zinc finger CCHC domain-containing protein 2 isoform X8 [Rattus norvegicus]
Protein Classification
zinc finger CCHC domain-containing protein( domain architecture ID 13063153)
zinc finger CCHC (ZCCHC) domain-containing protein contains a zinc knuckle or a zinc binding motif, CX2CX4HX4C, where X can be any amino acid, and may bind single-stranded RNA
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| Herpes_BLLF1 super family | cl37540 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
682-1013 | 1.23e-04 | ||||||
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo. The actual alignment was detected with superfamily member pfam05109: Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 46.45 E-value: 1.23e-04
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| zf-CCHC | pfam00098 | Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ... |
1123-1138 | 6.27e-04 | ||||||
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger. : Pssm-ID: 395050 [Multi-domain] Cd Length: 18 Bit Score: 37.89 E-value: 6.27e-04
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| PX_domain super family | cl02563 | The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ... |
356-456 | 2.29e-03 | ||||||
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting. The actual alignment was detected with superfamily member cd06883: Pssm-ID: 470617 Cd Length: 109 Bit Score: 38.88 E-value: 2.29e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
682-1013 | 1.23e-04 | ||||||
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo. Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 46.45 E-value: 1.23e-04
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| zf-CCHC | pfam00098 | Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ... |
1123-1138 | 6.27e-04 | ||||||
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger. Pssm-ID: 395050 [Multi-domain] Cd Length: 18 Bit Score: 37.89 E-value: 6.27e-04
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| PX_PI3K_C2 | cd06883 | The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The ... |
356-456 | 2.29e-03 | ||||||
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are also involved in the regulation of clathrin-mediated membrane trafficking as well as ATP-dependent priming of neurosecretory granule exocytosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. Class II PI3Ks include three vertebrate isoforms (alpha, beta, and gamma), the Drosophila PI3K_68D, and similar proteins. Pssm-ID: 132793 Cd Length: 109 Bit Score: 38.88 E-value: 2.29e-03
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| PHA03379 | PHA03379 | EBNA-3A; Provisional |
645-954 | 3.33e-03 | ||||||
EBNA-3A; Provisional Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 41.58 E-value: 3.33e-03
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| PTZ00368 | PTZ00368 | universal minicircle sequence binding protein (UMSBP); Provisional |
1113-1136 | 5.19e-03 | ||||||
universal minicircle sequence binding protein (UMSBP); Provisional Pssm-ID: 173561 [Multi-domain] Cd Length: 148 Bit Score: 38.63 E-value: 5.19e-03
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| ZnF_C2HC | smart00343 | zinc finger; |
1123-1138 | 5.86e-03 | ||||||
zinc finger; Pssm-ID: 197667 [Multi-domain] Cd Length: 17 Bit Score: 35.11 E-value: 5.86e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
682-1013 | 1.23e-04 | ||||||
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo. Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 46.45 E-value: 1.23e-04
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| Atrophin-1 | pfam03154 | Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
697-935 | 4.42e-04 | ||||||
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity. Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 44.37 E-value: 4.42e-04
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| zf-CCHC | pfam00098 | Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ... |
1123-1138 | 6.27e-04 | ||||||
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger. Pssm-ID: 395050 [Multi-domain] Cd Length: 18 Bit Score: 37.89 E-value: 6.27e-04
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| PX_PI3K_C2 | cd06883 | The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The ... |
356-456 | 2.29e-03 | ||||||
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are also involved in the regulation of clathrin-mediated membrane trafficking as well as ATP-dependent priming of neurosecretory granule exocytosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. Class II PI3Ks include three vertebrate isoforms (alpha, beta, and gamma), the Drosophila PI3K_68D, and similar proteins. Pssm-ID: 132793 Cd Length: 109 Bit Score: 38.88 E-value: 2.29e-03
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| Nucleoporin_FG2 | pfam15967 | Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ... |
899-992 | 2.38e-03 | ||||||
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif. Pssm-ID: 435043 [Multi-domain] Cd Length: 586 Bit Score: 41.96 E-value: 2.38e-03
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| PHA03379 | PHA03379 | EBNA-3A; Provisional |
645-954 | 3.33e-03 | ||||||
EBNA-3A; Provisional Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 41.58 E-value: 3.33e-03
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
732-957 | 3.99e-03 | ||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.46 E-value: 3.99e-03
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
769-1004 | 4.64e-03 | ||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.46 E-value: 4.64e-03
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| PTZ00368 | PTZ00368 | universal minicircle sequence binding protein (UMSBP); Provisional |
1113-1136 | 5.19e-03 | ||||||
universal minicircle sequence binding protein (UMSBP); Provisional Pssm-ID: 173561 [Multi-domain] Cd Length: 148 Bit Score: 38.63 E-value: 5.19e-03
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| ZnF_C2HC | smart00343 | zinc finger; |
1123-1138 | 5.86e-03 | ||||||
zinc finger; Pssm-ID: 197667 [Multi-domain] Cd Length: 17 Bit Score: 35.11 E-value: 5.86e-03
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| PX_NoxO1 | cd06889 | The phosphoinositide binding Phox Homology domain of Nox Organizing protein 1; The PX domain ... |
343-435 | 6.46e-03 | ||||||
The phosphoinositide binding Phox Homology domain of Nox Organizing protein 1; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Nox Organizing protein 1 (NoxO1) is a critical regulator of enzyme kinetics of the nonphagocytic NADPH oxidase Nox1, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Nox1 is expressed in colon, stomach, uterus, prostate, and vascular smooth muscle cells. NoxO1, a homolog of the p47phox subunit of phagocytic NADPH oxidase, is involved in targeting activator subunits (such as NoxA1) to Nox1. It is co-localized with Nox1 in the membranes of resting cells and directs the subcellular localization of Nox1. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of NoxO1 preferentially binds phosphatidylinositol-3,5-bisphosphate [PI(3,5)P2], PI5P, and PI4P. Pssm-ID: 132799 Cd Length: 121 Bit Score: 37.75 E-value: 6.46e-03
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| PX_p47phox | cd06887 | The phosphoinositide binding Phox Homology domain of the p47phox subunit of NADPH oxidase; The ... |
349-454 | 9.99e-03 | ||||||
The phosphoinositide binding Phox Homology domain of the p47phox subunit of NADPH oxidase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p47phox is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox), which plays a key role in the ability of phagocytes to defend against bacterial infections. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p47phox is required for activation of NADH oxidase and plays a role in translocation. It contains an N-terminal PX domain, two Src Homology 3 (SH3) domains, and a C-terminal domain that contains PxxP motifs for binding SH3 domains. The PX domain of p47phox is unique in that it contains two distinct basic pockets on the membrane-binding surface: one preferentially binds phosphatidylinositol-3,4-bisphosphate [PI(3,4)P2] and is analogous to the PI3P-binding pocket of p40phox, while the other binds anionic phospholipids such as phosphatidic acid or phosphatidylserine. Simultaneous binding in the two pockets results in increased membrane affinity. The PX domain of p47phox is also involved in protein-protein interaction. Pssm-ID: 132797 Cd Length: 118 Bit Score: 37.12 E-value: 9.99e-03
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