ID A0A1D2NH56_ORCCI Unreviewed; 809 AA.
AC A0A1D2NH56;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=Ocin01_02123 {ECO:0000313|EMBL:ODN04569.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODN04569.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODN04569.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODN04569.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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:ODN04569.1}.
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DR EMBL; LJIJ01000041; ODN04569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2NH56; -.
DR STRING; 48709.A0A1D2NH56; -.
DR OrthoDB; 5397179at2759; -.
DR Proteomes; UP000094527; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR11830; 40S RIBOSOMAL PROTEIN S3A; 1.
DR PANTHER; PTHR11830:SF3; CYLINDROMATOSIS, ISOFORM D; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000313|EMBL:ODN04569.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 341..760
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 147..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 809 AA; 88896 MW; B844314AB6D1A482 CRC64;
MSFKFIVPLD SYYESLFVFV QNSTTMIFAW SLVGMCVCFV GVKVFLLWRS SNKTIIIQNE
KHDGVKKGDR VVWVREPPET NESGVIRWTG VIEGEEIAGI EFDRPLGLGS GWYKNKQLFT
CTAQRGGLVA VAGLILEDDY FYNPEISTKD VEEDTGGQVS PIRGDSSLSA SSGIGSGSGI
HSSPSPSPSS SSSTSLDVGS YDTSSTSSTG SRKKRYNHSA DETSCSTITV SKNTVSDRPK
LYSAERIGQG DIGAGVTTAD GPVVAGPRVS QWTSKASGVL AASTSSYKCP PKTSETIQTD
NNLKQAVVSN GNNNDDSNMP IPFVQAPLRE EDGERISGRS KGIQGHRNSC YLDATLFSMF
SFSGVFDSIL LQEWNGQKDA GDEELARNVQ RILRDDVVNP LRKELYCTAR NVMKLRETMQ
HLDDKLTSEE MDPQEFLQLL FSKVLNLEEF MSLSSGHSDF FHQVLVAQTE EDKNKIPTIQ
QLFEQSLIMQ ELKLKTVPRP ALILQMPRSG NKYKMYDGIL PNLSIDITDL MEDIPRMCII
CGSLATHECP SCYGKFSSGG EARDTAVSPG GSGAESTAFC ETCLHQIHKR RDRQTHLSHI
VPIKYSFDAS QYFSFATPIS PTSTTGHHQH HLNHHLNNAN SGNIPSYLFG ASGSWATSGG
GGTGGFVGGN PNFNRNPSTA PLISSIPSPS YAVSSSRTIP RVTMDLFAVI CIETSHFVSF
VKCGTERQAP WVFFDSMADR VENPNGTGHN IPQVKLLPRM GCWLEELEKS PRNIKEFMSP
DSNMAPELRR LLSDPYICLY YSPQSCMYS
//