ID A0A024TAL3_9STRA Unreviewed; 453 AA.
AC A0A024TAL3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=H310_14246 {ECO:0000313|EMBL:ETV91083.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV91083.1};
RN [1] {ECO:0000313|EMBL:ETV91083.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV91083.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) 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 C85 family.
CC {ECO:0000256|ARBA:ARBA00010407}.
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DR EMBL; KI914015; ETV91083.1; -; Genomic_DNA.
DR RefSeq; XP_008880279.1; XM_008882057.1.
DR AlphaFoldDB; A0A024TAL3; -.
DR STRING; 157072.A0A024TAL3; -.
DR EnsemblFungi; H310_14246-t26_1; H310_14246-t26_1-p1; H310_14246.
DR EnsemblProtists; ETV91083; ETV91083; H310_14246.
DR GeneID; 20091296; -.
DR VEuPathDB; FungiDB:H310_14246; -.
DR eggNOG; KOG2605; Eukaryota.
DR OrthoDB; 691582at2759; -.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd22752; OTU_OTUD5-like; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR12419; OTU DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12419:SF4; OTU DOMAIN-CONTAINING PROTEIN 5; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS50330; UIM; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 172..300
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
SQ SEQUENCE 453 AA; 51115 MW; B1450287A9EC04DE CRC64;
MGLDPVAQVE GNEDAAMLRC NQASEMWRMK LRAHDSVDAQ NPFGTWCSAQ VVEATPQSVV
IRYHGMNSHW DERLPRDSAR LASSSTHARN DNLPIALGTP VHVFDNSSWR EAHVTCVCVD
HVRVLPTDSP TEVWLPFTPH SITPSEKQRT RRILHSNSCF EHYVHALRQI NMRLFAVDGD
GNCLFRAVSH QLYGDDRHHG IVRRFCMDYM ELQQSFFEPF IVGDMTAFQR YVRYKRQDAV
WGDDPELQAI CELYDRPAQV FAYDASAGAK RLRVFHDTQT RPPICLSFYG GGHYDSVVGP
SHRANLLADE PGAYEARKIA LAQHKQWSDE EASVLELSRK EFGGSTMTLE AALAASCEAY
DAEVAKRIDV AAIETVRAES ELHQLQNEML QCVAKQSEEE LLQAALEASM DPYQDELEVA
LALSTNGMDA YAIDAFDEEE AEMQRAIQMS MLQ
//
