ID A0A154PAP6_DUFNO Unreviewed; 1290 AA.
AC A0A154PAP6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 47 {ECO:0000256|ARBA:ARBA00026136};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Ubiquitin thioesterase 47 {ECO:0000256|ARBA:ARBA00029910};
DE AltName: Full=Ubiquitin-specific-processing protease 47 {ECO:0000256|ARBA:ARBA00032453};
GN ORFNames=WN55_09173 {ECO:0000313|EMBL:KZC08270.1};
OS Dufourea novaeangliae (Sweat bee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Halictidae; Rophitinae; Dufourea.
OX NCBI_TaxID=178035 {ECO:0000313|EMBL:KZC08270.1, ECO:0000313|Proteomes:UP000076502};
RN [1] {ECO:0000313|EMBL:KZC08270.1, ECO:0000313|Proteomes:UP000076502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0120121106 {ECO:0000313|EMBL:KZC08270.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KZC08270.1};
RA Pan H., Kapheim K.;
RT "The genome of Dufourea novaeangliae.";
RL Submitted (JUL-2015) 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};
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DR EMBL; KQ434846; KZC08270.1; -; Genomic_DNA.
DR RefSeq; XP_015430037.1; XM_015574551.1.
DR RefSeq; XP_015430038.1; XM_015574552.1.
DR STRING; 178035.A0A154PAP6; -.
DR EnsemblMetazoa; XM_015574551.1; XP_015430037.1; LOC107186642.
DR EnsemblMetazoa; XM_015574552.1; XP_015430038.1; LOC107186642.
DR GeneID; 107186642; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000076502; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02659; peptidase_C19C; 1.
DR CDD; cd17039; Ubl_ubiquitin_like; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR045578; USP47_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF702; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 47; 1.
DR Pfam; PF14560; Ubiquitin_2; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF19718; USP47_C; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KZC08270.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000076502};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 147..550
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 449..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1290 AA; 149101 MW; 905C9DAEAF245849 CRC64;
MVLKIETCLI ECHLFGGTKD NCISDVYPLY ETTCVKDLYI HVEKHYQLPP DSFKLYLVST
GKQTDLCGMK DKLMSEIGVD FSDKIYKMKN KCTVLVVNTI DTLTQKETEY DVSTDNSPPV
SPQHTILWGE DDNDDFKCFI KPKTGYVGLV NQAMTCYLNS LLQALYMTPE FRNALYNWEY
ASGAETDEAN SIPYQLQKLF LNLQTSSKSA VETTALTKSF GWNSTEAWQQ HDIQELCRVM
FEALEQKFKN TEQADLINRF YEGKMIDYVK CLECGTEKSR EDTFLDIPLP VRPFDSNVAY
NTVEAALKAF VQYETLEGSN QYHCEKCNKK CDAHKGLKFT KFPYLLTLHL KRFDFDFKTF
HRVKLNDKVT FPNILNLNPF ILSTTNQEFS VSEETVSSVK CDDSSTTDSG TLDHDFNLCE
YSLPNSNCSR NHDLDDDDEG VDVLINDSST SNCTEHNHEN EKNRSSDAVK GPYNYELFSI
MIHSGSASGG HYYAYIKDFR TQEWLCFNDQ NVTQITNDDI QKTYGGGPTR SYYSGACSST
NAYMLMYRQI DPSRNVLPMQ VQDFPNHIQE LLKKMKENED NDRKKGKGDK ICFRKNRRSY
LETSSDDFLL PKRKVNRTIR VEVGCIHPSM DIMVVAPVQI LPTITWAMAT KQCWQTLDVH
GIVSLNKCRL VCYDESRELI VCSYEGLEER TFNSIWNRTE YTLFLDIMNE NQKAEKNQHD
VICTNVCTLD VTEKKITEGP FHVRALPSQT VGEYKRLLSS LFGLPLSEMT VILRGQKTHL
TLLEYDDVKL STIDFSDTID VFVSTMRDNE WKSFLETATS CEIITNYGNY DNVITVRIKI
PKPSEINKEW NIPSLDVKSK DTDKPIDDSP SNVNVNDSHR STSPKRNEVL KIDKGNEDVP
PKTASPQLGE VEEWNTPEQS NSEDSSLSDS DKTLVGDAPD DEFQVPYFQY TKTLSVDILN
PICMEQWDCD DDDKEHYFKV TDSEYLKLEV ARRMKYSTFK KKLERYVGVP SEYFKIFHNS
RDLDDLECDS LQEKLVFYKE DQILHVKIGR FFEFKTAIYQ LRPNPDEIYK FLGEWIFCKD
MTVAEAKKEI LADIKRKHDI DIPFERCRLR KKFTELPATV YVNDQKLEDL QLYSNTEMVI
QKLPDKDPFT SSSQVIVRVQ KYIAGRTLCG SFQEIVVDGK SIKEIRKKLS EISDIPEEHI
EIVKIDSEMP VFPALDIDEN TVWYGYDSDV EFKLDNETGL LYRDNRHNWD LPKPMRRDDY
SLRIQEFGRA VVNHSSRKDT ALRIHLTTTE
//
