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Database: UniProt
Entry: A0A401RFN1_CHIPU
LinkDB: A0A401RFN1_CHIPU
Original site: A0A401RFN1_CHIPU 
ID   A0A401RFN1_CHIPU        Unreviewed;      1092 AA.
AC   A0A401RFN1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=USP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=chiPu_0017401 {ECO:0000313|EMBL:GCC16953.1};
OS   Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC   Chiloscyllium.
OX   NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC16953.1, ECO:0000313|Proteomes:UP000287033};
RN   [1] {ECO:0000313|EMBL:GCC16953.1, ECO:0000313|Proteomes:UP000287033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(2018).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GCC16953.1}.
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DR   EMBL; BEZZ01001278; GCC16953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401RFN1; -.
DR   STRING; 137246.A0A401RFN1; -.
DR   OMA; TCNKESA; -.
DR   Proteomes; UP000287033; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   CDD; cd22265; UDM1_RNF168; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR015063; USP8_dimer.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR048498; WW_USP8.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF27; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 8; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF08969; USP8_dimer; 1.
DR   Pfam; PF20625; WW_USP8; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   SUPFAM; SSF140856; USP8 N-terminal domain-like; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000287033}.
FT   DOMAIN          201..323
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          752..1083
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          124..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..144
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..592
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..617
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1092 AA;  125429 MW;  3B0D80486ADBC650 CRC64;
     MPAVSSDLKE LYLSTCLADL NKKAEVKLET KSTKNYVTSA CKIFKAAEEC RLDRDEEKAY
     VLYMKYLTVY DLIRKRTDFK HQQDYYLSLL GPANFRKAIE EAERLSESLK LRYEEAEVRK
     KLEENERLQE EKRKQQEEAK SKGYDNNLKT TTKSSSDCFG IKKRNLKEDF EVNDKKTHSE
     CNDSLQGAVT AEKLFAMMQD ENTEMIIMDA RSSKDYQDSH MQVARSHCIS VPEEAVSPGI
     TVNQIELKLP EESKEIWQKR QFVDYIILLD WDSSVHQVKR GTILQSLKDA LYKWDSQIIL
     RSEPLVLEGG YDSWLLCYPM YTTNAKVTVP KKEPPGAVQV SLNFSYPSLE EPPQPSKDLN
     ESKAVQELEI FNEHLSLLEE TPKKVNLKTI NVPNGILAPG VPVTGQPVAM KTIPQIDRTK
     KPSLKQSNRS LSKSEVVGAD SLPVHNGPVI PDRSTKPCIE SQNSLTDEER NQIHAEAALI
     GEKARKEREQ RERRQEEERK EKERLERLRE EERREKEQCE EEEKEFKTKA DQEREPKENE
     EQRAQEIEDN QQKEEAERKG LAEQKKTSPE KGKIESQIRD QADTRKSGEQ SVSELEGLRG
     TNLEKQEHRD TLTRARSEEM GRTVPGLPQG WMKFLDVVTG TYRYYHSPTN SVHMYPPEMV
     PSITPPATPP THKAKPQTAK DVDVPKLKRS FSSPDIAQAI QEEQNKATTK IVPTVNRETK
     PSGYSKTEIS SPSASQIRNL NPVYGGMGRA LTGLRNLGNT CYMNSILQCL SNTPHLAEYF
     NKNFYQQDIN RSNILGHKGE VAEEFGVIMK SLWSGQYKYI SPRDFKGRIG KINDTFAGYV
     QQDSQELLLF LMDGLHEDLN KADRKRYKEE NTDSLDDTRA ADLAWQKHKL LNESIIVALF
     QGQFKSTVQC LTCHKRSRTF EAFMYLSLPL PSSSKCSLQD CLKLFSKEEK LTDNNRFHCS
     NCKAHRDSTK KLEIWKLPPI LLVHLKRFSY EGRWKQKLQT NVDFPLENLD LFSYLIGPRS
     NVKRYNLFAV SNHYGGLDGG HYTAYCKNAV KQRWFKFDDQ DVSEISPSSV RSPAAYILFY
     SSLELRVVDL AT
//
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