ID A0A452H3G5_9SAUR Unreviewed; 1607 AA.
AC A0A452H3G5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000008962.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000008962.1}
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 STRING; 38772.ENSGAGP00000008962; -.
DR Ensembl; ENSGAGT00000010295.1; ENSGAGP00000008962.1; ENSGAGG00000007083.1.
DR Proteomes; UP000291020; 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; 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; 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; 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 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:UP000291020};
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..585
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 734..1570
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1323..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1607 AA; 182483 MW; 21CAD7401A1C0055 CRC64;
MGAKESRIGF LSYEEALRRV TDVELKRLRD AFKRTCGLSC YMSQQCFIRE VLGDGVPPKV
AEVIYCSFGG TSKGLHFNNL IVGLVLLTRG RDEEKAKYIF SLFSNESGSY VVREEMERML
HIVDGKIPDS LKRCFFEGEK VNYEKFKNWL LQNKDAFTFS RWLLSGGVYV TLTDDSDTPT
FYQTLAGVTH LEESDIIDLE KRYWLLKAQS RTGRFDLETF GPLVSPPIHP SLSEGLFNAF
DENRDNHIDF KEISCGLSAC CRGPLAERQK FCFKVFDVDR DGVLSRTELK EMVVALLEVW
KDNRTDKIPE LGMNLSEIVE DILDAHDTTK LGHLTLEDYQ IWSVKSALAN EFLNLLFQVC
HIVLGLRPAT PEEEGQIIRG WLERESRYGL QPGHNWFLIA MQWWQQWKEY VKYDANPVVI
EPSSVLSGGK NSLVATAIHT SEQREDKTGG LNYFSVTEEK FSDNISTASE ASETTSSSFL
YSSTPAADIC FARQHNTSDN NNQCLLGSSG NILLQLNPQR PGAIDNQPLV TQEPVKAASL
TLEGGRLKRS PHLIEGRDYK MVPEPVWRAL YHWYGANLAL PRPVIKNSKT GVAELELFPR
YLLFLRQQPA TRTQQSNIWV NMGNVPSPSA PLKRVLAYTG CFSRMQTIKE IHEYLSQRLR
IKEEDMRLWL YNSENYLTLL DDEDHMLEYL KIQDEQHLVI EVRNKDMSWP EEMSFIANSS
KIDRHKVPTE KGATGLSNLG NTCFMNSSIQ CVSNTQPLTQ YFISGKHLYE LNRTNPIGMK
GHMAKCYGDL VQELWSGTQK NIAPLKLRWT IAKYAPRFNG FQQQDSQELL AFLLDGLHED
LNRVHDKPYV ELKDSDGRPD WEVAAEAWEN HLRRNRSIVV DLFHGQLRSQ VKCKTCGHIS
VRFDPFNFLS LPLPMDSYMH LEITVIKLDG TTPVRYGLRL NMDEKYTGLK KQLSELCGLK
PEQILLAEVH SSNIKNFPQD NQKVRLSVSG FLCAFEIPVP GSPTSASSPV QTDLSTGPSA
NGMLNIMMNG DFPRPTLIPN GMPNTIVPCG TENNFANGMM NGHMSLLSDS PFIGYIIAVH
RKMMRTELYF LSSQKNRPSL FGMPLIVPCT VHTRKKDLYD AVWIQVSRLA SPLPPQEASN
HAQDCDDSMG YQYPFTLRVV QKDGNSCAWC PWYRFCRGCK IECAEDRAYI GNAYIAVDWD
PTALHLRYQT SQERIVEEHE SVEQSRRAQA EPINLDSCLR AFTSEEELGE DEMYYCSKCK
THCLATKKLD LWRLPPILII HLKRFQFVNG RWIKSQKIVK FPRENFDPSA FLVQRDPSHC
QRKQLTPQVD DLSEPRILQG EPKKTDLQNT YTSGEGDVLN RSPSSFNTSS ILNNIKASPS
PGRKSGTSCP SSKNSSPNSS PRTLGKGKGR LRLPQIGKNK LSNSKENLDA RKENGTDQDQ
KLTSDQGDAI SKGHVLGGSQ SELFIFQDEM TLANGYICEQ NAYSNGSING VIDNHNEEDI
TDDQREVCFN PIYNLYAISC HSGIMGGGHY VTYAKNPNNK WYCYNDSSCK ELHPDEIDTD
SAYILFYEQQ GVDYAQFLPK IDGKKMADTS SMDEDFESDY KKYCVLQ
//
