uncharacterized protein si:ch73-173p19.1 [Danio rerio]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||||
LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
548-859 | 6.53e-16 | ||||||
Leucine-rich repeat (LRR) protein [Transcription]; : Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 81.13 E-value: 6.53e-16
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UBX | cd01767 | Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; ... |
189-257 | 1.37e-14 | ||||||
Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; The UBXD family of proteins contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. Members in this family function as cofactors of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. Based on domain composition, UBXD proteins can be divided into two main groups, with and without ubiquitin-associated (UBA) domain. : Pssm-ID: 340466 [Multi-domain] Cd Length: 74 Bit Score: 69.21 E-value: 1.37e-14
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UBA_like_SF super family | cl21463 | UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains ... |
6-43 | 1.67e-05 | ||||||
UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains alpha-helical structural homology ubiquitin-binding domains, including UBA domains and coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domains which share a common three-helical bundle architecture. 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 bind the 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. CUE domain containing proteins are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. This superfamily also includes many UBA-like domains found in AMP-activated protein kinase (AMPK) related kinases, the NXF family of mRNA nuclear export factors, elongation factor Ts (EF-Ts), nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins. Although many UBA-like domains may have a conserved TG but not GF/Y-loop, they still show a high level of structural and sequence similarity with three-helical ubiquitin binding domains. The actual alignment was detected with superfamily member cd14333: Pssm-ID: 473871 Cd Length: 38 Bit Score: 42.53 E-value: 1.67e-05
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tolA super family | cl35847 | cell envelope integrity inner membrane protein TolA; Provisional |
108-163 | 4.75e-04 | ||||||
cell envelope integrity inner membrane protein TolA; Provisional The actual alignment was detected with superfamily member PRK09510: Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 4.75e-04
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Name | Accession | Description | Interval | E-value | ||||||
LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
548-859 | 6.53e-16 | ||||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 81.13 E-value: 6.53e-16
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UBX | cd01767 | Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; ... |
189-257 | 1.37e-14 | ||||||
Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; The UBXD family of proteins contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. Members in this family function as cofactors of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. Based on domain composition, UBXD proteins can be divided into two main groups, with and without ubiquitin-associated (UBA) domain. Pssm-ID: 340466 [Multi-domain] Cd Length: 74 Bit Score: 69.21 E-value: 1.37e-14
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UBX | pfam00789 | UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general ... |
187-257 | 2.11e-13 | ||||||
UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general Cdc48-interacting module. Pssm-ID: 395637 [Multi-domain] Cd Length: 80 Bit Score: 66.16 E-value: 2.11e-13
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AMN1 | cd09293 | Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ... |
750-888 | 2.80e-13 | ||||||
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model. Pssm-ID: 187754 [Multi-domain] Cd Length: 226 Bit Score: 70.05 E-value: 2.80e-13
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UBX | smart00166 | Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p. |
187-257 | 1.38e-10 | ||||||
Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p. Pssm-ID: 197552 [Multi-domain] Cd Length: 77 Bit Score: 58.08 E-value: 1.38e-10
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UBA_unchar_Eumetazoa | cd14333 | UBA domain found in some hypothetical proteins from Eumetazoa; The family includes some ... |
6-43 | 1.67e-05 | ||||||
UBA domain found in some hypothetical proteins from Eumetazoa; The family includes some uncharacterized Eumetazoan proteins. Although their biological function remain unclear, they all contain a very conserved ubiquitin-associated (UBA) domain which is a commonly occurring sequence motif found in proteins involved in ubiquitin-mediated proteolysis. Pssm-ID: 270518 Cd Length: 38 Bit Score: 42.53 E-value: 1.67e-05
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tolA | PRK09510 | cell envelope integrity inner membrane protein TolA; Provisional |
108-163 | 4.75e-04 | ||||||
cell envelope integrity inner membrane protein TolA; Provisional Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 4.75e-04
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Nop25 | pfam09805 | Nucleolar protein 12 (25kDa); Members of this family of proteins are part of the yeast nuclear ... |
116-166 | 7.12e-04 | ||||||
Nucleolar protein 12 (25kDa); Members of this family of proteins are part of the yeast nuclear pore complex-associated pre-60S ribosomal subunit. The family functions as a highly conserved exonuclease that is required for the 5'-end maturation of 5.8S and 25S rRNAs, demonstrating that 5'-end processing also has a redundant pathway. Nop25 binds late pre-60S ribosomes, accompanying them from the nucleolus to the nuclear periphery; and there is evidence for both physical and functional links between late 60S subunit processing and export. Pssm-ID: 430839 [Multi-domain] Cd Length: 134 Bit Score: 40.71 E-value: 7.12e-04
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LRR_4 | pfam12799 | Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
644-675 | 7.27e-04 | ||||||
