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Database: UniProt
Entry: E2B062_CAMFO
LinkDB: E2B062_CAMFO
Original site: E2B062_CAMFO 
ID   E2B062_CAMFO            Unreviewed;       682 AA.
AC   E2B062;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Ubiquitin carboxyl-terminal hydrolase 20 {ECO:0000313|EMBL:EFN60919.1};
GN   ORFNames=EAG_06030 {ECO:0000313|EMBL:EFN60919.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN60919.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC       perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008269}.
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DR   EMBL; GL444408; EFN60919.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2B062; -.
DR   STRING; 104421.E2B062; -.
DR   InParanoid; E2B062; -.
DR   OMA; LCSVICH; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.2230.10; DUSP-like; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF86; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF06337; DUSP; 2.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00695; DUSP; 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51283; DUSP; 2.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Hydrolase {ECO:0000313|EMBL:EFN60919.1};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00502};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00502};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00502}.
FT   DOMAIN          6..115
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          409..504
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          512..612
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   REGION          154..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          647..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..286
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   682 AA;  77549 MW;  4F856F4FC5754470 CRC64;
     MPLVVRNCPH LANRGDLAFI EALMTREERF AKCSDCDISG PNLWLCLFPD CRWVGCAETH
     LDHSTIHNQT YPTHCAHMNL STKRIWCYAC KSEAIAKHVP SPPLSPTQVE FKTMGNKFAG
     DAPGGSESKL DGLDRLMFDK FYGDWVANRI NSEKGNSFNE RSDSPDSTDS DESKDFSGKP
     RGIRTVHPMF RGYHQHDTQE FLRCFMDQLH EELKEHIEDD RDVQLRLKGL GDHSSEDEDE
     AEIDGNASSQ SDAEYETCDS GVSEQSSLSD EGERGTKRRY SRVSQTEKLR NKFTNRNLKK
     SNMEPAFAPP QRSPQNSPAK HRTKKQMKTR SIISDTFDGK LLSSVQCLTC DRISTRIETF
     QDLSLPIPSR DHIDMLHQGS LTPQKAGPCS DVVYVTNQSG WLSWFLQWMR SWFWGPVTME
     LMEISSRELS DLNFFVSRQW INRFNTFSEP GPIDNSDFLC PHGGVIPVRA HFVDKISMPI
     PQAVWEYLYN AFGGGPACTH LYECPICEEK YESLQKRRQY EMELFQRLNH TTDNHTAIYA
     LAMAWLRQWQ SFVRGKETQP PGPIDNNSIV VNKNGQNSLK VGSDYGQIPE ELWQFFLTTY
     GGGPELMLHS CQRPVPTQPN VSIHSVSNPN LIDSNLKCNR IEAKSNKLTT TRSSETISQQ
     DSAIESLLSS SDSHQTQRDV SE
//
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