ubiquitin specific protease 5, isoform A [Drosophila melanogaster]
Protein Classification
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 ... |
333-823 | 4.18e-111 | ||||||||
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: 341.61 E-value: 4.18e-111
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| zf-UBP_var | pfam17807 | Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ... |
11-77 | 5.97e-25 | ||||||||
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: 98.44 E-value: 5.97e-25
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| UBA1_UBP5_like | cd14294 | UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; ... |
631-674 | 7.27e-23 | ||||||||
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: 91.99 E-value: 7.27e-23
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| UBA2_UBP5 | cd14386 | UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ... |
696-737 | 2.50e-21 | ||||||||
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: 87.39 E-value: 2.50e-21
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| zf-UBP | pfam02148 | Zn-finger in ubiquitin-hydrolases and other protein; |
204-278 | 7.92e-20 | ||||||||
Zn-finger in ubiquitin-hydrolases and other protein; : Pssm-ID: 460464 Cd Length: 63 Bit Score: 83.85 E-value: 7.92e-20
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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 ... |
333-823 | 4.18e-111 | ||||||||
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: 341.61 E-value: 4.18e-111
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| UCH | pfam00443 | Ubiquitin carboxyl-terminal hydrolase; |
332-619 | 7.91e-39 | ||||||||
Ubiquitin carboxyl-terminal hydrolase; Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 146.82 E-value: 7.91e-39
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| zf-UBP_var | pfam17807 | Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ... |
11-77 | 5.97e-25 | ||||||||
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: 98.44 E-value: 5.97e-25
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| UBA1_UBP5_like | cd14294 | UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; ... |
631-674 | 7.27e-23 | ||||||||
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: 91.99 E-value: 7.27e-23
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| UBA2_UBP5 | cd14386 | UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ... |
696-737 | 2.50e-21 | ||||||||
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: 87.39 E-value: 2.50e-21
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| zf-UBP | pfam02148 | Zn-finger in ubiquitin-hydrolases and other protein; |
204-278 | 7.92e-20 | ||||||||
Zn-finger in ubiquitin-hydrolases and other protein; Pssm-ID: 460464 Cd Length: 63 Bit Score: 83.85 E-value: 7.92e-20
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| ZnF_UBP | smart00290 | Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
203-257 | 3.40e-15 | ||||||||
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; Pssm-ID: 197632 Cd Length: 50 Bit Score: 70.09 E-value: 3.40e-15
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| UBA | pfam00627 | UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
697-732 | 7.64e-12 | ||||||||
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: 60.15 E-value: 7.64e-12
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| UBP12 | COG5560 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
296-457 | 1.17e-10 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 65.29 E-value: 1.17e-10
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| UBA | smart00165 | Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ... |
697-733 | 4.71e-10 | ||||||||
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: 55.19 E-value: 4.71e-10
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| UBA | pfam00627 | UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
629-666 | 2.99e-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: 47.44 E-value: 2.99e-07
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| UBA | smart00165 | Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ... |
630-667 | 3.71e-03 | ||||||||
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: 35.54 E-value: 3.71e-03
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| rad23 | TIGR00601 | UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
685-734 | 6.79e-03 | ||||||||
UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273167 [Multi-domain] Cd Length: 378 Bit Score: 39.49 E-value: 6.79e-03
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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 ... |
333-823 | 4.18e-111 | ||||||||
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: 341.61 E-value: 4.18e-111
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| UCH | pfam00443 | Ubiquitin carboxyl-terminal hydrolase; |
332-619 | 7.91e-39 | ||||||||
