sperm-associated antigen 4 protein isoform X1 [Mus musculus]
SUN domain-containing protein( domain architecture ID 10543997)
SUN (Sad1-UNC-84 homology) domain-containing protein may be involved in nuclear migration, meiotic telomere tethering, and antiviral responses
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Sad1_UNC | pfam07738 | Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ... |
214-346 | 4.41e-55 | |||
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that is involved in nuclear anchoring and migration during development. The S. pombe Sad1 protein localizes at the spindle pole body. UNC-84 and and Sad1 share a common C-terminal region, that is often termed the SUN (Sad1 and UNC) domain. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm. : Pssm-ID: 400199 Cd Length: 130 Bit Score: 176.71 E-value: 4.41e-55
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PMI_typeI_cat super family | cl48665 | Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain ... |
5-74 | 5.00e-04 | |||
Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8) which contains a zinc-binding site. It is composed of beta-strands connected by long loops in a jelly roll conformation. The actual alignment was detected with superfamily member pfam20511: Pssm-ID: 466660 [Multi-domain] Cd Length: 143 Bit Score: 39.86 E-value: 5.00e-04
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Name | Accession | Description | Interval | E-value | |||
Sad1_UNC | pfam07738 | Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ... |
214-346 | 4.41e-55 | |||
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that is involved in nuclear anchoring and migration during development. The S. pombe Sad1 protein localizes at the spindle pole body. UNC-84 and and Sad1 share a common C-terminal region, that is often termed the SUN (Sad1 and UNC) domain. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm. Pssm-ID: 400199 Cd Length: 130 Bit Score: 176.71 E-value: 4.41e-55
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PMI_typeI_cat | pfam20511 | Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain ... |
5-74 | 5.00e-04 | |||
Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8) which contains a zinc-binding site. It is composed of beta-strands connected by long loops in a jelly roll conformation. Pssm-ID: 466660 [Multi-domain] Cd Length: 143 Bit Score: 39.86 E-value: 5.00e-04
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Name | Accession | Description | Interval | E-value | |||
Sad1_UNC | pfam07738 | Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ... |
214-346 | 4.41e-55 | |||
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that is involved in nuclear anchoring and migration during development. The S. pombe Sad1 protein localizes at the spindle pole body. UNC-84 and and Sad1 share a common C-terminal region, that is often termed the SUN (Sad1 and UNC) domain. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm. Pssm-ID: 400199 Cd Length: 130 Bit Score: 176.71 E-value: 4.41e-55
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PMI_typeI_cat | pfam20511 | Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain ... |
5-74 | 5.00e-04 | |||
Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8) which contains a zinc-binding site. It is composed of beta-strands connected by long loops in a jelly roll conformation. Pssm-ID: 466660 [Multi-domain] Cd Length: 143 Bit Score: 39.86 E-value: 5.00e-04
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Blast search parameters | ||||
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