ID A0A195CLW2_9HYME Unreviewed; 738 AA.
AC A0A195CLW2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, 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=ALC62_07399 {ECO:0000313|EMBL:KYN01721.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN01721.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYN01721.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYN01721.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN01721.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-2016) 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; KQ977580; KYN01721.1; -; Genomic_DNA.
DR RefSeq; XP_018396540.1; XM_018541038.1.
DR AlphaFoldDB; A0A195CLW2; -.
DR STRING; 456900.A0A195CLW2; -.
DR GeneID; 108774830; -.
DR OrthoDB; 2909231at2759; -.
DR Proteomes; UP000078542; 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:UP000078542};
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 82..111
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 160..189
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 449..608
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 45..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 83542 MW; 6DFAD6276EF30DDD CRC64;
MTSRLEETEQ KWTCEYCTYE NWPSSLKCTM CRGAKPLLGE DIYRLRDPSP QRGSSNVASG
PVSQISPTDN FTSQNYSQNL PSAGKWACSM CTYLNYQNTT RCIQCSNRKP INQSVNSLAS
NLHEHLAPLR LADGPPNSGS NSQLNPSPIN LHPERLYNMH PEKWSCHVCT YENWPKATKC
VMCGHPKEKD RRDKGTQGNV GVILPSPERE HTQRGLPSPP HAPYIHQTQR EDNLAIGRRG
PHRYAESRND SLSTPQSPNN CDYERRLKQL RRHTDWCWLN ACLGIVEGDN TPVEAYLASG
GDPARQLTHS EVLLLNRSSA FDVGHTLVHL AIRFQREDIL ATLLSQIEGS GSGVKRVPSY
VAPDLAVQIR RHVTNSIRLR KGSFPCYFVT DMATFALPAE VEDLPSIVQE QMLEELLDKE
AQQQLEGGGG EPPALNWSLE ITERLGSRLH ALWNRSAGDC LLDSAMQATW GVFDRDNALR
RALADTLQQA GQFFYPRWRE YEASQASRML DFTLEETQWQ EDWESLLATA AQPGSALEQL
HVFALAHILR RPIIVYGVKY VKSFRGEDIG YARFEGVYLP LLWEPSFCIR SPIALGYTRG
HFTALVPIEP YASSRIPPLA THGVVSGNNS PLEQLQIQMQ TTFMPLMDRE HKLLPIHFLT
TDEIGREESI YKEWLDVCRT EGGILVAQQK LHKRPLLVAQ MLEEWLNHYR RLAQTNEAPF
SRPPTLQDYS SDGDTEDE
//
