ID A0A2I0LG36_PUNGR Unreviewed; 907 AA.
AC A0A2I0LG36;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=CRG98_000201 {ECO:0000313|EMBL:PKI79386.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:PKI79386.1, ECO:0000313|Proteomes:UP000233551};
RN [1] {ECO:0000313|EMBL:PKI79386.1, ECO:0000313|Proteomes:UP000233551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AG2017 {ECO:0000313|Proteomes:UP000233551};
RC TISSUE=Leaf {ECO:0000313|EMBL:PKI79386.1};
RA Akparov Z., Amiraslanov A., Hajiyeva S., Abbasov M., Kaur K., Hamwieh A.,
RA Solovyev V., Salamov A., Braich B., Kosarev P., Mahmoud A., Hajiyev E.,
RA Babayeva S., Izzatullayeva V., Mammadov A., Mammadov A., Sharifova S.,
RA Ojaghi J., Eynullazada K., Bayramov B., Abdulazimova A., Shahmuradov I.;
RT "De-novo sequencing of pomegranate (Punica granatum L.) genome.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal
CC Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC precursors as well as that of ubiquitinated proteins.
CC {ECO:0000256|RuleBase:RU366025}.
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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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:PKI79386.1}.
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DR EMBL; PGOL01000006; PKI79386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0LG36; -.
DR STRING; 22663.A0A2I0LG36; -.
DR Proteomes; UP000233551; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02661; Peptidase_C19E; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 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 PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000233551};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..907
FT /note="Ubiquitin carboxyl-terminal hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016340026"
FT DOMAIN 183..487
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 584..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 907 AA; 99561 MW; CE2AC66B65A64DE5 CRC64;
MTKIPLWVFV GFNILSLFAP LFPPLSLAEA EKALCFPTRT PITPLTPADR SHGEIIPSFR
SRIGRESQLL IASLMAANAQ EVVAGSDSNP DFKSSFQGGS SIKYFEKKIE FVPARKPFNG
LTYSGGDFKI ETLNPGGPDR SSGQGSVQAA ANGKVKKGDG SEVFDGWLDP ELTLGVSFQR
IGAGLENLGN TCFLNSVLQC LTYTEPLAAY LQSGKHQNSC RINGFCALCA IQKHVSRTLK
ATGRILAPKD LVANLRCISR NFRNARQEDA HEYMVNLLES MHKCCLPSGV PSESPGAYEK
SLVHKIFGGR LRSQVKCMQC NNCSNKFDPF LDLSLEIAKA ESLPKAIRHF TAPEQLDGGE
RQYQCQKCKQ KVRALKQLTI HKAPYVLTIH LKRFHSHDPG QKINKNVSFD TTLDFKPFVS
GPYEGDLKYS LYGVLVHHGW STHSGHYYCY VRTSTNMWYS LDDNQVRQVS ESTVLQQKAY
MLFYVRNRNS TPRKPFEIAQ KEKSRENNHT GNRTSSFAFS QSSSCTVQVS QLADKCSTAV
TSSSSVITKD AISVSSVKEL QVSEPVSMES RKLGTALNAS LENKINNSDA SGESTKESTI
SKGLVENGAG KENESEIAGK VSNGSASDKI DCGSSASNAS QKSSQEEEAT APLVEKTAGA
VQDESHLLTG SSTMSSGSLQ GETIDSKASK KLKKKPIKYQ LTSAHFGANI LLRASLGVRK
KRMKRKHRVT EKDRMSCDLG PSTSDVSESV VSVQRRSVKS LTKKGTDKRA KREEMNTNGG
SQKDIVNAGT KVIENVKDCK SDAMENGLMS MLTRGLEETL VAHWDGIDLS PSPTIESPNA
GNPNGGNAIG YVLDEWDEEY DRGKRKKVRH SKHDFGGPNY FQEIASQKIK SKEARFDQFA
GNRPLRI
//
