ID A0A087V959_BALRE Unreviewed; 698 AA.
AC A0A087V959;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE Flags: Fragment;
GN ORFNames=N312_02021 {ECO:0000313|EMBL:KFO09151.1};
OS Balearica regulorum gibbericeps (East African grey crowned-crane).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO09151.1, ECO:0000313|Proteomes:UP000053309};
RN [1] {ECO:0000313|EMBL:KFO09151.1, ECO:0000313|Proteomes:UP000053309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO09151.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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; KL484500; KFO09151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087V959; -.
DR MEROPS; C64.004; -.
DR Proteomes; UP000053309; 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; 2.
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 ANK repeat {ECO:0000256|ARBA:ARBA00023043};
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:UP000053309};
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 6..36
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 87..116
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 152..181
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 421..582
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 41..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO09151.1"
FT NON_TER 698
FT /evidence="ECO:0000313|EMBL:KFO09151.1"
SQ SEQUENCE 698 AA; 79915 MW; 43169737044E960F CRC64;
KCTMTERGIK WACEYCTYEN WPSAIKCTMC RAQRPSGTII TEDPFKSGSS DIGRDWDPTS
TEGGSSPLIC PDSSARPRVK SSYSMESANK WSCHMCTYLN WPRAIRCTQC LSQRRTRSPT
ESPQSSGSGS RPVPFSVDSC EEYNDRNKLN TRAQHWTCSV CTYENWAKAR KCVVCDHPRP
NNIEAIELAD TEEASSIINE QDRARWRGSC SSGNSQRRSP PTTKRESDVK MDFQRIELAG
AVGSKEELEV DFKKLKQIKN RMKKTDWLFL NACVGVVEGD LAAVEAYKSS GGDIARQLTA
DEVRLLNRPS AFDVGYTLVH LAIRFQRQDM LAILLTEVKV TEQIRREIAA SLHQRKGDFA
CYFLTDLVTF TLPADIEDLP PTVQEKLFDE VLDRDVQKEL EEESPIINWS LELGTRLDSR
LYALWNRTAG DCLLDSVLQA TWGIYDKDSV LRKALHDSLH DCSHWFYTRW KEKKESWYSQ
SFGLHFSLRE EQWQEDWAFI LSLASQPGAS LEQTHIFVLA HILRRPIIVY GVKYYKSFRG
ETLGYTRFQG VYLPLLWEQS FCWKSPIALG YTRGHFSALV AMENDGYGNR GAGANLNTDD
DVTVTFLPLV DSERKLLHIH FLSAQEIGNE EQQEKLLREW LDCCVTEGGV LVAMQKSSRR
RNHPLVTQMV EKWLDRYRQI RPCTSLSDGE EDEDDDDE
//
