ID A0A087ST49_AUXPR Unreviewed; 844 AA.
AC A0A087ST49;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=APUTEX25_001861 {ECO:0000313|EMBL:RMZ57661.1}, F751_4067
GN {ECO:0000313|EMBL:KFM28903.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM28903.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM28903.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM28903.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
RN [2] {ECO:0000313|Proteomes:UP000279271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 25 {ECO:0000313|Proteomes:UP000279271};
RX DOI=10.1016/j.algal.2018.07.001;
RA Vogler B.W., Starkenburg S.R., Sudasinghe N., Schambach J.Y., Rollin J.A.,
RA Pattathil S., Barry A.N.;
RT "Characterization of plant carbon substrate utilization by Auxenochlorella
RT protothecoides.";
RL Algal Res. 34:37-48(2018).
RN [3] {ECO:0000313|EMBL:RMZ57661.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 25 {ECO:0000313|EMBL:RMZ57661.1};
RA Hovde B., Zhang X.;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:RMZ57661.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 25 {ECO:0000313|EMBL:RMZ57661.1};
RA Vogler B.W., Starkenburg S.R., Sudasinghe N., Schambach J.Y., Rollin J.A.,
RA Pattathil S., Barry A.N.;
RT "Characterization of plant carbon substrate utilization by Auxenochlorella
RT protothecoides.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal
CC Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC precursors as well as that of ubiquitinated proteins.
CC {ECO:0000256|RuleBase:RU366025}.
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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KL662184; KFM28903.1; -; Genomic_DNA.
DR EMBL; QOKY01000126; RMZ57661.1; -; Genomic_DNA.
DR RefSeq; XP_011401952.1; XM_011403650.1.
DR STRING; 3075.A0A087ST49; -.
DR GeneID; 23615458; -.
DR KEGG; apro:F751_4067; -.
DR eggNOG; KOG1870; Eukaryota.
DR OrthoDB; 653068at2759; -.
DR Proteomes; UP000028924; Unassembled WGS sequence.
DR Proteomes; UP000279271; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
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:0000256|RuleBase:RU366025, ECO:0000313|EMBL:KFM28903.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000028924};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 24..157
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 208..778
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 92182 MW; 49240A9E8620ED89 CRC64;
MHTEEESEME GEPIVDQGGG TTLPEPGKQA EAIKTTEAKC REASVKPGLK TFLVGNRWFT
AWCQHTGFTY NEARQRVSII RPSSPGPNPG PIDNSDLLAE CQHPAQSTLD EEEAAGVTTL
RSGLVEKKHF WALCEPTWEL LKGWYGVAGP EIVREYMQVG LNRSRVEMDP GQLHVKVVRE
ANESAGLERK SAVIAISELG SARRRGLTGL GNLGNTCFMN SSVQCLAHTV PVLEVFLSGV
YKKDCNADNP LGLGGKLALA FGGLVGKLWL PGASHVNPKH FKWQLSKFAP QFQGYAQQDS
QELLAFLLDG LHEDLNRIRV KPYVEEGDAD GRPDAELAAE AWRAYRARND SVIVDHFQGM
YKSTLVCPQC GHQSVKFDPF MYLSLPLPGP RTQDFRVTVL SMDGGAEPRQ YSVTLPKTGS
VGITYSTVLP PAVLFLSTED LEGLKLARIE SSTIGPEGSD NVLSAALLRS LRHGIDELLD
AVEDAELVAE PIQDGDMEMQ VDGGDAADAG PQVVPIIKAE DEGAPFDMFA AQAREPEVSM
AGESLDGCAS QIFTLKLANA EGRVRYSLIG DDAVPPALPT KDPLCFLAEW SSSAARQYGK
GRWDTPAKHR SVLEAEQAAH KPAPPLRLQS CVEAFLQMEQ LDAEDSWYCS KCKQHVQANK
KLDLWSLPEV LVVHLKRFSY SRASRDKLDT KVEFPLTDLD LGRHILGPAS DGSTPESNKY
DLYAVSNHYG GLGGGHYTAY CKMPDDNLWY LFDDGSVRCV PATEVQSPAA YVLFYRRQGS
KVALQEILED GAGIPIASDM AEVAGPEENG HRPALRASLQ LETIDSDDEL MGDPLHEDLD
ISPA
//
