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Database: UniProt
Entry: A0A6I8U821_AEDAE
LinkDB: A0A6I8U821_AEDAE
Original site: A0A6I8U821_AEDAE 
ID   A0A6I8U821_AEDAE        Unreviewed;      1864 AA.
AC   A0A6I8U821;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   18-JUN-2025, entry version 20.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   Name=5572946 {ECO:0000313|EnsemblMetazoa:AAEL027340-PA};
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159 {ECO:0000313|EnsemblMetazoa:AAEL027340-PA, ECO:0000313|Proteomes:UP000008820};
RN   [1] {ECO:0000313|EnsemblMetazoa:AAEL027340-PA, ECO:0000313|Proteomes:UP000008820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL027340-PA,
RC   ECO:0000313|Proteomes:UP000008820};
RG   Aedes aegypti Genome Working Group (AGWG);
RA   Matthews B.J.;
RT   "Aedes aegypti genome working group (AGWG) sequencing and assembly.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AAEL027340-PA}
RP   IDENTIFICATION.
RC   STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL027340-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};
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DR   FunCoup; A0A6I8U821; 1951.
DR   EnsemblMetazoa; AAEL027340-RA; AAEL027340-PA; AAEL027340.
DR   EnsemblMetazoa; AAEL027340-RB; AAEL027340-PB; AAEL027340.
DR   EnsemblMetazoa; AAEL027340-RD; AAEL027340-PD; AAEL027340.
DR   EnsemblMetazoa; AAEL027340-RE; AAEL027340-PE; AAEL027340.
DR   EnsemblMetazoa; AAEL027340-RF; AAEL027340-PF; AAEL027340.
DR   EnsemblMetazoa; AAEL027340-RG; AAEL027340-PG; AAEL027340.
DR   EnsemblMetazoa; AAEL027340-RI; AAEL027340-PI; AAEL027340.
DR   InParanoid; A0A6I8U821; -.
DR   OrthoDB; 265776at2759; -.
DR   Proteomes; UP000008820; Chromosome 3.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:TreeGrafter.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR   CDD; cd00051; EFh; 1.
DR   FunFam; 3.90.70.10:FF:000080; Ubiquitin carboxyl-terminal hydrolase 15; 1.
DR   FunFam; 3.10.20.90:FF:000218; Ubiquitin carboxyl-terminal hydrolase 32; 1.
DR   FunFam; 3.90.70.10:FF:000132; Ubiquitin carboxyl-terminal hydrolase 32; 1.
DR   FunFam; 1.10.238.10:FF:000444; Ubiquitin carboxyl-terminal hydrolase 6/32; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR050185; Ub_carboxyl-term_hydrolase.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF76; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 32; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF00443; UCH; 2.
DR   Pfam; PF25265; USP32_N; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008820}.
FT   DOMAIN          265..300
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          301..336
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          424..609
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          791..1826
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1100..1157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1273..1318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1448..1495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1100..1124
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1277..1289
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1452..1463
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1464..1495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1864 AA;  207752 MW;  B012C4C161EF1D56 CRC64;
     MGAKDSRPSC ISYEDAVKRV TDPELRRIKD AFKRSAGTSG TVLSKSAFVQ DVLGDGVPTV
     VADWLYAACG GTPKGITFKE LLCGLVLLTK GTQEEKIRFL WNLYCNESGT HILKQEFLKA
     IQIETAYQSN VLNTSTIGSS SISNSSSNPI NNNNNQVIVS KNNSLPKYTV ALFGLNDRVT
     FEQFKSWIQI YKGATVLSKW LLQDACVNLS SELETPTFYQ SLAGVTHLEE QDIGDLEKVF
     WLLKGLALTG QLDLESLGPL ISPPVPKAAL GGVFLAFDEN HDGHIDFKEL CCGVSAACRG
     PNVERSKFCF KVFDIDRDGV LNFGEVGKMV DILLFVAKET NAACYKNLTS KQMMGELYQR
     ANELCMGSSE TVRECVTIPD PLPEFRFTQE DFLIWSIESN INLVQPFLDL LFEVCHIVLG
     LRPQCKHLEG DIVKGWLARE VRRGYKVGQF WYLISSDWWH HWSQYTQPST NSSCVHCKIA
     SSYAISRNNA ASAVTGVDEA MICDESFTSN STESMGDLLN TGDSSSLGSG SSGISCGRHP
     GGPPGMIDNQ SLIAPILYKQ IPTLTGEGGR LKRDLTLVQH RDFELVPDSL WKALSQWYGG
     PLPLPRQVIQ PLSTGDVELE LYPLNLRILR HQIPSPQQQQ NSNSAWSNIS GGYGALTSGS
     YSNTSASNVL QPPKKYLAYT AAFSRLATVK QVAEFLCQRL KLRVEDIRLW HLAPTPNGVT
     EFPYLLEEDN NTLQELSISD NDQLLLEIRN KDLTWPEELG SLTIAHSNSH NNLERRGTIA
     SIQSQHPPGA TGLHNLGNTC FMNAALQVLF NTQPLTQYFI RQMHMYELNM ANKLGTKGQL
     AMRYAELLRE VWTASQRSIA PLKLRFCVTK HAPQFSGGGQ HDSQELLDWL LDALHEDLNR
     VMEKPYSELK DSDGRADVVV AAEAWNQHHA RNQSIIVDLF YGQLKSKVTC TGCGRDSVRF
     DPFSLLSLPL PVENYTYCEV LVTMLDGSVP VKYGLRLNSE MKYWDLKKQL SDLCALDPEL
     MLICELSNSQ IRCILANEKK IEPSTACELY VYELPKFDNI LVRSRAGSEL AINIEKGLKD
     IQRTPALLLP SIEPSQLTTT SLNTTISSSS NSSSTTVDDT VAITGRRSGP GDNPTKVGTG
     SGGAANRKAS GTATTNATTT TASKVSRCFG NTLCMPPNML CFKNIPEISA SPDSTFIFSE
     TTQYGASSYA MNTQYKDQNR KTVSTTNLLN NVDNSWNASA VGHDEQDTPC NDCDIIYNGH
     GTMEGDSGPF PYADVGHHHH LHQHHHHHQQ QQQHQHGDSF SLSAIKRPPS AGSGSASGMY
     HQQKGNYLIA VHRKLSRQDT YFLSHHKSRP GLFGVPLLIP CYDGVTNKEL YCSVWLQVAR
     LLSPLPPTPP DQSNHATDCD DSLGYDFPFT LRAVASGGRI CALCPWSRFC RGCEIPCNDE
     PLLQGLTYSG RSSSNNSTPN LSSREQTPTF RRKTYGSSTT SSLDGMQSSP TPSMRSINTN
     NIQIAIDWDP TALHLRYQST RERLWTEHES VAICRKQQTE PVDLDHCLRA FTSEEKLEQW
     YHCSHCKQKK PATKKLQIWK LPPVLIVHLK RFNFVNNKWV KSQKVVNFPY DEFDPTPYLA
     SVPQETILRH KELLEGGGTY DGRNHDCHDE IVEFDREMSM IDEVSDEVSI SSITGTIGHV
     SDDEDERGQQ VDINSITPAI IGTQPVVTVR QDDDSPSKAK GRLSIKSKGQ RKRLVSSSLT
     KTPVIDGQFT DFHKHHLKSE RDPFDLKYQL YAAVCHSGML NGGHYISYAA NPNGSWYCYN
     DSSCREIPTR PKIDPSTAYL LFYERRDLDY DPYLPKVDGR QIPPEHLAEF EESENELKKM
     CTLM
//
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