERILEVLQKE ELTDDNKYMC SRCNSLKNAT RWVKLRDCPP
VLHFPLMRFV YDIKTYERKK SKQVIQFPLS LNMKPFLNGG AYMDDQIYDL RGVLLHRGLS
AYHGHYIAQA YDVSKGQWFQ FNDEEVSPLD GLMGGNSATA AAASSKSSQT SKENKSTNIT
SIVESEGGIR PKFDEEDERP VPIQDRGKEK VEHVVELLDD EVEPEPSEHP IDSSTPNSIP
RYLRSKDAYM LIYARRDVIT PADVPECPLP GTSGASAKPD CNTPAIPPVP LAAQREVDRL
NEEHDRKCDE YVKREQVVLE TFSQVRAVKQ EIYSSWNIQT HDDDSVVVNA EQLTKWLGQG
LDVPKQPIKE TENDIEVLES LAVNAESGVE ATTPGSSETP RSSIPPPCGR ELENIIPTAP
NILPENEPEP IVSDADSSKT LVSSPPVANP AVLQTNWLQG TLTSDSLCEH GLIVPPATSL
KRINQAAYMR LLSLGVIFEP ALAHTAVCPD CTEHVVSERI YGIRHPELVK VFQDQNIIHS
PEDVAYWVSK QWLKDWLSSR PKMHAYGQLD PPPNAEPWKN DLVCEHEGLK ISEKDRKLVS
AQAYRLLRTI YPGWETFSNT VEVCVVCQEA EDLTSDARAD ARKAADRERS RLRSMLSINP
LASRPVSLIE GFVYAVVPSA FIRAWRSWLI HPLTNSRPTS LDTSIFFCPH EKIYFDSNEA
VDMEDVDLVV IKESEWNILA QLYPAGQMIR LEPTTHIDEN ETVRNVVICN QEVCQQCRRE
RKSSFEEAPV TMYFMDITDP LPIGNTPNSE QPNAPSASNA DDLDIVSVSA QTGKSSPVKS
ESTLDAYVYG TSGNYDGGLR KSKRLRATKQ RGMNRTIIIR KGDTVKDIKV ELFDQFNIPT
IYQRLFHAGR EITDWSDKTV ADIGILAQDT ISVLEVKPVD EDDDEGGRPK KKRREEGPAF
GGTLLSRGGI PPPASATAPA VDTNASHKPD SMDSSHACAV AEALCAAPRP PDSNAPTDLA
DFEDSLHCPT CTFINPAGVS ACTMCDTPFA VA
//
