ID A0A1S3JY83_LINUN Unreviewed; 1483 AA.
AC A0A1S3JY83;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=LOC106177185 {ECO:0000313|RefSeq:XP_013415343.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013415343.1};
RN [1] {ECO:0000313|RefSeq:XP_013415343.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013415343.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_013415343.1; XM_013559889.1.
DR STRING; 7574.A0A1S3JY83; -.
DR EnsemblMetazoa; XM_013559889.1; XP_013415343.1; LOC106177185.
DR GeneID; 106177185; -.
DR KEGG; lak:106177185; -.
DR InParanoid; A0A1S3JY83; -.
DR OrthoDB; 3060821at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 3.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF35; UBIQUITINYL HYDROLASE 1; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}; Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 115..1364
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 1020..1065
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1412..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1483 AA; 163606 MW; 8026FDFCB93610AE CRC64;
MTAAEDNKLA VDPTPDAPET SHQGSPPSPL TPNTAIPLPY YTESVNTVTV PKAQHNNSPD
PNNEPLSKSL YLPPSVELLP SYYPPGHQSS PQAQGEGKDA CSKDVKDSSA TPGVCGLRNL
GNTCFMNSGL QCVLSNPYLV KFFVENYVQG KSLTEDNTLT GKFCHLLHKV WCGQFSGIYP
LDFKEILGMY HPQFRDFRQH DCQEFLALLL DTLHEQLNVA SPQNNTTRAA KLSTEEGVTT
SNAGAGVAVN QQIKCSNVDP VSMETNIVHD TMETEPATMD TMETNTDQSS DAIRDDQSDV
TDAGTNQSDL MTDNQSDITE IGTEGDQLDA MVEDTDRLVA AHSQSQSPVD SLSHLHSEDS
NHSSASLQSS DSHKLLENSS YRMQAVPEDI KKRALTESPS LDPKSVTMIT DPSLSNNKLE
KNVISNNKAH SIRLVGLEEM YMKDTKTKNV NVLAKEFMVE EVQTDSEKFA KHDNRQHEQE
MAQNTLDEEM MEVEKHTPKR IKMTNIFRDL DGDGYAQHNK ANNEGDDNSI NNIKRIKIEE
ERHKGHKTRQ LKRKVITAKN PTRDLDLEMD QSDQGSPMAS EEGAWGVSPE EASNSDHVIG
TDLKNTVASK NESLEHHRYV EAAEKSWKEY LSQNKSVIVD TFQGQFKSTV ICEECQHISV
TFEPFMYLSV PLPRAMERQI IVTYVASESK HPVRYCLTLF KGDCIRKLKE GLRTMIGLDE
SCDLIIAEVL ENHVARIVDE NTMLRYLNDH NRKVYAFEMP PAPQFDDIST ENNDISTETG
DVTPVMNNTA PLRAGVSMAG CSSGGGDVFA NMGYWGLQAP HNKASAAQGR APSEDSSDVR
WDDPIPSTST AYRESDVRDN SAVNKGTDSD LWPTTEESKP LNWDPDDIEN QNYFSPSGTV
SGGGVWQGSQ GDLDGDSKDM EGGPSLDSGF GLQRNPLDVT SDAIWGAFPS SATGAGDDSN
ATWGSDDNNS RSGDFSSGPD VWKGSASPED CRNCGDSVDN DSLAPKTSCI NLSTQQWKTC
AICLEEMVDS ELLVHLSCGG TLCQPCLEMS FKHYGEAALN CPVCSCAVKP AEDFVVLSSV
GDGGPNVRIL SMPVLYRYDQ VDPSDGEVKM TLFGHPNILY VPSDLTADRL YDLVDRTAPF
IGTYSLLLTD GQGYRCARCM FTDHCRGCEI PREGEVHFAP SDHLAVRYTE ISQDQLDTAL
HCLDHKSMEL LRPNRPLTLF ECFEAFTESE VLDEHNPWFC PCCKRNQCAR KSMTVWSLPD
TLVVYLKRFV FHERTSTKID TKVSFPVEDL DLSTFISGPQ THDLTFDLHA CVCHFGGVTA
GHYTAYSKHP QLNRWSYYND ELVTEQRPTE DDYSNAYILF YQRKGTLVNF RKPVPPPLTL
VTSKVGPDLQ MVPYQPITQE TISRILDDLA RDGQKRDDAR PKDVGTSTDD LGSERGSKDA
VVGDDRPGRG IAAGSDSRTK TGGGTYGEGD AEPVGGGAVE GLE
//