Ubiquitin carboxyl-terminal hydrolase; Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 146.82 E-value: 7.91e-39
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| Peptidase_C19 | cd02257 | Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
333-824 | 8.35e-27 | ||||||||
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: 110.27 E-value: 8.35e-27
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| zf-UBP_var | pfam17807 | Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ... |
11-77 | 5.97e-25 | ||||||||
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: 98.44 E-value: 5.97e-25
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| UBA1_UBP5_like | cd14294 | UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; ... |
631-674 | 7.27e-23 | ||||||||
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: 91.99 E-value: 7.27e-23
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| UBA2_UBP5 | cd14386 | UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ... |
696-737 | 2.50e-21 | ||||||||
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: 87.39 E-value: 2.50e-21
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| zf-UBP | pfam02148 | Zn-finger in ubiquitin-hydrolases and other protein; |
204-278 | 7.92e-20 | ||||||||
Zn-finger in ubiquitin-hydrolases and other protein; Pssm-ID: 460464 Cd Length: 63 Bit Score: 83.85 E-value: 7.92e-20
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| ZnF_UBP | smart00290 | Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
203-257 | 3.40e-15 | ||||||||
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; Pssm-ID: 197632 Cd Length: 50 Bit Score: 70.09 E-value: 3.40e-15
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| peptidase_C19C | cd02659 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
330-602 | 2.46e-14 | ||||||||
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: 74.99 E-value: 2.46e-14
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| UBA1_spUBP14_like | cd14385 | UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ... |
630-675 | 4.32e-14 | ||||||||
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: 67.05 E-value: 4.32e-14
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| UBA1_NUB1_like | cd14291 | UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ... |
697-732 | 1.55e-13 | ||||||||
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: 65.16 E-value: 1.55e-13
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| UBA1_scUBP14_like | cd14296 | UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ... |
631-669 | 5.19e-13 | ||||||||
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: 63.80 E-value: 5.19e-13
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| UBA1_UBP5 | cd14383 | UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ... |
629-676 | 9.45e-13 | ||||||||
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: 63.15 E-value: 9.45e-13
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| UBA2_spUBP14_like | cd14297 | UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ... |
698-736 | 2.09e-12 | ||||||||
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: 62.11 E-value: 2.09e-12
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| Peptidase_C19L | cd02668 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
333-602 | 2.70e-12 | ||||||||
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: 68.60 E-value: 2.70e-12
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| Peptidase_C19D | cd02660 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
333-620 | 6.99e-12 | ||||||||
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: 67.40 E-value: 6.99e-12
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| UBA | pfam00627 | UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
697-732 | 7.64e-12 | ||||||||
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: 60.15 E-value: 7.64e-12
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| UBA2_UBP13 | cd14387 | UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ... |
698-732 | 2.96e-11 | ||||||||
UBA2 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 UBA2 domain. Pssm-ID: 270570 Cd Length: 35 Bit Score: 58.54 E-value: 2.96e-11
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| UBA2_scUBP14_like | cd14298 | UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ... |
698-735 | 7.15e-11 | ||||||||
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: 57.47 E-value: 7.15e-11
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| UBP12 | COG5560 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
296-457 | 1.17e-10 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 65.29 E-value: 1.17e-10
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| UBA_RUP1p | cd14307 | UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins; RUP1p is a ... |
698-735 | 1.50e-10 | ||||||||
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: 56.54 E-value: 1.50e-10
