ID A0A0N0U6P9_9HYME Unreviewed; 711 AA.
AC A0A0N0U6P9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=WN51_10329 {ECO:0000313|EMBL:KOX78521.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX78521.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX78521.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX78521.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX78521.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-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 -!- SIMILARITY: Belongs to the peptidase C64 family.
CC {ECO:0000256|ARBA:ARBA00005865}.
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DR EMBL; KQ435721; KOX78521.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0U6P9; -.
DR STRING; 166423.A0A0N0U6P9; -.
DR OrthoDB; 2909231at2759; -.
DR Proteomes; UP000053105; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd22767; OTU_ZRANB1; 1.
DR Gene3D; 1.25.40.560; -; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 3.
DR InterPro; IPR041294; AnkUBD.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR InterPro; IPR049768; ZRANB1_OTU.
DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR PANTHER; PTHR13367:SF28; UBIQUITIN THIOESTERASE ZRANB1; 1.
DR Pfam; PF18418; AnkUBD; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF00641; zf-RanBP; 3.
DR SMART; SM00547; ZnF_RBZ; 3.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 3.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 3.
DR PROSITE; PS50199; ZF_RANBP2_2; 3.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00322}.
FT DOMAIN 8..37
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 79..108
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 137..166
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 425..584
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 44..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 80553 MW; 842236EA236C67B0 CRC64;
MNSRLEEQES KWTCEYCTYE NWPSSLKCTM CRGAKPLLGE DIYRLRDPSP QRSGSNVASG
PVTHLSPTDS YNLSSQNVPL GKWSCAMCTY LNYQNTTRCV QCGNRKPTGD PPPNSGSNPP
PINLHPERYY NLQANLHPEK WSCLICTYEN WPKATKCVMC GNPKEKDKRD RTTNNVAVIL
PSPERDHSQR NLPSPPHAPY IHQNQRDENL AVGRRNSHRY PDSRNDNLST PQSPNNCDYE
RRLKQLRRHT DWCWLNACLG IVEGDNAPVE AYLASGGDPA RQLTHSEVLL LNRSSAFDVG
HTLVHLAIRF QREDILATLL SQIEGSGSGV KRVPSYVAPD LAAQIRRHVT NSIRLRKGSF
PCYFVTDIAT FALPAEVEDL PSIVQEQMLE ELLDKEAQQQ LEGGGGEPPA LNWSLEITER
LGSRLHALWN RSAGDCLLDS AMQATWGVFD RDNALRRALA DSLQQAGQFF YPRWREYEAS
QASRMLDFTL EETQWQEDWE SLLATAAQPG SALEQLHVFA LAHILRRPII VYGVKYVKSF
RGEDIGYARF EGVYLPLLWE PSFCIRSPIA LGYTRGHFTA LVPIEPYASS RIPPLSSHGG
GNGPLQQLQI QMQTTFMPLM DREHKLLPIH FLSLEEVGRE ESILKEWLDV CRTEGGILVA
QQKLHKRPLL VAQMLEEWLN HYRRLAQTNN APFLRPAVLQ DYSSDGDTED E
//
