Ubiquitin carboxyl-terminal hydrolase [Caenorhabditis elegans]
ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 1004990)
ubiquitin carboxyl-terminal hydrolase family protein may be a C19 family peptidase that deubiquitinates polyubiquitinated target proteins
List of domain hits
Name | Accession | Description | Interval | E-value | ||||||||
Peptidase_C19B | cd02658 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
320-786 | 5.79e-104 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. : Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 321.96 E-value: 5.79e-104
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zf-UBP | pfam02148 | Zn-finger in ubiquitin-hydrolases and other protein; |
185-266 | 3.64e-17 | ||||||||
Zn-finger in ubiquitin-hydrolases and other protein; : Pssm-ID: 460464 Cd Length: 63 Bit Score: 76.15 E-value: 3.64e-17
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zf-UBP_var super family | cl39301 | Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ... |
19-78 | 1.75e-14 | ||||||||
Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is related to the pfam02148 domain. However, it has an altered pattern of zinc binding residues. The actual alignment was detected with superfamily member pfam17807: Pssm-ID: 407678 Cd Length: 64 Bit Score: 68.39 E-value: 1.75e-14
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UBA1_scUBP14_like | cd14296 | UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ... |
597-634 | 1.76e-12 | ||||||||
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain. : Pssm-ID: 270482 [Multi-domain] Cd Length: 39 Bit Score: 62.26 E-value: 1.76e-12
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UBA_atUPL1_2_like | cd14327 | UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ... |
660-695 | 1.34e-11 | ||||||||
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins. : Pssm-ID: 270512 [Multi-domain] Cd Length: 38 Bit Score: 59.62 E-value: 1.34e-11
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Name | Accession | Description | Interval | E-value | ||||||||
Peptidase_C19B | cd02658 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
320-786 | 5.79e-104 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 321.96 E-value: 5.79e-104
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UCH | pfam00443 | Ubiquitin carboxyl-terminal hydrolase; |
319-785 | 6.49e-46 | ||||||||
Ubiquitin carboxyl-terminal hydrolase; Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 166.46 E-value: 6.49e-46
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zf-UBP | pfam02148 | Zn-finger in ubiquitin-hydrolases and other protein; |
185-266 | 3.64e-17 | ||||||||
Zn-finger in ubiquitin-hydrolases and other protein; Pssm-ID: 460464 Cd Length: 63 Bit Score: 76.15 E-value: 3.64e-17
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zf-UBP_var | pfam17807 | Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ... |
19-78 | 1.75e-14 | ||||||||
Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is related to the pfam02148 domain. However, it has an altered pattern of zinc binding residues. Pssm-ID: 407678 Cd Length: 64 Bit Score: 68.39 E-value: 1.75e-14
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ZnF_UBP | smart00290 | Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
184-245 | 5.50e-14 | ||||||||
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; Pssm-ID: 197632 Cd Length: 50 Bit Score: 66.62 E-value: 5.50e-14
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UBA1_scUBP14_like | cd14296 | UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ... |
597-634 | 1.76e-12 | ||||||||
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain. Pssm-ID: 270482 [Multi-domain] Cd Length: 39 Bit Score: 62.26 E-value: 1.76e-12
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UBA_atUPL1_2_like | cd14327 | UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ... |
660-695 | 1.34e-11 | ||||||||
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins. Pssm-ID: 270512 [Multi-domain] Cd Length: 38 Bit Score: 59.62 E-value: 1.34e-11
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UBA | pfam00627 | UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
602-631 | 1.16e-07 | ||||||||
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280. Pssm-ID: 395502 [Multi-domain] Cd Length: 37 Bit Score: 48.21 E-value: 1.16e-07
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UBP12 | COG5560 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
317-431 | 1.31e-07 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 55.27 E-value: 1.31e-07
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UBA | smart00165 | Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ... |
602-632 | 2.58e-07 | ||||||||
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin. Pssm-ID: 197551 [Multi-domain] Cd Length: 37 Bit Score: 47.48 E-value: 2.58e-07
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Name | Accession | Description | Interval | E-value | ||||||||
Peptidase_C19B | cd02658 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
320-786 | 5.79e-104 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 321.96 E-value: 5.79e-104
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UCH | pfam00443 | Ubiquitin carboxyl-terminal hydrolase; |
319-785 | 6.49e-46 | ||||||||
Ubiquitin carboxyl-terminal hydrolase; Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 166.46 E-value: 6.49e-46
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zf-UBP | pfam02148 | Zn-finger in ubiquitin-hydrolases and other protein; |
185-266 | 3.64e-17 | ||||||||
Zn-finger in ubiquitin-hydrolases and other protein; Pssm-ID: 460464 Cd Length: 63 Bit Score: 76.15 E-value: 3.64e-17
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Peptidase_C19 | cd02257 | Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
320-786 | 7.23e-17 | ||||||||
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239072 [Multi-domain] Cd Length: 255 Bit Score: 80.99 E-value: 7.23e-17
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zf-UBP_var | pfam17807 | Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ... |
19-78 | 1.75e-14 | ||||||||
Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is related to the pfam02148 domain. However, it has an altered pattern of zinc binding residues. Pssm-ID: 407678 Cd Length: 64 Bit Score: 68.39 E-value: 1.75e-14
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ZnF_UBP | smart00290 | Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
184-245 | 5.50e-14 | ||||||||
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; Pssm-ID: 197632 Cd Length: 50 Bit Score: 66.62 E-value: 5.50e-14
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UBA1_scUBP14_like | cd14296 | UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ... |
597-634 | 1.76e-12 | ||||||||
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain. Pssm-ID: 270482 [Multi-domain] Cd Length: 39 Bit Score: 62.26 E-value: 1.76e-12
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UBA1_UBP5_like | cd14294 | UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; ... |
602-639 | 3.64e-12 | ||||||||
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13, is an ortholog of UBP5. It has similar domain architecture, but functions differently from USP5 in cellular deubiquitination processes. It exhibits a weak deubiquitinating activity preferring to Lys63-linked polyubiquitin in a non-activation manner. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA1 domain. Pssm-ID: 270480 [Multi-domain] Cd Length: 44 Bit Score: 61.17 E-value: 3.64e-12
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UBA_atUPL1_2_like | cd14327 | UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ... |
660-695 | 1.34e-11 | ||||||||
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins. Pssm-ID: 270512 [Multi-domain] Cd Length: 38 Bit Score: 59.62 E-value: 1.34e-11
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UBA1_spUBP14_like | cd14385 | UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ... |
603-641 | 8.28e-10 | ||||||||
UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain. Pssm-ID: 270568 [Multi-domain] Cd Length: 47 Bit Score: 54.72 E-value: 8.28e-10
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Peptidase_C19A | cd02657 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
733-786 | 2.20e-08 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239122 [Multi-domain] Cd Length: 305 Bit Score: 56.57 E-value: 2.20e-08
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UBA | pfam00627 | UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
602-631 | 1.16e-07 | ||||||||
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280. Pssm-ID: 395502 [Multi-domain] Cd Length: 37 Bit Score: 48.21 E-value: 1.16e-07
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UBP12 | COG5560 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
317-431 | 1.31e-07 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 55.27 E-value: 1.31e-07
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UBA | smart00165 | Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ... |
602-632 | 2.58e-07 | ||||||||
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin. Pssm-ID: 197551 [Multi-domain] Cd Length: 37 Bit Score: 47.48 E-value: 2.58e-07
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Peptidase_C19L | cd02668 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
727-779 | 3.49e-07 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 52.81 E-value: 3.49e-07
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UBA1_UBP5 | cd14383 | UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ... |
599-639 | 3.31e-06 | ||||||||
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA1 domain. Pssm-ID: 270566 [Multi-domain] Cd Length: 49 Bit Score: 44.66 E-value: 3.31e-06
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UBA_VP13D | cd14306 | UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ... |
602-635 | 3.86e-06 | ||||||||
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required. Pssm-ID: 270491 Cd Length: 36 Bit Score: 43.97 E-value: 3.86e-06
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UBA2_spUBP14_like | cd14297 | UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ... |
659-696 | 1.03e-05 | ||||||||
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain. Pssm-ID: 270483 [Multi-domain] Cd Length: 39 Bit Score: 42.85 E-value: 1.03e-05
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UBA_PUB_plant | cd14290 | UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family ... |
602-640 | 1.26e-05 | ||||||||
UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family includes some uncharacterized hypothetical proteins found in plants. Although their biological function remain unclear, all family members contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal PUB domain. UBA domain, along with UBL (ubiquitin-like) domain, has been implicated in proteasomal degradation by associating with substrates destined for degradation as well as with subunits of the proteasome, thus regulating protein turnover. PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins. Pssm-ID: 270476 [Multi-domain] Cd Length: 49 Bit Score: 42.81 E-value: 1.26e-05
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COG5533 | COG5533 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
733-788 | 1.71e-05 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 47.49 E-value: 1.71e-05
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UBA1_atUBP14 | cd14295 | UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ... |
602-639 | 2.24e-05 | ||||||||
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins; atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain. Pssm-ID: 270481 [Multi-domain] Cd Length: 45 Bit Score: 42.36 E-value: 2.24e-05
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Peptidase_C19G | cd02663 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
732-786 | 3.33e-05 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 46.53 E-value: 3.33e-05
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UBA2_UBP5 | cd14386 | UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ... |
657-697 | 3.35e-05 | ||||||||
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA2 domain. Pssm-ID: 270569 [Multi-domain] Cd Length: 43 Bit Score: 41.55 E-value: 3.35e-05