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains. Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 38.00 E-value: 7.27e-04
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YqiK | COG2268 | Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
118-163 | 9.91e-04 | ||||||
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 9.91e-04
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UBA | smart00165 | Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ... |
11-43 | 1.58e-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: 36.70 E-value: 1.58e-03
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sucrsPsyn_pln | TIGR02468 | sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
133-204 | 2.77e-03 | ||||||
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein. Pssm-ID: 274147 [Multi-domain] Cd Length: 1050 Bit Score: 41.69 E-value: 2.77e-03
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UBA | pfam00627 | UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
11-42 | 3.45e-03 | ||||||
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: 35.88 E-value: 3.45e-03
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Name | Accession | Description | Interval | E-value | ||||||
LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
548-859 | 6.53e-16 | ||||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 81.13 E-value: 6.53e-16
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UBX | cd01767 | Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; ... |
189-257 | 1.37e-14 | ||||||
Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; The UBXD family of proteins contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. Members in this family function as cofactors of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. Based on domain composition, UBXD proteins can be divided into two main groups, with and without ubiquitin-associated (UBA) domain. Pssm-ID: 340466 [Multi-domain] Cd Length: 74 Bit Score: 69.21 E-value: 1.37e-14
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LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
534-776 | 9.56e-14 | ||||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 74.20 E-value: 9.56e-14
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UBX | pfam00789 | UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general ... |
187-257 | 2.11e-13 | ||||||
UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general Cdc48-interacting module. Pssm-ID: 395637 [Multi-domain] Cd Length: 80 Bit Score: 66.16 E-value: 2.11e-13
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AMN1 | cd09293 | Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ... |
750-888 | 2.80e-13 | ||||||
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model. Pssm-ID: 187754 [Multi-domain] Cd Length: 226 Bit Score: 70.05 E-value: 2.80e-13
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UBX_UBXN4 | cd16117 | Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; ... |
187-257 | 4.37e-13 | ||||||
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; UBXN4, also termed ERAD (endoplasmic-reticulum-associated protein degradation) substrate erasing protein (erasin), or UBX domain-containing protein 2 (UBXD2), or UBXDC1, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN4 is an endoplasmic reticulum (ER) localized protein that interacts with p97 (also known as VCP or Cdc48) via its UBX domain. Erasin exists in a complex with other p97/VCP-associated factors involved in endoplasmic-reticulum-associated protein degradation (ERAD). p97 is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The overexpression of UBXN4 increases degradation of a classical ERAD substrate and UBXN4 levels are increased in ER stressed cells. Anti-UBXN4 staining is increased in neuropathological lesions in brains of patients with Alzheimer's disease. Pssm-ID: 340534 [Multi-domain] Cd Length: 77 Bit Score: 65.04 E-value: 4.37e-13
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UBX_UBXN1 | cd01772 | Ubiquitin regulatory domain X (UBX) found in UBX domain protein 1 (UBXN1) and similar proteins; ... |
185-257 | 5.18e-12 | ||||||
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 1 (UBXN1) and similar proteins; UBXN1, also termed SAPK substrate protein 1 (SAKS1), UBA/UBX 33.3 kDa protein (Y33K), or UBXD10, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (Ubl or UBX) domain that has a beta-grasp ubiquitin-like fold without the C-terminal double glycine motif. UBXN1 has been identified as a substrate for stress-activated protein kinases (SAPKs). It binds polyubiquitin and valosin-containing protein (VCP), suggesting a role as an adaptor that directs VCP to polyubiquitinated proteins facilitating its destruction by the proteasome. In addition, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and be involved in the Ub-proteasome proteolytic pathways. UBXN1 can also associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domains. Pssm-ID: 340470 [Multi-domain] Cd Length: 81 Bit Score: 62.33 E-value: 5.18e-12
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RNA1 | COG5238 | Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
597-892 | 5.91e-12 | ||||||
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis]; Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 68.66 E-value: 5.91e-12
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UBX | smart00166 | Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p. |
187-257 | 1.38e-10 | ||||||
Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p. Pssm-ID: 197552 [Multi-domain] Cd Length: 77 Bit Score: 58.08 E-value: 1.38e-10
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AMN1 | cd09293 | Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ... |
644-856 | 4.46e-10 | ||||||
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model. Pssm-ID: 187754 [Multi-domain] Cd Length: 226 Bit Score: 60.80 E-value: 4.46e-10
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LRR_RI | cd00116 | Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
649-891 | 5.00e-10 | ||||||
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1). Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 61.99 E-value: 5.00e-10
