ID A0A084WM55_ANOSI Unreviewed; 605 AA.
AC A0A084WM55;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=ZHAS_00019351 {ECO:0000313|EMBL:KFB51299.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB51299.1};
RN [1] {ECO:0000313|EMBL:KFB51299.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC019351-PA}
RP IDENTIFICATION.
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,
CC ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family. UBP8 subfamily.
CC {ECO:0000256|ARBA:ARBA00038490}.
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DR EMBL; ATLV01024388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE525351; KFB51299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084WM55; -.
DR STRING; 74873.A0A084WM55; -.
DR EnsemblMetazoa; ASIC019351-RA; ASIC019351-PA; ASIC019351.
DR VEuPathDB; VectorBase:ASIC019351; -.
DR VEuPathDB; VectorBase:ASIS019796; -.
DR OMA; QRDQWFK; -.
DR Proteomes; UP000030765; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF33; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 22; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000030765};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 23..121
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 158..600
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 304..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 67096 MW; 7C83CB447D93608E CRC64;
MGDVGCSHFA TYIKEFGYDS FTVVHAYFSA CIGKEARRRK ALSCLCHKCG GSGPQLFSCL
HCIYFGCKGA HINEHYKLTK HFMALELCYG MLYCYQCRDF IYNSECQAIA ERHLRREARS
LNKSLSWRPW SPSKLEIELL LKNPKRRHVT AYSSIGLRGL LNLGSTCFMN CIVQALIHTP
LLRDYFLAEL HECTSKTAAK CLVCEVSRLF QEFYSGARGP LSLHRLLHLI WNHARHLAGY
EQQDAHEFFI ATLDVLHRHC KISMTELAAN VAAAAAAEKS QQQPQNQHSN ANFHLPQGSL
QQQLLQQSTS NAQSLPSTTT GAQPMAPNAT NATPADPNPA QCNCIIDQIF TGGLQSDVVC
QACNGVSTTI DPFWDISLDL GESSNSQGYG GPPKSLIDCL ERFTRAEHLG SSAKIKCNTC
KSYQESTKQL SMRTLPIVAS FHLKRFEHSS LIDKKISTFI SFPSELDMTP FMSQKKSDQQ
QNPLPGGADR KASSHSTDNV GANGSSTTAT MAGASSSQGD EDRGSNGGGN GSQHSRDTAD
FRYSLYAVIN HVGTLDAGHY TAYVRHQKDI WVKCDDHIIT TATLKQVLDS EGYLLFYHKK
ILEYE
//
