ID E3KDF8_PUCGT Unreviewed; 1410 AA.
AC E3KDF8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=PGTG_08350 {ECO:0000313|EMBL:EFP82394.2};
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP82394.2, ECO:0000313|Proteomes:UP000008783};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CRL 75-36-700-3;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA Schein J.;
RT "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT 700-3.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRL 75-36-700-3 / race SCCL
RC {ECO:0000313|Proteomes:UP000008783};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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; DS178282; EFP82394.2; -; Genomic_DNA.
DR RefSeq; XP_003326813.2; XM_003326765.2.
DR STRING; 418459.E3KDF8; -.
DR EnsemblFungi; EFP82394; EFP82394; PGTG_08350.
DR GeneID; 10529771; -.
DR KEGG; pgr:PGTG_08350; -.
DR VEuPathDB; FungiDB:PGTG_08350; -.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_2_0_1; -.
DR InParanoid; E3KDF8; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000008783; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 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; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 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:0000313|EMBL:EFP82394.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008783}.
FT DOMAIN 11..122
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 345..1184
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 267..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1404
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1410 AA; 155926 MW; 8E39D77289A2D2AB CRC64;
MVKEVEMDEI PSPQEQARLY HSFRSIRMAT DQTWYLIHQQ WFNTWSSSIG IATDDSTAAG
TTTTTTDIPS IDNSDLLDHE NQLRFGISIG IDCEIIPEEF WNLLVKWYGL KQPTHAIPRS
VIAPSGPSSE SVEFYPPSFI FHLILPSSNL EELESEQQYD LNLIRQLPNL VIQKRFSIGN
SIGDLKRELT SNLLPAGLLT RSFKLWSIHS PPSNPNQLIL SVSEFGNLET QLVEPSSGDA
ADLNEALLTD PVNVLAIEQQ DQEGHWLINP KSAPPSTPPQ LQDDDPTSSG PVFGGQEWLD
RMEKMNQANL LDPKFSITSP NSDLSLVAFN SAQSAFKARG IRGLVGLTNL GNTCFMNSAL
QCLSNCPELK TYFLSRVYIN ELNRTNPLGM GGKVAETFGQ LIERMWSSEY EVSRRIQGST
SGTNGPTSYG GSSHQSISPR EFKSIVGRFN SLFLGYGQQD SQELLTFLLD ALHEDLNRVK
VKPFDEIPDY DDQNSLNDPL LEAQKILKLA KTCWNLYRRR NDSVIVDLFQ GQYKSTLICP
DCNKVAIKFD EIMYLTLQLP INKKFRGTIY FVPLDLSKPR IKVNYQINKD STIRQLKQHI
GQILCVDPDR MAAIEDWSGK PWKIWHDTDS LEGVMERDVI NVFETPLPFA ALKSGIYHTN
GEEEEVPDLL IPVVSYRPAE RMNMGSSTSI HKPSSTAFGV FFVARISAKD RLSTRAVYDA
VAREYARYTS QAEELFERNE DEDVVMNEPT AEIPPSSSSQ PTLHAVPNLF KISVPKTPCS
TVFPVSNAMG NATIELEERV KLSASKAPPG PAPVSGVNED ANGSNGAVFE MEENEDLYED
KAAAPEPRSS SSPSHSSQTG PVVFEGDYFE CEWTPSAMGH FFGLDKNLPN SKNWIDPPVI
EDPELVASRV AEQNKKSGAA GELTIEECFK DFSKPEKLGS EDKWYCPRCK NHVQATKQMQ
IWKVPDILVV HFKRFSSART SYGRSSKVDN FVDFPIQGLD LSNEVEGIKV VRELKKHQRN
LKASSRDQPV ADQDQDHKNL PQILVDDHLP SSSNPSDHNN NDKVGGEGKE IDAILEDQNT
ELDDGKEERQ QQQQQDGDRE RDGHENPQQE GEDDEDEEEE ESLIYDLFAV DNHFGGLGGG
HYTAFAKNEE DGKWHNYDDS HVTEVNSPER VKSSAAYLLF YRRRTTRKLG LKTHGIVSSA
MQSRDISARS SSQGNSSHMA DDDEDGSRAA IKTGAGARHA AMASSSSNGL ERPTSQEEEE
EVDELDEGVG AGVGAVGRGS SIGSVGREDG SLRSESPFSD LRPNLSRPIS SSSSSPASHS
PDASHSASPA SHSSSSELVP SLPLGHHSLL DSSDPILSHH SANHRDSSNL PAVGPSPADD
RHHVAPSAAP IPLPPVPPPP YKPHSSASSR
//
