ID A0A182QNK9_9DIPT Unreviewed; 790 AA.
AC A0A182QNK9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Anopheles farauti.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF013782-PA, ECO:0000313|Proteomes:UP000075886};
RN [1] {ECO:0000313|Proteomes:UP000075886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AFAF013782-PA}
RP IDENTIFICATION.
RC STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF013782-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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; AXCN02000343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182QNK9; -.
DR STRING; 69004.A0A182QNK9; -.
DR EnsemblMetazoa; AFAF013782-RA; AFAF013782-PA; AFAF013782.
DR VEuPathDB; VectorBase:AFAF013782; -.
DR OrthoDB; 2909231at2759; -.
DR Proteomes; UP000075886; 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; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 2.
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 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 47..76
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 114..144
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 262..291
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 539..697
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 88309 MW; BFE4E0F980234C7B CRC64;
MSGSSSTNKP DQQEQETEQS QLRQYQQHSL QQAQDETQQE QHCSSQQQPK WVCEYCTYEN
YPLSLKCIMC KGSKPLLKED IFRLSPTQQL SATNRSNPNL ASGAVKLTTI TETDSNQRWP
CTACTYLNLP HTRRCLQCDT VRKDDLIPMQ RQPSPPRRVI TSENDSISDQ LNAMNICRSA
SPGDDSGLVT ACGTGGSGGK RNRNNSPASG ASFGSGSRLA TNVNDGEPGG KGCASDTKHS
PSPVSSSPGS TIGRAVASSP VNTGKWFCSV CTYENWPKSL KCSMCLHPRD SSASGIVMGS
CGKTTHQQAA AKASPDHDEN NSINVASNIM VNNKRNQQFM GHADSMNNMD ACKQERYLQL
LRRQPDWDWL NACVGIAENN IGAVEAYLEC GGDPSRALTS AEAFLISRNN CAFDVGHTLI
HLAIRFHRDE MLPLLLAQIS GSGPGIKRVP AYVAPDLASD IRRHFAQSLR IRKVASFNCQ
FVNEHATFSL PADIEELPLV LQEQLYEELL DKDAQKQLEM APPALNWSLE ITDRLGSRLM
VLWNRSAGDC LLDSVLQATW GVFDRDNTLR RALADSLHQC SHVFYPRWKE NELFQAALLQ
YTVAEIQLEK DWNTLLSLAS HPGSSLEQLH IFALAHIMRR PIIVYGVKYV KSFRGEDIGF
ARFEGVYLPL LWEQSFCITS PIALGYTRGH FSALVPTEPY SRIDATRDDR EDITFLPLMD
CEMKLLPVHF LTKNEIGREE MVLRQWLEVC ETEGGLLVAQ QKLHKRPLLV AQLLEEWLNH
YRRIAISRLF
//
