ID A0A093FYF1_DRYPU Unreviewed; 1591 AA.
AC A0A093FYF1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE Flags: Fragment;
GN ORFNames=N307_14171 {ECO:0000313|EMBL:KFV61823.1};
OS Dryobates pubescens (Downy woodpecker) (Picoides pubescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Dryobates.
OX NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV61823.1, ECO:0000313|Proteomes:UP000053875};
RN [1] {ECO:0000313|EMBL:KFV61823.1, ECO:0000313|Proteomes:UP000053875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV61823.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL214799; KFV61823.1; -; Genomic_DNA.
DR STRING; 118200.A0A093FYF1; -.
DR MEROPS; C19.044; -.
DR Proteomes; UP000053875; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 3.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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:SF76; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 32; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR PRINTS; PR00450; RECOVERIN.
DR SMART; SM00695; DUSP; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000313|EMBL:KFV61823.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053875}.
FT DOMAIN 213..248
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 249..284
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 354..568
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 717..1554
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 987..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV61823.1"
FT NON_TER 1591
FT /evidence="ECO:0000313|EMBL:KFV61823.1"
SQ SEQUENCE 1591 AA; 179968 MW; A4529E02A5EAECEB CRC64;
SLNTVTDIEL KRLKDAFKRT CGLSYYMTQQ CFIREVLGDG VPPKVAEVIY CSFGGISKGL
HFNNLIVGLV LLTRGREEEK AKYIFSLFSN ESGSYVVREE MEKMLHVVDG KVPESLKKCF
SESEKVNYEK FRVWLLHNKD AFTFSRWLLS GGVYVTLTDD SDTPTFYQTL AGVTHLEESD
IIDLEKRYWL LKAQSRTGRF DLETFAPLVS PPIHPSLSEG LFNAFDENRD NHIDFKEISC
GLSACCRGPL AERQKFCFKV FDIDRDGVLS RTELKDMVVA LLEVWKDNRT DKIPELGMDL
SDIVEDILNM HDTTKLGHLT LEDYQIWSVK SALANEFLNL LFQVCHIVLG LRPATPEEEG
QIIRGWLERE SRYGLQPGHN WFLIAMPWWH QWKEYVKYDA NPVVIEPSSV LNGGKNSLVA
AAASEQGEEK MGGLNNFSAS EEKFSDNIST ASEASETTSS NALYPGTPGT DVCFARQHNT
SDNNNQCFLG ANGNNLLQLN PQKPGAIDNQ PLVTQEPVKA ASLTMEGGRL KRSPQLIEGK
DYVMVPEPVW RALYHWYGAN LSLPRPVIKN SKTNVPELEL FPRYLLFLRQ QPATRTQQSN
IWVNMGNVPS PNAPLKRVLA YTGCFSRMQT IKEIHEYLSQ RLRIKEEDMR LWLYNSENYL
TLLDDEDHRL EYLKIQDEQH LVIEVRNKDM SWPEEMSFIA NSSKIDRHKV PTEKGATGLS
NLGNTCFMNS SIQCVSNTQP LTRYFISGRH LYELNRTNPI GMKGHMAKCY GDLVQELWSG
TQKNIAPLKL RWTIAKYAPR FNGFQQQDSQ ELLAFLLDGL HEDLNRVHDK PYVELKDSDG
RPDWEVAAEA WENHLRRNRS IVVDLFHGQL KSQVKCKTCG HISVRFDPFN FLSLPLPMDS
YMHLEITVIK LDGTTPVRYG LRLNMDEKYT GLKKQLSELC GLKPEQILLA EVHSSNIKNF
PQDNQKVRLS VSGFLCAFEI PIPGSPTSAS SPVQTDVSTG PSANGTPNIM MNGDLPKPTL
IPNGMPNTVV PCGTERNHTS WTPNGHLPSL SDSPCTGYII AVHRKMMRTE LYFLSSQKNR
PSLFGMPLIV PCTVHTRKKD LYDAVWIQVS RLASPLPPQE ASNHAQDCDD SMGYQYPFTL
RVVQKDGNSC AWCPWYRFCR GCKIECTEDR ACVGNACIAV DWDPTALHLR YQTSQERIVE
EHESVEQSRR AQAEPINLDS CLRAFTSEEE LGEDEMYYCS KCKTHCLATK KLDLWRLPPI
LIIHLKRFQF VNGRWIKSQK IVKFPRENFD PSAFLVQRDP NHLQRKQLTF QLDSLPEPRT
LPGEPRKIDL QITYTAGEGD SLNRSPSSLN TAVLNNIKAS PSLGRKSGTS CPSSKNSSPN
SSPRTLGRGK GRLRLPQLGK NKLSSSKENL DASKENGTDQ EQRLTADQGD ALSRGQILSG
SQGELYTAQD SEATLANGYI CEQSAYSNGS VNGQADNQSE DDTADDQRDE VCVNPIYNLY
AISCHSGIMG GGHYVTYAKN PNNKWYCYND SSCKELHPDE IDTDSAYILF YEQQGVDYAQ
FLPKIDGKKM ADTSSMDEDF ESDYKKYCVL Q
//
