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Database: UniProt
Entry: A0A096MCM2_POEFO
LinkDB: A0A096MCM2_POEFO
Original site: A0A096MCM2_POEFO 
ID   A0A096MCM2_POEFO        Unreviewed;      1605 AA.
AC   A0A096MCM2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   Name=USP6 {ECO:0000313|Ensembl:ENSPFOP00000029163.1};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000029163.1, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000029163.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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};
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DR   EMBL; AYCK01010885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01010886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01010887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01010888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01010889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01010890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSPFOT00000027161.1; ENSPFOP00000029163.1; ENSPFOG00000016583.2.
DR   GeneTree; ENSGT00940000155797; -.
DR   OMA; FKADNRR; -.
DR   Proteomes; UP000028760; 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   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
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; IPR029071; Ubiquitin-like_domsf.
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; 1.
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   SUPFAM; SSF54236; Ubiquitin-like; 1.
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:0000256|ARBA:ARBA00022807};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          228..263
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          264..299
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          369..584
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          733..1568
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          440..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1369..1435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1369..1388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1404..1419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1605 AA;  180184 MW;  0456C21B99AA1392 CRC64;
     MGAKESRIGF LSYDEAVKRV TDVELKRLKD AFKRTSGLSC YMTQQCFYRE VLGDGVPPKV
     AEVIYSSFGG SSKGLHFNNL IVGLVLLTRG RDEEKAKYLF SLFASDLSGY AAREDIEAVL
     QALDGEVPSS LKRCFIESDK VNYERFRNWL LQNKEAFTLS RWLLSGGVCV TLTDDSDTPT
     FYQTLAGVTH LEESDIIDLE KRYWLLKAQS RTGRFDLETF VPLVSPPIHA SLSEGLFHAF
     DENRDNHIDF KEISCGLSAC CRGPVAERQK FCFKVFDVDR DGVLSRDELH EMVVALLEVW
     KDNRTDTIPE LHSSVSDIVE EIVKMHDTTK LGHLTLEDYQ IWSVKSALAN EFLNLLFQVC
     HIVLGLRPAT PEEEGQIIRW YLERESRHGL QQGQSWFLIS MLWWQQWKDY VKYEHKDIVV
     EQPSILSSLR PLTVTATVEP AHPDMPGGLG TFGPFSPSEE KSPDAVSSAS EATETALSPQ
     LGPSSAESCF ARQHNISENN NQCFSGANGH LPSQLTAQRP GAIDNQSLVT TDPIKAPTLT
     MEGGRLKRSL QLVPGRDFEM MPEPVWRALY HWYGANLSLP RPVILESKTG QAELELFPRY
     LLFLRQQPAT RSPQSNIWVN MGNVPSPNAP LKRMLAYTGC FSRMATIKDI HLYLSQRLRI
     KEEDMRLWLY NSENYLTLLD DEDHTLESLK IQDEQQLVIE VRNKDMSWPE EMSFIANSSK
     MDRHKVPTEK GATGLSNLGN TCFMNSSIQC VSNTKPLSDY FLSGRHLYEL NRINPIGMRG
     HMAKCYGDLV LELWSGTQKS IAPLKLRWTI AKYAPRFNGF QQQDSQELLA FLLDGLHEDL
     NRVHEKPYVE LKDSDGRPDW EVASEAWDNH LRRNRSIVVD LFHGQLKSQV KCKTCGHISA
     RFDPFNFLSL PLPMDSSMHL EITVIKLDGS TPVRYGLRLN MDEKYTGLKK LLSELCSLKP
     EQILLAEVHA SNIKNFPQDN QKVRLSVNGF LCAFEVPVPG SPTSLSSPTL TGYSPVAADF
     SRTGGLHVQP DITPTAANGH LIANGGLGTL LPSTPETPLV NGVANGHISP LQDSPFIGYI
     IAMHRKMMRT ELYFLSSQKN RPSLFGMPLI VPCTVHTSKK DLYDAVWIQV SRLASPLPPQ
     EASNHAQDCD DSMGYQYPFT LRVVGKDGNS CAWCPWYRFC RGCTIECTED RASVGNAYIA
     VDWDPTALHL RYQTSQERIV EEHCSVEQSR RAQAEPISLD SCLKAFTSEE ELGEDELYYC
     SKCKTHRLAT KKLDLWRLPP ILIVHLKRFQ FVNGRWIKSQ KIVKFPQESF DPSAFLAPRD
     LEHRSLHSRS ESEDLLREIL SLDSQSTPLS AVLSTIVSHL FTLNITSPAS SRRSAPSLSR
     NSSPSGSPKP AGHRPGRLRL PQLSSKHRLS SSKENLDGAA SSEADSRDGA PQADTEERVA
     IAAGAGPVGY SDQAASESSC SREASSSYCD VILMNGDSNG MGSDCSIESN VDPDSSLLQH
     RDMCLDPLYN LYAISCHSGI MGGGHYVTYA KNPNDKWYCY NDSSLEGHEV HSEEIDTDSA
     YILFYEQQGV DYSQFLPKID GKKMADTSSM DEDFESDYKK YCVLQ
//
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