GenomeNet

Database: UniProt
Entry: H9GF73_ANOCA
LinkDB: H9GF73_ANOCA
Original site: H9GF73_ANOCA 
ID   H9GF73_ANOCA            Unreviewed;       669 AA.
AC   H9GF73;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000009257.3, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000009257.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000009257.3};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000009257.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) 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   AlphaFoldDB; H9GF73; -.
DR   STRING; 28377.ENSACAP00000009257; -.
DR   Ensembl; ENSACAT00000009450.4; ENSACAP00000009257.3; ENSACAG00000009302.4.
DR   eggNOG; KOG1870; Eukaryota.
DR   GeneTree; ENSGT00940000158829; -.
DR   HOGENOM; CLU_004896_0_0_1; -.
DR   TreeFam; TF352179; -.
DR   Proteomes; UP000001646; Unplaced.
DR   Bgee; ENSACAG00000009302; Expressed in adrenal gland and 10 other cell types or tissues.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 2.
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; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF13; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 20; 1.
DR   Pfam; PF06337; DUSP; 2.
DR   Pfam; PF00443; UCH; 2.
DR   SMART; SM00695; DUSP; 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 2.
DR   PROSITE; PS51283; DUSP; 2.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001646}.
FT   DOMAIN          1..440
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   DOMAIN          442..535
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          544..647
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   REGION          70..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          137..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   669 AA;  74908 MW;  1E9A55BB06DB2E68 CRC64;
     RTDKKPALCK SYQKLVSEVW HKKRPSYVVP SSLSHGIKLV NPSFRGYAQQ DTQEFLRCLM
     DQLHEELKEP VAAEVRDLEA SEADDKREGD RSPSEDEFLS CDSGSSDRGE GDGQAGKAGG
     TGMPEAELLI QDEAGRGISE KERLKDRKFS CSHQRSHSEQ VDEDADVDTS VETGTEGRAS
     PDILQPPTPR PASPARTPGI SLVCSPCWID LLFSLFPQVS TTVETFQDLS LPIPGKEDLA
     KLHSAIYQNV PAKTGSCAGD NYAASQGWIA FIVEYIRRFV VSCIPSWFWG PVVTLEDCLA
     AFFAADELKG DNMYSCERCK KLGFEVLQVP LLLSQILCIH LKRFRHEVMY SFKISSHVSF
     PLEGLDLRPF LAKESASQVT TYDLLSVICH HGTAGSGHYI AYCQNVINGQ WYEFDDQYVT
     EVHETVVQNA EAYVLFYRKS SEEAVRERQK VVSLATMKEP GLLQFYISRE WLNKFNTFAE
     PGPITNHTFL CSHGGIPPNK YHYIDDLVVI LPQNVWEYLY NRFGGGPAVN HLYVCSVCQV
     EIEALAKRRK MEIDTFIKLN KAFQAEESPG VIYCISMQWF REWEAFVKGK DNEPPGPIDN
     SKIAVAKGSG HVQVKPGADY GQISEETWIY LSTLYGGGPE IAIRQNVAQV QEVETLHGEQ
     KIEAETRAA
//
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