ID K7G872_PELSI Unreviewed; 934 AA.
AC K7G872;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=OTUD7A {ECO:0000313|Ensembl:ENSPSIP00000016483.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000016483.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000016483.1}
RP IDENTIFICATION.
RG Ensembl;
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase C64 family.
CC {ECO:0000256|ARBA:ARBA00005865}.
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DR EMBL; AGCU01176482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01176483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01176484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01176485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01176486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01176487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006136921.1; XM_006136859.2.
DR RefSeq; XP_014435961.1; XM_014580475.1.
DR RefSeq; XP_014435962.1; XM_014580476.1.
DR RefSeq; XP_014435963.1; XM_014580477.1.
DR AlphaFoldDB; K7G872; -.
DR STRING; 13735.ENSPSIP00000016483; -.
DR MEROPS; C64.002; -.
DR Ensembl; ENSPSIT00000016559.1; ENSPSIP00000016483.1; ENSPSIG00000014649.1.
DR GeneID; 102461860; -.
DR KEGG; pss:102461860; -.
DR CTD; 161725; -.
DR eggNOG; KOG4345; Eukaryota.
DR GeneTree; ENSGT00940000158999; -.
DR HOGENOM; CLU_013263_0_0_1; -.
DR OMA; RCAKQPE; -.
DR OrthoDB; 2909231at2759; -.
DR TreeFam; TF323312; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd22773; OTU_OTUD7A; 1.
DR CDD; cd14347; UBA_Cezanne_like; 1.
DR Gene3D; 1.20.5.4770; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR002653; Znf_A20.
DR PANTHER; PTHR13367:SF9; OTU DOMAIN-CONTAINING PROTEIN 7A; 1.
DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF01754; zf-A20; 1.
DR SMART; SM00259; ZnF_A20; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS51036; ZF_A20; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 200..382
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT DOMAIN 891..926
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT REGION 84..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 104755 MW; 09DB1130232FDDA2 CRC64;
MPCRPPTNPA TAACVAALLH DHMTLDMDAV LSDFVRSTGA EPGLARDLLE GKNWDLTAAL
SDYEQLRQVH TANLPQVFNE GKYYKQQERD SPQQVNKTER PSLQRQDEIA QEKRLSRGIS
HASSAIVSLA RSHVANECNN EQFPLEMPIY TFQLPDLSVY SEDFRSFIER DLIEQATMVA
LEQAGRLNWW STVCTSCKRL LPLATTGDGN CLLHAASLGM WGFHDRDLVL RKALYTMMRS
GAEREALKRR WRWQQTQQNK ESGLVYTEEE WEREWNELLK LASSEPRTHF GKNGGSGGGV
DNSEDPVYES LEEFHVFVLA HILRRPIVVV ADTMLRDSGG EAFAPIPFGG IYLPLEVPPN
RCHCSPLVLA YDQAHFSALV SMEQKDQQRE QAVIPLTDSE HKLLPLHFAV DPGKDWEWGK
DDNDNTRLAN LILSLEAKLN LLHSYMNVTW IRIPSETRAP LAQPESPTAS AGEDVQSLAD
SMDSDRDSVC SNSNGSNGKN CKEKEKDKQR KDKDKNRTDS VANKLGSLSK TLGIKLKKNM
GGLGGLVHGK MNRANSGNGK NGDIMEKGKE KKSKSRKGSK EESGQSASTS PSEKTTPSPT
DKASVSPAEK MNTKSLSDKQ SDAWKYSTDV KLSLNILRAA MQGERKFIFA GLLLTSHRHQ
FHEEMIGYYL TSAQERFNAE QEQKRKEAEK KAVLNGSSCR KLEQESYSKE KLESSPQDRA
SPVLPQSHTT QLVLKFKDRT SPTPGSFSSP SNGAKKSGPV PVSAHYSHTP PVQRQSVIHL
HDVNSKPSSF QDDSYKPVVG TLKTCATYPQ QNRSLSSQSY SPARIAGIRT VNTVESLTYA
LPTEHKSQTF TNGFNTGDIR DCLEYADEEA PQTWLNNDKN RGRSTVCPIY SIQQNRCKKE
NCSFYGRPET ENYCSYCYKE ELKRRERENK GHRH
//
