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Database: UniProt
Entry: G1KHK7_ANOCA
LinkDB: G1KHK7_ANOCA
Original site: G1KHK7_ANOCA 
ID   G1KHK7_ANOCA            Unreviewed;       899 AA.
AC   G1KHK7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   24-JAN-2024, entry version 84.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
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:ENSACAP00000008111.3, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000008111.3, ECO:0000313|Proteomes:UP000001646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000008111.3,
RC   ECO:0000313|Proteomes:UP000001646};
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:ENSACAP00000008111.3}
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,
CC         ECO:0000256|RuleBase:RU366025};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP4 subfamily.
CC       {ECO:0000256|ARBA:ARBA00037971}.
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DR   AlphaFoldDB; G1KHK7; -.
DR   STRING; 28377.ENSACAP00000008111; -.
DR   MEROPS; C19.010; -.
DR   Ensembl; ENSACAT00000008283.4; ENSACAP00000008111.3; ENSACAG00000008007.4.
DR   eggNOG; KOG1870; Eukaryota.
DR   GeneTree; ENSGT00940000156645; -.
DR   HOGENOM; CLU_001060_7_1_1; -.
DR   InParanoid; G1KHK7; -.
DR   TreeFam; TF106276; -.
DR   Proteomes; UP000001646; Chromosome 2.
DR   Bgee; ENSACAG00000008007; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 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; IPR028135; Ub_USP-typ.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF45; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 4; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF14836; Ubiquitin_3; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU366025};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          259..872
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          599..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..634
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   899 AA;  100817 MW;  576823DACF96EB51 CRC64;
     MAAAEAGFEG GGGGGSSGGA TASPRPDAGT QRTELTPLLG APLCPGESCR WPPNGLALDS
     ETQTLKEHLI DELDYVLVPT EAWNKLVNWY GCIEGQKPIL RKVSHLLKIH GVRCFFFFSA
     TIEKEMRKQF NIPDGKEIRL WSRYMSNTYE QLSKLDSTIQ DAGLYQGQVV LIEVKNEDGS
     WPRQSSQTKS STATSRNLAT SSKSSAGSCS SVVASSAITN GDSNNSYGLN SSHGKGGSSF
     SCNFYNNRES SPQSQPGLCG LSNLGNTCFM NSALQCLSNT PPLTEYFLED EYEAEINQEN
     PLGMRGEIAE AYAELIKQMW SGRYTHVAPR IFKVTFGHPV VLDFNSQKSQ LASSCWELWE
     LKSKIPGGPK NFHLNSELML YRAYGCEQYV NHRLRNDSII VDIFHGLFKS TLVCPKCSKV
     SVTFDPFCYL TLPLPMKKDR TMEVLFVFAD PQRKPSQCRV VVPMMGGVTD LCDALSQLSG
     IPAENMVVTD VYNHRFHKIF QMDEGLSNIM PKDNIFVYEI SKPAEDGAEC VTLSIYFREK
     KARQSSATPA TVLYGQPLLI AVPKHKLTLD YLYSVILERI GRYVKIPSKE DCPDVCSDNE
     TCNGSNSVSE GEVEEMEHQN GEEENKEKIL ETDASQSEDG TQVESGKEGL HHRKRLFTFS
     LVNSYGTSEI NSLPTEGKIL KLSSHATVAI DWDSDTRKLL FDEHEAQAFE KHCSMFQPQK
     RKTAVALRDC IELFTTMETL GEHDPWYCPN CKKHQQATKK FDLWSLPRIL VVHLKRFSYN
     RYWRDKLDTV VEFPIRDLNM SEFVCDPAAS PYVYDLIAVS NHYGGMGVGH YTAYAKNKIN
     GKWYYFDDSS VSPASEEQIV TKAAYVLFYQ RRDDKLQRNP SPCTNTKMKS EECDGMDTN
//
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