similar to hypothetical protein LOC199675 (predicted) [Rattus norvegicus]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Lectin_N super family | cl04343 | Hepatic lectin, N-terminal domain; This is the N-terminal domain found in hepatic lectins, ... |
66-146 | 3.06e-03 | |||
Hepatic lectin, N-terminal domain; This is the N-terminal domain found in hepatic lectins, also known as Asialoglycoprotein receptors (ASGRs). ASGRs function as scavengers to mediate the endocytosis of plasma glycoproteins with terminal galactose and N-acetylgalactosamine units. ASGR is composed of a major (ASGR1) and a minor (ASGR2) subunits, both of which are type II, single-pass transmembrane proteins. ASGR is highly expressed in liver but has been also identified in human peripheral blood monocytes, representing a mobile pool of the receptor reaching distant sites from the liver to play a scavenger function where there is an infection or a damaged tissue. This domain includes the short, single transmembrane domain and the stalk region which mediates the oligomerization between subunits. The actual alignment was detected with superfamily member pfam03954: Pssm-ID: 461106 Cd Length: 140 Bit Score: 36.53 E-value: 3.06e-03
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Name | Accession | Description | Interval | E-value | |||
Lectin_N | pfam03954 | Hepatic lectin, N-terminal domain; This is the N-terminal domain found in hepatic lectins, ... |
66-146 | 3.06e-03 | |||
Hepatic lectin, N-terminal domain; This is the N-terminal domain found in hepatic lectins, also known as Asialoglycoprotein receptors (ASGRs). ASGRs function as scavengers to mediate the endocytosis of plasma glycoproteins with terminal galactose and N-acetylgalactosamine units. ASGR is composed of a major (ASGR1) and a minor (ASGR2) subunits, both of which are type II, single-pass transmembrane proteins. ASGR is highly expressed in liver but has been also identified in human peripheral blood monocytes, representing a mobile pool of the receptor reaching distant sites from the liver to play a scavenger function where there is an infection or a damaged tissue. This domain includes the short, single transmembrane domain and the stalk region which mediates the oligomerization between subunits. Pssm-ID: 461106 Cd Length: 140 Bit Score: 36.53 E-value: 3.06e-03
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EnvC | COG4942 | Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
73-182 | 4.83e-03 | |||
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 36.67 E-value: 4.83e-03
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Name | Accession | Description | Interval | E-value | |||
Lectin_N | pfam03954 | Hepatic lectin, N-terminal domain; This is the N-terminal domain found in hepatic lectins, ... |
66-146 | 3.06e-03 | |||
Hepatic lectin, N-terminal domain; This is the N-terminal domain found in hepatic lectins, also known as Asialoglycoprotein receptors (ASGRs). ASGRs function as scavengers to mediate the endocytosis of plasma glycoproteins with terminal galactose and N-acetylgalactosamine units. ASGR is composed of a major (ASGR1) and a minor (ASGR2) subunits, both of which are type II, single-pass transmembrane proteins. ASGR is highly expressed in liver but has been also identified in human peripheral blood monocytes, representing a mobile pool of the receptor reaching distant sites from the liver to play a scavenger function where there is an infection or a damaged tissue. This domain includes the short, single transmembrane domain and the stalk region which mediates the oligomerization between subunits. Pssm-ID: 461106 Cd Length: 140 Bit Score: 36.53 E-value: 3.06e-03
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EnvC | COG4942 | Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
73-182 | 4.83e-03 | |||
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 36.67 E-value: 4.83e-03
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Blast search parameters | ||||
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