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| UBA | smart00165 | Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ... |
697-733 | 4.71e-10 | ||||||||
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: 55.19 E-value: 4.71e-10
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| Peptidase_C19G | cd02663 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
333-603 | 6.07e-10 | ||||||||
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: 61.17 E-value: 6.07e-10
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| UBA1_atUBP14 | cd14295 | UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ... |
630-674 | 1.12e-09 | ||||||||
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: 54.30 E-value: 1.12e-09
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| UBA_PUB_plant | cd14290 | UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family ... |
630-675 | 2.07e-09 | ||||||||
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: 53.60 E-value: 2.07e-09
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| UBA1_scUBP14_like | cd14296 | UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ... |
698-735 | 2.34e-09 | ||||||||
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: 53.40 E-value: 2.34e-09
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| Peptidase_C19K | cd02667 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
333-602 | 2.88e-09 | ||||||||
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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 58.94 E-value: 2.88e-09
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| UBA | cd14270 | UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ... |
701-730 | 4.87e-09 | ||||||||
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ubiquitin-associated (UBA) domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only the bind UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains. Pssm-ID: 270456 [Multi-domain] Cd Length: 30 Bit Score: 51.97 E-value: 4.87e-09
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| UBA_VP13D | cd14306 | UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ... |
701-736 | 7.81e-09 | ||||||||
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: 51.67 E-value: 7.81e-09
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| Peptidase_C19R | cd02674 | A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
333-613 | 2.11e-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 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: 55.76 E-value: 2.11e-08
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| Peptidase_C19A | cd02657 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
333-601 | 4.76e-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: 55.41 E-value: 4.76e-08
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| UBA1_UBP13 | cd14384 | UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ... |
630-676 | 5.88e-08 | ||||||||
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: 49.64 E-value: 5.88e-08
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| UBA1_spUBP14_like | cd14385 | UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ... |
697-737 | 7.92e-08 | ||||||||
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: 49.33 E-value: 7.92e-08
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| UBA_UBS3B | cd14301 | UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and ... |
699-735 | 1.31e-07 | ||||||||
UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and similar proteins; UBS3B, or Cbl-interacting protein p70, suppressor of T-cell receptor signaling 1 (Sts-1), T-cell ubiquitin ligand 2 (TULA-2), or tyrosine-protein phosphatase STS1/TULA2, is ubiquitously expressed in mammalian tissues in a variety of cell types. It exhibits high phosphatase activity, but demonstrates no proapoptotic activity. It negatively regulates the tyrosine kinase Zap-70 activation and T cell receptor (TCR) signaling pathways that modulate T cell activation. Moreover, UBS3B acts as a Cbl- and ubiquitin-interacting protein that inhibits endocytosis of epidermal growth factor receptor (EGFR) and platelet-derived growth factor receptor. Pssm-ID: 270486 [Multi-domain] Cd Length: 38 Bit Score: 48.21 E-value: 1.31e-07
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| Peptidase_C19F | cd02662 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
333-600 | 1.49e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 53.14 E-value: 1.49e-07
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| Peptidase_C19A | cd02657 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
769-808 | 2.40e-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 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: 53.49 E-value: 2.40e-07
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| UBA | pfam00627 | UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
629-666 | 2.99e-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: 47.44 E-value: 2.99e-07