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Peptidase_C19E | cd02661 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
319-428 | 3.67e-05 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 46.50 E-value: 3.67e-05
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peptidase_C19C | cd02659 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
317-434 | 7.19e-05 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 45.71 E-value: 7.19e-05
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Peptidase_C19E | cd02661 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
728-785 | 1.03e-04 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 44.96 E-value: 1.03e-04
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Peptidase_C19H | cd02664 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
320-429 | 1.40e-04 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 44.79 E-value: 1.40e-04
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Peptidase_C19D | cd02660 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
320-433 | 1.76e-04 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 44.29 E-value: 1.76e-04
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UBA1_atUBP14 | cd14295 | UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ... |
658-697 | 1.76e-04 | ||||||||
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins; atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain. Pssm-ID: 270481 [Multi-domain] Cd Length: 45 Bit Score: 39.66 E-value: 1.76e-04
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UCH_1 | pfam13423 | Ubiquitin carboxyl-terminal hydrolase; |
728-766 | 1.94e-04 | ||||||||
Ubiquitin carboxyl-terminal hydrolase; Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 44.18 E-value: 1.94e-04
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Peptidase_C19F | cd02662 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
320-343 | 2.09e-04 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 43.51 E-value: 2.09e-04
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Peptidase_C19A | cd02657 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
320-420 | 3.80e-04 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239122 [Multi-domain] Cd Length: 305 Bit Score: 43.47 E-value: 3.80e-04
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Peptidase_C19H | cd02664 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
698-786 | 4.84e-04 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 43.25 E-value: 4.84e-04
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UBA_UBXN1 | cd14302 | UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ... |
662-697 | 6.17e-04 | ||||||||
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also called SAPK substrate protein 1 (SAKS1) or UBA/UBX 33.3 kDa protein, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (UBX) domain. It binds polyubiquitin and valosin-containing protein (VCP), and has been identified as a substrate for stress-activated protein kinases (SAPKs). Moreover, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and may be involved in the Ub-proteasome proteolytic pathways. In addition, UBXN1 can associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domain. Pssm-ID: 270487 [Multi-domain] Cd Length: 41 Bit Score: 38.04 E-value: 6.17e-04
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peptidase_C19C | cd02659 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
731-769 | 8.11e-04 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 42.24 E-value: 8.11e-04
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Peptidase_C19R | cd02674 | A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
732-786 | 8.91e-04 | ||||||||
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 41.50 E-value: 8.91e-04
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UBA_UBXN1 | cd14302 | UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ... |
603-637 | 1.11e-03 | ||||||||
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also called SAPK substrate protein 1 (SAKS1) or UBA/UBX 33.3 kDa protein, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (UBX) domain. It binds polyubiquitin and valosin-containing protein (VCP), and has been identified as a substrate for stress-activated protein kinases (SAPKs). Moreover, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and may be involved in the Ub-proteasome proteolytic pathways. In addition, UBXN1 can associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domain. Pssm-ID: 270487 [Multi-domain] Cd Length: 41 Bit Score: 37.27 E-value: 1.11e-03
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UBA1_NUB1_like | cd14291 | UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ... |
658-692 | 1.54e-03 | ||||||||
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called negative regulator of ubiquitin-like proteins 1, renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) which may function in the regulation of cell cycle progression. NUB1 contains three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif. This model corresponds to UBA1 domain. Pssm-ID: 270477 [Multi-domain] Cd Length: 36 Bit Score: 36.66 E-value: 1.54e-03
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UBA_HERC2 | cd14402 | UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ... |
661-697 | 2.15e-03 | ||||||||
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, also called HECT domain and RCC1-like domain-containing protein 2, is a SUMO-regulated E3 ubiquitin ligase that plays an important role in the SUMO-dependent pathway which orchestrates the DNA double-strand break (DSB) response. Moreover, HERC2 functions as a RNF8 auxiliary factor that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. In addition to a ubiquitin-association (UBA) domain, HERC2 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain. Pssm-ID: 270585 Cd Length: 45 Bit Score: 36.58 E-value: 2.15e-03
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UBA2_scUBP14_like | cd14298 | UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ... |
659-695 | 2.91e-03 | ||||||||
UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain. Pssm-ID: 270484 [Multi-domain] Cd Length: 38 Bit Score: 35.90 E-value: 2.91e-03
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UBA2_UBP5 | cd14386 | UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ... |
603-637 | 3.22e-03 | ||||||||
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA2 domain. Pssm-ID: 270569 [Multi-domain] Cd Length: 43 Bit Score: 36.16 E-value: 3.22e-03
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UBA1_UBP13 | cd14384 | UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ... |
602-639 | 3.41e-03 | ||||||||
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13, is an ortholog of UBP5 implicated in catalyzing hydrolysis of various ubiquitin (Ub)-chains. It contains a zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. Due to the non-activating catalysis for K63-polyubiquitin chains, UBP13 may function differently from USP5 in cellular deubiquitination processes. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA1 domain. Pssm-ID: 270567 Cd Length: 49 Bit Score: 36.15 E-value: 3.41e-03
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UBA2_spUBP14_like | cd14297 | UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ... |
603-635 | 3.82e-03 | ||||||||
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain. Pssm-ID: 270483 [Multi-domain] Cd Length: 39 Bit Score: 35.53 E-value: 3.82e-03
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COG5077 | COG5077 | Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
317-439 | 4.09e-03 | ||||||||
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 40.62 E-value: 4.09e-03
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UBA_RUP1p | cd14307 | UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins; RUP1p is a ... |
659-695 | 4.16e-03 | ||||||||
UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins; RUP1p is a ubiquitin-associated (UBA) domain-containing protein encoded by a nonessential yeast gene RUP1. It can mediate the association of Rsp5 and Ubp2. The N-terminal UBA domain is responsible for antagonizing Rsp5 function, as well as bridging the Rsp5-Ubp2 interaction. No other characterized functional domains or motifs are found in RUP1p. Pssm-ID: 270492 Cd Length: 38 Bit Score: 35.73 E-value: 4.16e-03
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UBA_HUWE1 | cd14288 | UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ... |
657-695 | 4.21e-03 | ||||||||
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, also called ARF-binding protein 1 (ARF-BP1), HECT, UBA and WWE domain-containing protein 1, homologous to E6AP carboxyl terminus homologs protein 9 (HectH9), large structure of UREB1 (LASU1), Mcl-1 ubiquitin ligase E3 (Mule), upstream regulatory element-binding protein 1 (URE-B1), or URE-binding protein 1, may function as a ubiquitin-protein ligase that involves in the ubiquitination cascade that targets specific substrate proteins in proteolysis. It can ubiquitylate DNA polymerase beta (Pol beta), the major BER DNA polymerase and modulates base excision repair (BER). HUWE1 also acts as a critical mediator of both the p53-independent and p53-dependent tumor suppressor functions of ARF tumor suppressor in p53 regulation. Moreover, HUWE1 is both required and sufficient for the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involving in DNA damage-induced apoptosis. Furthermore, HUWE1 plays an important role in the regulation of Cdc6 stability after DNA damage. In addition, HUWE1 works as a partner of N-Myc oncoprotein in neural cells. It ubiquitinates N-Myc and primes it for proteasomal-mediated degradation. HUWE1 contains a ubiquitin-associated (UBA) domain, a WWE domain, and a Bcl-2 homology region 3 (BH3) domain at the N-terminus and a HECT domain at the C-terminus. WWE domain plays a role in the regulation of specific protein-protein interactions in a ubiquitin conjugation system. BH3 domain is responsible for the specific binding to Mcl-1. HECT domain involves in the inhibition of the transcriptional activity of p53 via a ubiquitin-dependent degradation pathway. It also controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein. Pssm-ID: 270474 Cd Length: 40 Bit Score: 35.45 E-value: 4.21e-03
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UBA_VP13D | cd14306 | UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ... |
662-696 | 4.56e-03 | ||||||||
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required. Pssm-ID: 270491 Cd Length: 36 Bit Score: 35.50 E-value: 4.56e-03
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UBA_Mud1_like | cd14308 | UBA domain found in Schizosaccharomyces pombe UBA domain-containing protein mud1 and similar ... |
659-692 | 5.50e-03 | ||||||||
UBA domain found in Schizosaccharomyces pombe UBA domain-containing protein mud1 and similar proteins; Schizosaccharomyces pombe mud1 is an ortholog of the Saccharomyces cerevisiae DNA-damage response protein Ddi1. S. cerevisiae Ddi1, also called v-SNARE-master 1 (Vsm1), belongs to a family of proteins known as the ubiquitin receptors which can bind ubiquitinated substrates and the proteasome. It is involved in the degradation of the F-box protein Ufo1, involved in the G1/S transition. It also participates in Mec1-mediated degradation of Ho endonuclease. Both S. pombe mud1 and S. cerevisiae Ddi1 contain an N-terminal ubiquitin-like (UBL) domain, an aspartyl protease-like domain, and a C-terminal ubiquitin-associated (UBA) domain. S. pombe mud1 binds to K48-linked polyubiquitin (polyUb) through UBA domain. Pssm-ID: 270493 Cd Length: 36 Bit Score: 35.17 E-value: 5.50e-03
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Peptidase_C19O | cd02671 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
733-769 | 5.68e-03 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 39.88 E-value: 5.68e-03
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Peptidase_C19R | cd02674 | A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
320-337 | 7.47e-03 | ||||||||
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 38.81 E-value: 7.47e-03
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