ID A0A0J7KWP2_LASNI Unreviewed; 828 AA.
AC A0A0J7KWP2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=RF55_4871 {ECO:0000313|EMBL:KMQ94947.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ94947.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ94947.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ94947.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) 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 -!- 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:KMQ94947.1}.
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DR EMBL; LBMM01002347; KMQ94947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7KWP2; -.
DR STRING; 67767.A0A0J7KWP2; -.
DR PaxDb; 67767-A0A0J7KWP2; -.
DR OrthoDB; 5397179at2759; -.
DR Proteomes; UP000036403; 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:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 2.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
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 Pfam; PF00443; UCH; 1.
DR SMART; SM01052; CAP_GLY; 2.
DR SUPFAM; SSF74924; Cap-Gly domain; 2.
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:KMQ94947.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000036403};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 467..822
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 828 AA; 94636 MW; B8D44F411D8B7BC2 CRC64;
MEDRDGSKEH RVLQHYIAKQ DTVLIRIYGA CVVNVNELRV GMLVEALEDL KESVLKVRVI
DTIGGSKIWC GTEWRCHKYD LIPVSPKIWQ YLLTVQSPQE RIRIANDEAL CERIRNISVN
DRVLYCSDSS NRRAKEIALV RYIGSVKQLG LGHYFGLELL ESQEVSKTSV LAKEYFISTH
SNANVTFATV NNIYPYKAES DTISGNIEKT FLKSNTGTDY TNDKKRSVHL LDSTPAVLLE
QFTLFDDNKN NNQESVNILK ERHQAAKSNL ENNVNNYTKS NDHSLFKCAE LQNIPIFVLE
HKWSSDIESN VYSDVEDARS IDLLDYSNAL EKNEIEKFKV ENKGDLMVGS TVKVLLDSDI
HYGVIRWIGT PSGISPGKLM AAVELDDGHP LGTDGTYKDV KYFHCRPYRA IFTDIEHCSH
YENTKLNEQP ALTNNDNFGN MESSVIAGLV RPISVKGDLE SICGKYRGIQ GHHNSCYLDA
TLFSMFTFTS VFDNLLFRPP NEKDCPQYEE VQRVLREEIV NPLRKNMFVR ADRVMKLRTL
LEKLSSVSGL TSEEKDPEEF LTSLVAQILN AEPFLKLSSG QDAYHYQLFV EKDDHLNLPT
VQQLLEQSFL TSNIRLKEVP SCLIIQMPRF GKSFKMYQKI QPTLLLDVTD IIEDSPRQCT
VCGKLAEFEC KECYGQCGVG LESIAFCLQC LEKVHRHERR FNHEPKKLIV PMEFAILQEH
CPVPRLYLEL SAVVCIETSH YVSFVKCGPG SEAPWCFFDS MADRKGEQNG YNIPEMVPCP
DFPYWLSEEG GNYLIELTDD RHLPEHAKRL LCDAYMCMYQ SPDVMMYK
//