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| UBA_scDdi1_like | cd14309 | UBA domain found in Saccharomyces cerevisiae DNA-damage response protein Ddi1 and similar ... |
699-733 | 3.65e-07 | ||||||||
UBA domain found in Saccharomyces cerevisiae DNA-damage response protein Ddi1 and similar proteins; Ddi1, also called v-SNARE-master 1 (Vsm1), is a ubiquitin receptor involved in regulation of the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as a ubiquitin association domain (UBA)- ubiquitin-like-domain (UBL) shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. Ddi1 contains an N-terminal UBL domain and a C-terminal UBA domain. It also harbors a central retroviral aspartyl-protease-like domain (RVP) which may be important in cell-cycle control. At this point, Ddi1 may function proteolytically during regulated protein turnover in the cell. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also called transporter regulator RS1 (RS1) which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1. Pssm-ID: 270494 Cd Length: 36 Bit Score: 47.14 E-value: 3.65e-07
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| UBA2_atUBP14 | cd14388 | UBA2 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ... |
704-735 | 3.85e-07 | ||||||||
UBA2 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 UBA2 domain which show a high level of sequence similarity with mammalian ubiquitin-associated and SH3 domain-containing protein A (UBS3A). Pssm-ID: 270571 Cd Length: 38 Bit Score: 47.18 E-value: 3.85e-07
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| UBA_atUPL1_2_like | cd14327 | UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ... |
699-735 | 5.11e-07 | ||||||||
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: 46.52 E-value: 5.11e-07
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| UBA_Mud1_like | cd14308 | UBA domain found in Schizosaccharomyces pombe UBA domain-containing protein mud1 and similar ... |
698-732 | 5.91e-07 | ||||||||
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: 46.34 E-value: 5.91e-07
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| UBA2_KPC2 | cd14304 | UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ... |
697-734 | 8.69e-07 | ||||||||
UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar proteins; KPC2, also called ubiquitin-associated domain-containing protein 1 (UBAC1), or glialblastoma cell differentiation-related protein 1, is one of two subunits of Kip1 ubiquitination-promoting complex (KPC), a novel E3 ubiquitin-protein ligase that also contains KPC1 subunit and regulates the ubiquitin-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor p27 at G1 phase. KPC2 contains a ubiquitin-like (UBL) domain and two ubiquitin-associated (UBA) domains. This model corresponds to the UBA2 domain. Pssm-ID: 270489 Cd Length: 39 Bit Score: 46.10 E-value: 8.69e-07
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| COG5533 | COG5533 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
771-825 | 2.31e-06 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 50.19 E-value: 2.31e-06
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| UBA_HUWE1 | cd14288 | UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ... |
697-735 | 2.88e-06 | ||||||||
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: 44.70 E-value: 2.88e-06
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| UBA_UBS3A_like | cd14300 | UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and ... |
704-735 | 5.53e-06 | ||||||||
UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and similar proteins; UBS3A, also called Cbl-interacting protein 4 (CLIP4), suppressor of T-cell receptor signaling 2 (Sts-2), or T-cell ubiquitin ligand 1 (TULA-1), is a lymphoid protein only detected in thymus, spleen, and bone marrow. UBS3A exhibits extremely low phosphatase activity, but is capable of promoting T-cell apoptosis independent of either T cell receptor (TCR)/CD3-mediated signaling or caspase activity. It functions as a negative regulator of TCR signaling. UBS3A can also inhibit HIV-1 biogenesis through the binding of ATP-binding cassette protein family E member 1 (ABCE-1), a host factor of HIV-1 assembly. Moreover, UBS3A acts as the Cbl- and ubiquitin-interacting protein that can inhibit endocytosis and downregulation of ligand-activated epidermal growth factor receptor (EGFR) by impairing Cbl-induced ubiquitination, as well as inhibit clathrin-dependent endocytosis in general. This family also includes Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and some uncharacterized AAA-type ATPase-like proteins found in plants. Pssm-ID: 270485 Cd Length: 37 Bit Score: 43.68 E-value: 5.53e-06
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| Peptidase_C19E | cd02661 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
770-811 | 7.99e-06 | ||||||||
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: 48.43 E-value: 7.99e-06
