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Database: UniProt
Entry: J9HYY6_AEDAE
LinkDB: J9HYY6_AEDAE
Original site: J9HYY6_AEDAE 
ID   J9HYY6_AEDAE            Unreviewed;       666 AA.
AC   J9HYY6;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=AaeL_AAEL017004 {ECO:0000313|EMBL:EJY57700.1};
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|EMBL:EJY57700.1, ECO:0000313|Proteomes:UP000682892};
RN   [1] {ECO:0000313|EMBL:EJY57700.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:EJY57700.1};
RA   Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA   Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA   Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA   Rogers Y.-H., Kravitz S., Fraser C.M.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EJY57700.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Liverpool {ECO:0000313|EMBL:EJY57700.1};
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
RN   [3] {ECO:0000313|EMBL:EJY57700.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:EJY57700.1};
RG   VectorBase;
RL   Submitted (SEP-2012) 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};
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DR   EMBL; CH477461; EJY57700.1; -; Genomic_DNA.
DR   RefSeq; XP_011493395.1; XM_011495093.1.
DR   AlphaFoldDB; J9HYY6; -.
DR   STRING; 7159.J9HYY6; -.
DR   PaxDb; 7159-AAEL017004-PA; -.
DR   VEuPathDB; VectorBase:AAEL017004; -.
DR   eggNOG; KOG1864; Eukaryota.
DR   HOGENOM; CLU_412339_0_0_1; -.
DR   PhylomeDB; J9HYY6; -.
DR   Proteomes; UP000682892; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02663; Peptidase_C19G; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR24006:SF944; RE52890P; 1.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          9..59
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          322..663
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          433..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   666 AA;  75818 MW;  6421F5E57C9BBFD8 CRC64;
     MSKLVKNPNG HCKLCTNKDS MDNMVECDDC DRWYHLSCAK LDRSPTAEES WICEHCADIQ
     RKWYKQGAAA IEKKIATQKQ TENKSPNSNE QILQELTNAI TNNSSSKSTL DRSFPNWGKR
     RTIDEEEAKA IRDKTPQNKR VKTNSSNSLG KIMLATTTLL SIANAINIKP IEEDGLIFDH
     EGTCLLKRGS WKTNIYTGIS PAQDINFIDH VHQNLTIALK EMERQTKDQT IHQLATSIGH
     QCDDAIQEIQ QITRKRRSKG IFGFLKDIFF GGDDIDEAVE AMRIQEDNKI HHVSETVQKG
     ANVSQLERDI GADQFPPNEH YFGLVNFGNT CYSNSVLQAL YFCRPFREKV LEYKAKNKRT
     KETLLTCLAD LFYSIATQKK KVGSIAPKKF IARLRKEKEE FDNYMQQDAH EFLNFLINHI
     NEIILAERNQ AKGAGTSGSK NAGTIGGGGG SLNGDNPGQP QEPTWVHEIF QGILTSETRC
     LNCETVSSKD ENFFDLQVDV DQNTSITHCL RCFSNTETLC SDNKFKCDNC CSYQEAQKRM
     RVKKLPMILA LHLKRFKYME QYNRHIKVSH RVVFPLELRL FNTSDDAVNP DRLYDLMAVV
     IHCGSGPNRG HYISIVKSHG FWLLFDDDMV DKIEASTIED FYGLTSDIQK SSETGYILFY
     QSRDAT
//
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