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UBX_UBXN3A | cd01771 | Ubiquitin regulatory domain X (UBX) found in FAS associated factor 1 (FAF1, also known as ... |
187-253 | 1.12e-07 | ||||||
Ubiquitin regulatory domain X (UBX) found in FAS associated factor 1 (FAF1, also known as UBXN3A) and similar proteins; UBX domain-containing protein 3A (UBXN3A),also termed UBX domain-containing protein 12 (UBXD12), or FAF1, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, FAF1 contains two tandem ubiquitin-like (Ubl) domains, which shows high structural similarity with UBX domain. FAF1 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The FAF1-p97 complex inhibits the proteasomal protein degradation in which p97 acts as a co-chaperone. Moreover, FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF1 is widely expressed in adult and embryonic tissues, and in tumor cell lines, and is localized not only in the cytoplasm where it interacts with Fas, but also in the nucleus. FAF1 contains phosphorylation sites for protein kinase CK2 within the nuclear targeting domain. Phosphorylation influences nuclear localization of FAF1 but does not affect its potentiation of Fas-induced apoptosis. Other functions have also been attributed to FAF1. It inhibits nuclear factor-kappaB (NF-kappaB) by interfering with the nuclear translocation of the p65 subunit. Although the precise role of FAF1 in the ubiquitination pathway remains unclear, FAF1 interacts with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway. This family corresponds to UBX domain. Pssm-ID: 340469 Cd Length: 80 Bit Score: 49.92 E-value: 1.12e-07
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AMN1 | cd09293 | Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ... |
523-701 | 1.40e-07 | ||||||
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model. Pssm-ID: 187754 [Multi-domain] Cd Length: 226 Bit Score: 53.10 E-value: 1.40e-07
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LRR_RI | cd00116 | Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
587-869 | 1.30e-06 | ||||||
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1). Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 51.20 E-value: 1.30e-06
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PPP1R42 | cd21340 | protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
564-703 | 4.19e-06 | ||||||
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation. Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 48.63 E-value: 4.19e-06
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UBX_UBXN7 | cd01773 | Ubiquitin regulatory domain X (UBX) found in UBX domain protein 7 (UBXN7) and similar proteins; ... |
187-261 | 7.97e-06 | ||||||
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 7 (UBXN7) and similar proteins; UBXN7, also termed UBX domain-containing protein 7 (UBXD7), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN7 functions as a ubiquitin-binding adaptor that mediates the interaction between the AAA+ ATPase p97 (also known as VCP or Cdc48) and the transcription factor HIF1-alpha. It binds only to the active, NEDD8- or Rub1-modified form of cullins. In addition to having a UBX domain, UBXD7 contains a ubiquitin-associated (UBA), ubiquitin-associating (UAS), and ubiquitin-interacting motif (UIM) domains. Either UBA or UIM could serve as a docking site for neddylated-cullins. UBA domain is required for binding ubiquitylated-protein substrates, while the UIM motif is responsible for the binding to cullin RING ligases (CRLs), and the UBX domain is essential for p97 binding. Pssm-ID: 340471 Cd Length: 76 Bit Score: 44.54 E-value: 7.97e-06
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UBA_unchar_Eumetazoa | cd14333 | UBA domain found in some hypothetical proteins from Eumetazoa; The family includes some ... |
6-43 | 1.67e-05 | ||||||
UBA domain found in some hypothetical proteins from Eumetazoa; The family includes some uncharacterized Eumetazoan proteins. Although their biological function remain unclear, they all contain a very conserved ubiquitin-associated (UBA) domain which is a commonly occurring sequence motif found in proteins involved in ubiquitin-mediated proteolysis. Pssm-ID: 270518 Cd Length: 38 Bit Score: 42.53 E-value: 1.67e-05
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UBX_UBXN11 | cd17077 | Ubiquitin regulatory domain X (UBX) found in UBX domain protein 11 (UBXN11) and similar ... |
187-260 | 3.01e-05 | ||||||
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 11 (UBXN11) and similar proteins; UBXN11, also termed colorectal tumor-associated antigen COA-1, or socius, or UBX domain-containing protein 5 (UBXD5), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN11 may function as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. UBXN11 also acts as a novel interacting partner of Rnd proteins (Rnd1, Rnd2, and Rnd3/RhoE), new members of Rho family of small GTPases. It directly binds to Rnd GTPases through its C-terminal region, and further participates in disassembly of actin stress fibers. UBXN11 also binds directly to Galpha12 and Galpha13 through its N-terminal region. As a novel activator of the Galpha12 family, UBXN11 promotes the Galpha12-induced RhoA activation. Pssm-ID: 340597 Cd Length: 76 Bit Score: 42.98 E-value: 3.01e-05
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LRR_RI | cd00116 | Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
543-821 | 1.84e-04 | ||||||
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1). Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 44.65 E-value: 1.84e-04
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RNA1 | COG5238 | Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
587-841 | 1.94e-04 | ||||||
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis]; Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 44.78 E-value: 1.94e-04
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UBA_atUPL1_2_like | cd14327 | UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ... |
11-43 | 3.28e-04 | ||||||
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: 38.82 E-value: 3.28e-04
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tolA | PRK09510 | cell envelope integrity inner membrane protein TolA; Provisional |
108-163 | 4.75e-04 | ||||||