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| UBA_UBXN1 | cd14302 | UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ... |
699-737 | 1.17e-05 | ||||||||
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: 43.05 E-value: 1.17e-05
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| UBA_UBXN1 | cd14302 | UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ... |
637-672 | 1.65e-05 | ||||||||
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: 42.66 E-value: 1.65e-05
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| Peptidase_C19H | cd02664 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
333-448 | 2.60e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 47.10 E-value: 2.60e-05
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| Peptidase_C19G | cd02663 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
770-823 | 4.41e-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: 46.15 E-value: 4.41e-05
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| UBA_UBS3B | cd14301 | UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and ... |
634-669 | 4.48e-05 | ||||||||
UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and similar proteins; UBS3B, or Cbl-interacting protein p70, suppressor of T-cell receptor signaling 1 (Sts-1), T-cell ubiquitin ligand 2 (TULA-2), or tyrosine-protein phosphatase STS1/TULA2, is ubiquitously expressed in mammalian tissues in a variety of cell types. It exhibits high phosphatase activity, but demonstrates no proapoptotic activity. It negatively regulates the tyrosine kinase Zap-70 activation and T cell receptor (TCR) signaling pathways that modulate T cell activation. Moreover, UBS3B acts as a Cbl- and ubiquitin-interacting protein that inhibits endocytosis of epidermal growth factor receptor (EGFR) and platelet-derived growth factor receptor. Pssm-ID: 270486 [Multi-domain] Cd Length: 38 Bit Score: 41.27 E-value: 4.48e-05
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| UBA_II_E2_UBCD4 | cd14391 | UBA domain found in Drosophila melanogaster ubiquitin-conjugating enzyme E2-22 kDa (UbcD4) and ... |
704-733 | 7.75e-05 | ||||||||
UBA domain found in Drosophila melanogaster ubiquitin-conjugating enzyme E2-22 kDa (UbcD4) and similar proteins; UbcD4, also called ubiquitin carrier protein or ubiquitin-protein ligase, is a class II E2 ubiquitin-conjugating enzyme encoded by Drosophila E2 gene which is only expressed in pole cells in embryos. It is a putative E2 enzyme homologous to the Huntingtin interacting protein-2 (HIP2) of human. UbcD4 specifically interacts with the polyubiquitin-binding subunit of the proteasome. It contains a C-terminal ubiquitin-associated (UBA) domain in addition to an N-terminal catalytic ubiquitin-conjugating enzyme E2 (UBCc) domain. Pssm-ID: 270574 Cd Length: 36 Bit Score: 40.36 E-value: 7.75e-05
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| Peptidase_C19R | cd02674 | A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
767-809 | 1.00e-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: 44.59 E-value: 1.00e-04
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| UBA2_spUBP14_like | cd14297 | UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ... |
630-669 | 1.34e-04 | ||||||||
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: 39.77 E-value: 1.34e-04
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| UBA_At3g58460_like | cd14287 | UBA domain found in uncharacterized protein At3g58460 from Arabidopsis thaliana and its ... |
698-732 | 1.38e-04 | ||||||||
UBA domain found in uncharacterized protein At3g58460 from Arabidopsis thaliana and its homologs from other plants; The uncharacterized protein At3g58460 from Arabidopsis thaliana is also known as rhomboid-like protein 15 which is encoded by RBL15 gene. Although the biological function of the family members remains unclear, they all contain an N-terminal rhomboid-like domain and a C-terminal ubiquitin-associated (UBA) domain. Pssm-ID: 270473 [Multi-domain] Cd Length: 36 Bit Score: 39.68 E-value: 1.38e-04
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| COG5077 | COG5077 | Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
330-358 | 2.45e-04 | ||||||||
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 44.86 E-value: 2.45e-04
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| UBA1_Rad23_like | cd14280 | UBA1 domain of Rad23 proteins found in eukaryotes; The Rad23 family includes the yeast ... |
696-734 | 2.71e-04 | ||||||||
