ID A0A1A6H7T9_NEOLE Unreviewed; 845 AA.
AC A0A1A6H7T9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=A6R68_15105 {ECO:0000313|EMBL:OBS74364.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS74364.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS74364.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS74364.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS74364.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OBS74364.1}.
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DR EMBL; LZPO01044436; OBS74364.1; -; Genomic_DNA.
DR STRING; 56216.A0A1A6H7T9; -.
DR Proteomes; UP000092124; 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 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:SF8; OTU DOMAIN-CONTAINING PROTEIN 7B; 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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000092124};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00451}.
FT DOMAIN 798..833
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT REGION 87..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 845 AA; 92812 MW; 4E8505FE8A6F66BC CRC64;
MDLKESASKE LLQITQVEAW ILIYVLLTSC YQRVLDDPMT LDMDAVLSDF VRSTGAEPGL
ARDLLEGKNW DVSAALSDFE QLRQVHAGNL SPPFSGGSSC SKTPEKGCSD REPTRPSRPI
LQRQDDIIQE RRLSRGISHA SSSVVSLARS HVSSNGGGGG SSEHPLEMPI CAFQLPDLTV
YKEDFRSFIE RDLIEQSMLV ALEQAGMWGF HDRDLVLRKA LYALMEKGVE KEALKRRWRW
QQTQQNKESG LVYTEDEWQK EWNELIKLAS SEPRMHLGTN GASGGGVESS EEPVYESLEE
FHVFVLAHVL KRPIVVVADT MLRDSGGEAF APIPFGGIYL PLEVPASQCH RSPLVLAYDQ
AHFSALVSME QKDSAKEQAV IPLTDSEHKL LPLHFAVDPG KGWEWGKDDN DNVRLASIIL
SLEVKLHLLH SYMNVKWIPL SSDAQAPLAQ PESPTASAGD EPRSTPESGE SDKESVGSSS
TSNGXSRRKD KSKRDREKDK KRADSVANKL GSFGKTLGSK LKKNMGGLMH SKGPKPGGLG
SGSAVGSGTE TLEKKRKNTS LKSWKGGKEE AAGDGPVSEK PSSESVGNGG SKYSQEVMQS
LSIMRIAMQG EGKFIFVGTL KMGHRHQYQE EMIQRYLAEA EERFLAEQKQ KEAERKIMNG
GLVSGPPPAK KPEPDGGEDQ PNDSPAESKA LAFSTGYPGG FTIPRPSGGG VHCQEPRRQL
AGGPCVGSIP PYATFPRQYP PGRPYPHQDS IPSLEPGKDG VHRGALLPPQ FRVADSYSNG
YREPPEPDGW AGGSRGILQT QTKCKQPNCS FYGHPETNNF CSCCYREELR RREREPGGEL
LAHRF
//