cell envelope integrity inner membrane protein TolA; Provisional Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 4.75e-04
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Nop25 | pfam09805 | Nucleolar protein 12 (25kDa); Members of this family of proteins are part of the yeast nuclear ... |
116-166 | 7.12e-04 | ||||||
Nucleolar protein 12 (25kDa); Members of this family of proteins are part of the yeast nuclear pore complex-associated pre-60S ribosomal subunit. The family functions as a highly conserved exonuclease that is required for the 5'-end maturation of 5.8S and 25S rRNAs, demonstrating that 5'-end processing also has a redundant pathway. Nop25 binds late pre-60S ribosomes, accompanying them from the nucleolus to the nuclear periphery; and there is evidence for both physical and functional links between late 60S subunit processing and export. Pssm-ID: 430839 [Multi-domain] Cd Length: 134 Bit Score: 40.71 E-value: 7.12e-04
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LRR_4 | pfam12799 | Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
644-675 | 7.27e-04 | ||||||
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains. Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 38.00 E-value: 7.27e-04
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UBA_VP13D | cd14306 | UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ... |
14-46 | 9.39e-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: 37.42 E-value: 9.39e-04
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YqiK | COG2268 | Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
118-163 | 9.91e-04 | ||||||
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 9.91e-04
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UBA1_Rad23_like | cd14280 | UBA1 domain of Rad23 proteins found in eukaryotes; The Rad23 family includes the yeast ... |
11-43 | 1.23e-03 | ||||||
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: 37.21 E-value: 1.23e-03
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UBA | smart00165 | Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ... |
11-43 | 1.58e-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: 36.70 E-value: 1.58e-03
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CCDC66 | pfam15236 | Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
100-178 | 1.63e-03 | ||||||
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure. Pssm-ID: 434558 [Multi-domain] Cd Length: 154 Bit Score: 40.16 E-value: 1.63e-03
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TPH | pfam13868 | Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
100-158 | 2.69e-03 | ||||||
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain. Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 2.69e-03
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sucrsPsyn_pln | TIGR02468 | sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
133-204 | 2.77e-03 | ||||||
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein. Pssm-ID: 274147 [Multi-domain] Cd Length: 1050 Bit Score: 41.69 E-value: 2.77e-03
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UBA2_UBP5 | cd14386 | UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ... |
11-47 | 3.02e-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: 3.02e-03
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YqiK | COG2268 | Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
106-164 | 3.12e-03 | ||||||
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.01 E-value: 3.12e-03
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UBA | pfam00627 | UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
11-42 | 3.45e-03 | ||||||
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: 35.88 E-value: 3.45e-03
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UBA1_Rad23 | cd14377 | UBA1 domain of Rad23 proteins found in metazoa; The family includes mammalian orthologs of ... |
11-45 | 4.35e-03 | ||||||
UBA1 domain of Rad23 proteins found in metazoa; The family includes mammalian orthologs of yeast nucleotide excision repair (NER) proteins, Rad23p (in Saccharomyces cerevisiae) and Rhp23p (in Schizosaccharomyces pombe). 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: 270560 Cd Length: 40 Bit Score: 35.84 E-value: 4.35e-03
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UBA1_scUBP14_like | cd14296 | UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ... |
10-44 | 5.65e-03 | ||||||
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: 35.30 E-value: 5.65e-03
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PPP1R42 | cd21340 | protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
758-891 | 8.09e-03 | ||||||
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation. Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 39.00 E-value: 8.09e-03
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UBA2_spUBP14_like | cd14297 | UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ... |
11-45 | 8.35e-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: 34.76 E-value: 8.35e-03
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LRR_4 | pfam12799 | Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
543-583 | 8.80e-03 | ||||||
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains. Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 34.91 E-value: 8.80e-03
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UBX_UBXN3B | cd16120 | Ubiquitin regulatory domain X (UBX) found in FAS associated factor 2 (FAF2, also known as ... |
189-260 | 9.10e-03 | ||||||
Ubiquitin regulatory domain X (UBX) found in FAS associated factor 2 (FAF2, also known as UBXN3B) and similar proteins; UBX domain-containing protein 3B (UBXN3B), also termed protein ETEA, or FAF2, or UBX domain-containing protein 8 (UBXD8), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. FAF2 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The p97-UBXD8 complex destabilizes mRNA by promoting release of ubiquitinated the RNA-binding protein HuR from messenger ribonucleoprotein (mRNP). Moreover, FAF2 is the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. A yeast two-hybrid assay showed that FAF2 can interact with Fas. Pssm-ID: 340537 Cd Length: 80 Bit Score: 36.10 E-value: 9.10e-03
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