UBA1 domain of Rad23 proteins found in eukaryotes; The Rad23 family includes the yeast nucleotide excision repair (NER) proteins, Rad23p (in Saccharomyces cerevisiae) and Rhp23p (in Schizosaccharomyces pombe), their mammalian orthologs HR23A and HR23B, and putative DNA repair proteins from plants. Rad23 proteins play dual roles in DNA repair as well as in proteosomal degradation. They have affinity for both the proteasome and ubiquitinylated proteins and participate in translocating polyubiquitinated proteins to the proteasome. Rad23 proteins carry a ubiquitin-like (UBL) and two ubiquitin-associated (UBA) domains, as well as a xeroderma pigmentosum group C (XPC) protein-binding domain. UBL domain is responsible for the binding to proteasome. UBA domains are important for binding of ubiquitin (Ub) or multi-ubiquitinated substrates which suggests Rad23 proteins might be involved in certain pathways of ubiquitin metabolism. Both UBL domain and XPC-binding domain are necessary for efficient NER function of Rad23 proteins. This model corresponds to the UBA1 domain. Pssm-ID: 270466 Cd Length: 39 Bit Score: 39.14 E-value: 2.71e-04
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| Peptidase_C19O | cd02671 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
329-520 | 2.98e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 43.73 E-value: 2.98e-04
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| UBA_cnDdi1_like | cd14310 | UBA domain found in Cryptococcus neoformans DNA-damage response protein Ddi1 and similar ... |
703-728 | 3.10e-04 | ||||||||
UBA domain found in Cryptococcus neoformans DNA-damage response protein Ddi1 and similar proteins; The family includes some uncharacterized Ddi and similar proteins which show a high level of sequence similarity with yeast Ddi1. Ddi1, also called v-SNARE-master 1 (Vsm1), is a ubiquitin receptor involved in regulation of the cell cycle and late secretory pathway in yeast. It functions as a ubiquitin association domain (UBA)- ubiquitin-like-domain (UBL) shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. Ddi1 contains an N-terminal UBL domain and a C-terminal UBA domain. It also harbors a central retroviral aspartyl-protease-like domain (RVP) which may be important in cell-cycle control. At this point, Ddi1 may function proteolytically during regulated protein turnover in the cell. Pssm-ID: 270495 Cd Length: 30 Bit Score: 38.67 E-value: 3.10e-04
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| UBA_VP13D | cd14306 | UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ... |
634-669 | 3.16e-04 | ||||||||
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: 38.58 E-value: 3.16e-04
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| UCH_1 | pfam13423 | Ubiquitin carboxyl-terminal hydrolase; |
770-807 | 3.22e-04 | ||||||||
Ubiquitin carboxyl-terminal hydrolase; Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 43.41 E-value: 3.22e-04
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| UBA_PLICs | cd14399 | UBA domain of eukaryotic protein linking integrin-associated protein (IAP, also known as CD47) ... |
701-730 | 8.10e-04 | ||||||||
UBA domain of eukaryotic protein linking integrin-associated protein (IAP, also known as CD47) with cytoskeleton (PLIC) proteins; The PLIC proteins (or ubiquilins) family contains human homologs of the yeast ubiquitin-like Dsk2 protein, PLIC-1 (also called ubiquilin-1), PLIC-2 (also called ubiquilin-2 or Chap1), PLIC-3 (also called ubiquilin-3) and PLIC-4 (also called ubiquilin-4, Ataxin-1 interacting ubiquitin-like protein, A1Up, Connexin43-interacting protein of 75 kDa, or CIP75), and mouse PLIC proteins. They are ubiquitin-binding adaptor proteins involved in all protein degradation pathways through delivering ubiquitinated substrates to proteasomes. They also promote autophagy-dependent cell survival during nutrient starvation. PLIC-1 regulates the function of the thrombospondin receptor CD47 and G protein signaling. It plays a role in TLR4-mediated signaling through interacting with the Toll/interleukin-1 receptor (TIR) domain of TLR4. It also inhibits the TLR3-Trif antiviral pathway by reducing the abundance of Trif. Moreover, PLIC-1 binds to gamma-aminobutyric acid receptors (GABAARs) and modulates the ubiquitin-dependent, proteasomal degradation of GABAARs. Furthermore, PLIC-1 acts as a molecular chaperone regulating amyloid precursor protein (APP) biosynthesis, trafficking, and degradation by stimulating K63-linked polyubiquitination of lysine 688 in the APP intracellular domain. In addition, PLIC-1 is involved in the protein aggregation-stress pathway via associating with the ubiquitin-interacting motif (UIM) proteins ataxin 3, HSJ1a, and epidermal growth factor substrate 15 (EPS15). PLIC-2 is a protein that binds the ATPase domain of the HSP70-like Stch protein. It functions as a negative regulator of G protein-coupled receptor (GPCR) endocytosis. It also involved in amyotrophic lateral sclerosis (ALS)-related dementia. PLIC-3 is encoded by UBQLN3, a testis-specific gene. It shows high sequence similarity with the Xenopus protein XDRP1, a nuclear phosphoprotein that binds to the N-terminus of cyclin A and inhibits Ca2+-induced degradation of cyclin A, but not cyclin B. PLIC-4 is a ubiquitin-like nuclear protein that interacts with ataxin-1 and further links ataxin-1 with the chaperone and ubiquitin-proteasome pathways. It also binds to the non-ubiquitinated gap junction protein connexin43 (Cx43) and regulates the turnover of Cx43 through the proteasomal pathway. PLIC proteins contain an N-terminal ubiquitin-like (UBL) domain that is responsible for the binding of ubiquitin-interacting motifs (UIMs) expressed by proteasomes and endocytic adaptors, and C-terminal ubiquitin-associated (UBA) domain that interacts with ubiquitin chains present on proteins destined for proteasomal degradation. In addition, mammalian PLIC2 proteins have an extra collagen-like motif region which is absent in other PLIC proteins and the yeast Dsk2 protein. Pssm-ID: 270582 Cd Length: 40 Bit Score: 37.51 E-value: 8.10e-04
