ID A0A2B4RU97_STYPI Unreviewed; 1264 AA.
AC A0A2B4RU97;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Ubiquitin carboxyl-terminal hydrolase 8 {ECO:0000313|EMBL:PFX21181.1};
GN Name=USP8 {ECO:0000313|EMBL:PFX21181.1};
GN ORFNames=AWC38_SpisGene14356 {ECO:0000313|EMBL:PFX21181.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX21181.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
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:PFX21181.1}.
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DR EMBL; LSMT01000288; PFX21181.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4RU97; -.
DR STRING; 50429.A0A2B4RU97; -.
DR EnsemblMetazoa; XM_022941941.1; XP_022797676.1; LOC111335935.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd02674; Peptidase_C19R; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR015063; USP8_dimer.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF104; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR SUPFAM; SSF140856; USP8 N-terminal domain-like; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:PFX21181.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706}.
FT DOMAIN 788..820
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 921..1253
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 124..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1264 AA; 139001 MW; 940E34D19FD666C7 CRC64;
MPSSAKKKVK DLHLASNLEE LNKIADPGLP VDRNANPTPY IKSADKVYLK AQDNDLDGDE
EYAYVYYMRY FKIISLIKKS VKYSGNKKYF DNLLGKNKII KSIERAEALQ GSLRKRYEKL
KTQQDAEAKA QEEAKQKEEE DKKKLAALKA RNDSDSGFES DVDSRLNGNG ISSSSEVYNK
LKVSHNSILT PEMSENDSGA LISGLESPAS SFVTDGVKCI SAQELYNLIK VSEFKILILD
CRPHAKFTEN WIQCSCCINI PAELLDQGVS VGSIERRLPE LTRKAWNRRG EKEFVILMDE
STKVSEITPE CRIQRLKDVI FTYDSYSSLK HEPVFLDGGF HSWLWHYPSL AMKPELPMVR
SQPKSVTPVD LSSLDYPELP EDKILIPQST VTKPTSSPLQ YPSIPNADLQ NMLGPKDSTE
QNKASSPAQA EFSSNVPSPG QPGIIPSGAA WNHGPGAKFR QLGIHPAVPP SQPPSDIGLP
RPADAGSLQH EAPKREPMNL PPTQSVSSSE GSPLPSVGPQ SSVGIVPQAV NPSSADLRTT
GPVPKTMVPH SSSQPIFQPN VPSTAPKTVP STQPSSQSSV VVAKPFPKPS VPFTGSSNTP
TAQPGTPPKQ PSNLKSNLQP STSIPGTQPS NVNSIPSPVT PATSVQVTPV ISTLPSPQVS
GVVSPPHPNN VSQQVTQRVE PQNQPSVSPL VSQVPHISHA SISTSQSHQV TTTSIPGADA
RNINSTAVKP SAAAQSGSPQ HSLQGPMQNK TSRPYTTVGK DSASSAPPNI SDSSQQPDSR
PSNFFTSPGL PHGWEKVIEQ NRTYYKDHNT QTTHWNPPTT GKGDVTPQSG AQRQQQQPPV
KRQSSVERPK LHRSNSSPNL AKIKDQGPSG PKKPIIDRLS KPESGQKGQT RPVVNRVAKP
LSANQLDSFN PSYGGPGIGL TGLRNLGNTC YMNSVVQCLS SVAPLAKYFM SGVFREDINR
SNRDGTRGEL AESFSVLIRV LHSGQYKCVS AGEFKRTVGK FKSQFSGYDQ HDSQELLAFL
MDGLQEDLNK VKVKPYLKAP GDDLDPQTAA DMAWENHKKR NESIMVELFD GLFMSTVQCM
VCSKESRTFD SFSNLTLPLP PHKSQCTLED CLKLFTKPEK MAGDDKWFCP KCRQRREASK
RIQIWKLPRI LVVHLKRFQY EGMWRQKLQT GVNFHMDQVD MSAFVVGPKS ATRCYNLHAV
SNHYGTMHGG HYTAFAKNVY DKKWYKFDDQ YVTEMSPRDV VTSAGYLLFY TSIDFPPPTF
NFKS
//