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Database: UniProt
Entry: S8DRQ2_FOMPI
LinkDB: S8DRQ2_FOMPI
Original site: S8DRQ2_FOMPI 
ID   S8DRQ2_FOMPI            Unreviewed;       535 AA.
AC   S8DRQ2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   03-JUL-2019, entry version 37.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   ORFNames=FOMPIDRAFT_152388 {ECO:0000313|EMBL:EPS95951.1};
OS   Fomitopsis pinicola (strain FP-58527) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Fomitopsis.
OX   NCBI_TaxID=743788 {ECO:0000313|EMBL:EPS95951.1, ECO:0000313|Proteomes:UP000015241};
RN   [1] {ECO:0000313|EMBL:EPS95951.1, ECO:0000313|Proteomes:UP000015241}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FP-58527 SS1 {ECO:0000313|EMBL:EPS95951.1};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A.,
RA   Henrissat B., Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S.,
RA   Aerts A., Benoit I., Boyd A., Carlson A., Copeland A., Coutinho P.M.,
RA   de Vries R.P., Ferreira P., Findley K., Foster B., Gaskell J.,
RA   Glotzer D., Gorecki P., Heitman J., Hesse C., Hori C., Igarashi K.,
RA   Jurgens J.A., Kallen N., Kersten P., Kohler A., Kues U., Kumar T.K.,
RA   Kuo A., LaButti K., Larrondo L.F., Lindquist E., Ling A., Lombard V.,
RA   Lucas S., Lundell T., Martin R., McLaughlin D.J., Morgenstern I.,
RA   Morin E., Murat C., Nagy L.G., Nolan M., Ohm R.A., Patyshakuliyeva A.,
RA   Rokas A., Ruiz-Duenas F.J., Sabat G., Salamov A., Samejima M.,
RA   Schmutz J., Slot J.C., St John F., Stenlid J., Sun H., Sun S.,
RA   Syed K., Tsang A., Wiebenga A., Young D., Pisabarro A., Eastwood D.C.,
RA   Martin F., Cullen D., Grigoriev I.V., Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed
RT   from 31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide,
CC         peptide and isopeptide bonds formed by the C-terminal Gly of
CC         ubiquitin (a 76-residue protein attached to proteins as an
CC         intracellular targeting signal).; EC=3.4.19.12;
CC         Evidence={ECO:0000256|RuleBase:RU366025,
CC         ECO:0000256|SAAS:SAAS01117307};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025, ECO:0000256|SAAS:SAAS01045498}.
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DR   EMBL; KE504197; EPS95951.1; -; Genomic_DNA.
DR   STRING; 40483.S8DRQ2; -.
DR   EnsemblFungi; EPS95951; EPS95951; FOMPIDRAFT_152388.
DR   OMA; KCDDHLI; -.
DR   OrthoDB; 929408at2759; -.
DR   Proteomes; UP000015241; Unassembled WGS sequence.
DR   GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016578; P:histone deubiquitination; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR037798; UBP8.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR21646:SF33; PTHR21646:SF33; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000015241};
KW   Hydrolase {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044238};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01044152};
KW   Protease {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044292};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015241};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044269};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044331}; Zinc {ECO:0000256|SAAS:SAAS01044373};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS01044352}.
FT   DOMAIN       45    104       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      157    489       USP. {ECO:0000259|PROSITE:PS50235}.
FT   ZN_FING      45    104       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
FT   COILED      503    530       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   535 AA;  59895 MW;  BAF9E4AE6C4C25DE CRC64;
     MCPHTVPYSL DKGHVLERMK ALGNWNTRRV HQASRPSKRR KLSLPACGTC QSTLRQFACL
     QCAFFGCWHN GHVKDHLEDA GHNFCVDVKT GSIYCNECAD FVYESAAART FAIATFDAEE
     IIGGVRKSRQ PFEPWKPNQK ERAILQTAIA MPCQARRGLL NLGNTCFMNA ILQSFIVNPL
     LRDFFLSDKH NHLLCKNTDC TCCEVDKLFS EMYSEDEAPY GPASFLATTW RASAELSGYA
     QQDAHEFFMA ALNHIHSTSR GSTKLSCICI VHSTFAGLLQ SDVKCGRCGN VTTASDPMLD
     ISLELQDKAG SGHAGHELTL ASCLRRFTQP EKLGPNEYAC AKCGKASHEA NKRLSLRKLP
     PVLSFQFKRF EHKTGDKTAA QKIEAPVRFP STINMAPYTS LAMAVREREG KDGTQTSALF
     SIPGPGSMYE YDLFAVVCHE GQIDNGHYTC FARSQDEWYR FDDDKVSHSS LRACLSSRSQ
     AYMCFYVKKH LDYKPYVTPS YKVAREAEAV KEKRREKEEA AARMREVEAA LLATV
//
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