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| UBA_atDRM2_like | cd14330 | UBA domain found in Arabidopsis thaliana DNA (cytosine-5)-methyltransferase DRM2 (atDRM2) and ... |
698-734 | 9.51e-04 | ||||||||
UBA domain found in Arabidopsis thaliana DNA (cytosine-5)-methyltransferase DRM2 (atDRM2) and similar proteins; atDRM2, also called protein domains rearranged methylase 2, is a homolog of the mammalian de novo methyltransferase DNMT3. It is the major de novo methyltransferase targeted to DNA by small interfering RNAs (siRNAs) in the RNA-directed DNA methylation (RdDM) pathway in Arabidopsis thaliana. atDRM2 is a part of the RdDM effector complex and plays a catalytic role in RdDM. It contains an N-terminal UBA domains and a C-terminal methyltransferase domain, both of which are required for normal RdDM. Pssm-ID: 270515 Cd Length: 37 Bit Score: 37.42 E-value: 9.51e-04
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| UBA_II_E2_UBE2K_like | cd14313 | UBA domain found in vertebrate ubiquitin-conjugating enzyme E2 K (UBE2K), Drosophila ... |
704-733 | 1.15e-03 | ||||||||
UBA domain found in vertebrate ubiquitin-conjugating enzyme E2 K (UBE2K), Drosophila melanogaster ubiquitin-conjugating enzyme E2-22 kDa (UbcD4) and similar proteins; UBE2K, also called Huntingtin-interacting protein 2 (HIP-2), ubiquitin carrier protein, ubiquitin-conjugating enzyme E2-25 kDa (E2-25K), or ubiquitin-protein ligase, is a multi-ubiquitinating enzyme with the ability to synthesize Lys48-linked polyubiquitin chains which is involved in the ubiquitin (Ub)-dependent proteolytic pathway. It interacts with the frameshift mutant of ubiquitin B and functions as a crucial factor regulating amyloid-beta neurotoxicity. It has also been characterized as Huntingtin-interacting protein that modulates the neurotoxicity of Amyloid-beta (Abeta), the principal protein involved in Alzheimer's disease pathogenesis. Moreover, E2-25K increases aggregate the formation of expanded polyglutamine proteins and polyglutamine-induced cell death in the pathology of polyglutamine diseases. UbcD4, also called ubiquitin carrier protein, or ubiquitin-protein ligase, is encoded by Drosophila E2 gene which is only expressed in pole cells in embryos. It is a putative E2 enzyme homologous to the Huntingtin interacting protein-2 (HIP2) of human. UbcD4 specifically interacts with the polyubiquitin-binding subunit of the proteasome. This family also includes a putative ubiquitin conjugating enzyme from plasmodium Yoelii (pyUCE). It shows a high level of sequence similarity with UBE2K and may also plays a role in the ubiquitin-mediated protein degradation pathway. All family members are class II E2 conjugating enzymes which contain a C-terminal ubiquitin-associated (UBA) domain in addition to an N-terminal catalytic ubiquitin-conjugating enzyme E2 (UBCc) domain. Pssm-ID: 270498 Cd Length: 36 Bit Score: 37.30 E-value: 1.15e-03
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| UBA_AAA_plant | cd14389 | UBA domain found in plant AAA-type ATPase-like proteins; This family includes some ... |
704-735 | 1.21e-03 | ||||||||
UBA domain found in plant AAA-type ATPase-like proteins; This family includes some uncharacterized AAA-type ATPase-like proteins found in plant. The AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. Members in this family contains an N-terminal ubiquitin-association (UBA) domain, a AAA-type ATPase domain and a C-terminal MgsA AAA+ ATPase domain. This model corresponds to the UBA domain which show a high level of sequence similarity with mammalian ubiquitin-associated and SH3 domain-containing protein A (UBS3A). Pssm-ID: 270572 Cd Length: 37 Bit Score: 37.33 E-value: 1.21e-03
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| Peptidase_C19E | cd02661 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
332-350 | 1.48e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 41.49 E-value: 1.48e-03
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| UBA2_NUB1 | cd14292 | UBA2 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ... |
699-728 | 1.52e-03 | ||||||||
UBA2 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 UBA2 domain. Pssm-ID: 270478 Cd Length: 35 Bit Score: 36.62 E-value: 1.52e-03
