ID A0A1R2BA62_9CILI Unreviewed; 812 AA.
AC A0A1R2BA62;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=SteCoe_27604 {ECO:0000313|EMBL:OMJ73668.1};
OS Stentor coeruleus.
OC Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ73668.1, ECO:0000313|Proteomes:UP000187209};
RN [1] {ECO:0000313|EMBL:OMJ73668.1, ECO:0000313|Proteomes:UP000187209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM001 {ECO:0000313|EMBL:OMJ73668.1};
RA Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA Sood P.;
RT "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT introns.";
RL Submitted (NOV-2016) 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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMJ73668.1}.
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DR EMBL; MPUH01000805; OMJ73668.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R2BA62; -.
DR OrthoDB; 1423057at2759; -.
DR Proteomes; UP000187209; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR044635; UBP14-like.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR43982:SF6; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 2-RELATED; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000187209};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 25..442
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT COILED 264..298
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 812 AA; 94675 MW; 69C821DFDC2BB1A5 CRC64;
MNIYRGSIFE PMSISQNKRD CGMPQGLRNV GNTCFMNSLL QCYFMIPPLV KEVMMASFDN
DYQTNGYYAK FVRALQMLFA SMIKSTRKYA DPSNLIDTLL DSFGNQVQFG DQQDIGEFHM
IIVENIVKGL HACKQVQGMI LWKSLKEQGK IESLFTGVNA EILSYKENNE KTIIQKDVKF
GPIILGIEEG DLMSSWKSAS KNIIKDYKIM NKNTTAKQEI WIQNLPSVLI FQLKRHFFIE
GDPTPLKSNA CFKFPDVIYP DRFMLQYKDQ IKELKKSAKS LHSEINQLKK QKSTLQYDLN
GKTSILDSLK VIKDFLSTES GKKISSESAL LYEKLEILSN EIQKKILDID NKIQEISQQL
DDIYSNFKNN KYCLNSILIH EGAAISGHYY AFIKDFDQPE YLQWRKYNDI IVTNVSQEEV
RKTSEGFNDS LSSAYCLMYV REELVKPQTD LPLHLFNPGS EMEFSDEYST FLKEDAINYY
KNMNENDELN RENIIMEEQV SRILEDFNQL YTADLATFNK MNVMKKKYYH LELVNCAVYI
MSIPNCAHLA KYFRLDNYMW KTFRKTLTDS SMRKLKDKLR EKMAGYGLPD VSLKEADLNN
YSRIYKLYTE EFTDLIYANE ILTQICENNL KFSLKIYAIC ILQSERGQNS IRTELHEIFK
SVLVYMVMSL YNMCKNKNIS EVIEICECIN LIFYNFSSQT IGKGVLSLIN QIKVAFIKDF
NDTKKEFEQA LFNSVCEEVN DLTLIKYYSQ VEAYQHSLVG YDFFNTYHYE DVDRYQKLCN
TLTSEYLKQG IQLVLKIESS KTITLQQLNS KY
//