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| UBA_UBL7 | cd14326 | UBA domain found in ubiquitin-like protein 7 (UBL7) and similar proteins; UBL7, also called ... |
701-733 | 1.92e-03 | ||||||||
UBA domain found in ubiquitin-like protein 7 (UBL7) and similar proteins; UBL7, also called bone marrow stromal cell ubiquitin-like protein (BMSC-UbP), or ubiquitin-like protein SB132, is a novel ubiquitin-like protein that may play roles in regulation of bone marrow stromal cell (BMSC) function or cell differentiation via an evocator-associated and cell-specific pattern. UBL7 contains an N-terminal ubiquitin domain (UBQ) and a C-terminal ubiquitin-associated (UBA) domain. UBQ domain interacts with 26S proteasome-dependent degradation, and UBA domain links cellular processes and the ubiquitin system. Pssm-ID: 270511 Cd Length: 38 Bit Score: 36.54 E-value: 1.92e-03
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| Peptidase_C19H | cd02664 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
771-823 | 2.10e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 41.32 E-value: 2.10e-03
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| UBA1_atUBP14 | cd14295 | UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ... |
697-737 | 2.30e-03 | ||||||||
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: 36.58 E-value: 2.30e-03
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| COG5533 | COG5533 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
333-357 | 2.47e-03 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 40.56 E-value: 2.47e-03
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| UBA1_KPC2 | cd14303 | UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ... |
698-736 | 2.67e-03 | ||||||||
UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar proteins; KPC2, also called ubiquitin-associated domain-containing protein 1 (UBAC1), or glialblastoma cell differentiation-related protein 1, is one of two subunits of Kip1 ubiquitination-promoting complex (KPC), a novel E3 ubiquitin-protein ligase that also contains KPC1 subunit and regulates the ubiquitin-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor p27 at G1 phase. KPC2 contains a ubiquitin-like (UBL) domain and two ubiquitin-associated (UBA) domains. This model corresponds to the UBA1 domain. Pssm-ID: 270488 [Multi-domain] Cd Length: 41 Bit Score: 36.22 E-value: 2.67e-03
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| UBA_HUWE1 | cd14288 | UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ... |
630-669 | 3.70e-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: 35.84 E-value: 3.70e-03
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| UBA | smart00165 | Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ... |
630-667 | 3.71e-03 | ||||||||
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: 35.54 E-value: 3.71e-03
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| Peptidase_C19O | cd02671 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
771-807 | 3.91e-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: 40.26 E-value: 3.91e-03
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| UBA_PLCs_like | cd14323 | UBA domain of eukaryotic protein linking integrin-associated protein with cytoskeleton (PLIC) ... |
699-733 | 6.47e-03 | ||||||||
UBA domain of eukaryotic protein linking integrin-associated protein with cytoskeleton (PLIC) proteins, Saccharomyces cerevisiae proteins Dsk2p and Gts1p, and similar proteins; The PLIC proteins (or ubiquilins) family contains human homologs of the yeast ubiquitin-like Dsk2 protein, PLIC-1 (also called ubiquilin-1), PLIC-2 (also called ubiquilin-2 or Chap1), PLIC-3 (also called ubiquilin-3) and PLIC-4 (also called ubiquilin-4, Ataxin-1 interacting ubiquitin-like protein, A1Up, Connexin43-interacting protein of 75 kDa, or CIP75), and mouse PLIC proteins. They are ubiquitin-binding adaptor proteins involved in all protein degradation pathways through delivering ubiquitinated substrates to proteasomes. They also promote autophagy-dependent cell survival during nutrient starvation. Saccharomyces cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Gts1p, also called protein LSR1, is encoded by a pleiotropic gene GTS1 in budding yeast. The formation of Gts1p-mediated protein aggregates may induce reactive oxygen species (ROS) production and apoptosis. Gts1p also plays an important role in the regulation of heat and other stress responses under glucose-limited or -depleted conditions in either batch or continuous culture. Pssm-ID: 270508 Cd Length: 39 Bit Score: 35.07 E-value: 6.47e-03
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| rad23 | TIGR00601 | UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
685-734 | 6.79e-03 | ||||||||
UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273167 [Multi-domain] Cd Length: 378 Bit Score: 39.49 E-value: 6.79e-03
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