beta amyloid protein precursor-like, isoform A [Drosophila melanogaster]
Protein Classification
DDRGK domain-containing protein( domain architecture ID 13258441)
DDRGK domain-containing protein similar to Arabidopsis thaliana DDRGK domain-containing protein 1 that is a substrate adapter for ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| APP_E2 | pfam12925 | E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ... |
388-580 | 2.41e-99 | ||||
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains of the amyloid precursor protein. The structure of E2 consists of two coiled-coil sub-structures connected through a continuous helix, and bears an unexpected resemblance to the spectrin family of protein structures.E 2 can reversibly dimerize in solution, and the dimerization occurs along the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against the C-terminal substructure of a second monomer. The high degree of conservation of residues at the putative dimer interface suggests that the E2 dimer observed in the crystal could be physiologically relevant. Heparin sulfate proteoglycans, the putative ligands for the precursor present in extracellular matrix, bind to E2 at a conserved and positively charged site near the dimer interface. : Pssm-ID: 463752 Cd Length: 190 Bit Score: 307.73 E-value: 2.41e-99
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| A4_EXTRA super family | cl30964 | amyloid A4; amyloid A4 precursor of Alzheimers disease |
26-198 | 1.75e-95 | ||||
amyloid A4; amyloid A4 precursor of Alzheimers disease The actual alignment was detected with superfamily member smart00006: Pssm-ID: 128326 [Multi-domain] Cd Length: 165 Bit Score: 296.72 E-value: 1.75e-95
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| APP_amyloid | pfam10515 | Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the ... |
835-884 | 1.08e-19 | ||||
Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the beta-Amyloid precursor protein (APP) which is a conserved and ubiquitous transmembrane glycoprotein strongly implicated in the pathogenesis of Alzheimer's disease but whose normal biological function is unknown. The C-terminal 100 residues are released and aggregate into amyloid deposits which are strongly implicated in the pathology of Alzheimer's disease plaque-formation. The domain is associated with family A4_EXTRA, pfam02177, further towards the N-terminus. : Pssm-ID: 463129 Cd Length: 52 Bit Score: 83.15 E-value: 1.08e-19
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| DDRGK super family | cl25550 | DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
632-682 | 6.63e-04 | ||||
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif. The actual alignment was detected with superfamily member pfam09756: Pssm-ID: 370664 [Multi-domain] Cd Length: 188 Bit Score: 41.56 E-value: 6.63e-04
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| Name | Accession | Description | Interval | E-value | |||||
| APP_E2 | pfam12925 | E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ... |
388-580 | 2.41e-99 | |||||
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains of the amyloid precursor protein. The structure of E2 consists of two coiled-coil sub-structures connected through a continuous helix, and bears an unexpected resemblance to the spectrin family of protein structures.E 2 can reversibly dimerize in solution, and the dimerization occurs along the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against the C-terminal substructure of a second monomer. The high degree of conservation of residues at the putative dimer interface suggests that the E2 dimer observed in the crystal could be physiologically relevant. Heparin sulfate proteoglycans, the putative ligands for the precursor present in extracellular matrix, bind to E2 at a conserved and positively charged site near the dimer interface. Pssm-ID: 463752 Cd Length: 190 Bit Score: 307.73 E-value: 2.41e-99
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| A4_EXTRA | smart00006 | amyloid A4; amyloid A4 precursor of Alzheimers disease |
26-198 | 1.75e-95 | |||||
amyloid A4; amyloid A4 precursor of Alzheimers disease Pssm-ID: 128326 [Multi-domain] Cd Length: 165 Bit Score: 296.72 E-value: 1.75e-95
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| APP_N | pfam02177 | Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor ... |
33-141 | 6.30e-45 | |||||
Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor protein, is the heparin-binding domain of the protein. this region is also responsible for stimulation of neurite outgrowth. The structure reveals both a highly charged basic surface that may interact with glycosaminoglycans in the brain and an abutting hydrophobic surface that is proposed to play an important functional role such as in dimerization or ligand-binding. Structural similarities with cysteine-rich growth factors, taken together with its known growth-promoting properties, suggest the APP N-terminal domain could function as a growth factor in vivo. Pssm-ID: 460474 Cd Length: 100 Bit Score: 156.69 E-value: 6.30e-45
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| APP_amyloid | pfam10515 | Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the ... |
835-884 | 1.08e-19 | |||||
Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the beta-Amyloid precursor protein (APP) which is a conserved and ubiquitous transmembrane glycoprotein strongly implicated in the pathogenesis of Alzheimer's disease but whose normal biological function is unknown. The C-terminal 100 residues are released and aggregate into amyloid deposits which are strongly implicated in the pathology of Alzheimer's disease plaque-formation. The domain is associated with family A4_EXTRA, pfam02177, further towards the N-terminus. Pssm-ID: 463129 Cd Length: 52 Bit Score: 83.15 E-value: 1.08e-19
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| JMTM_APLP1 | cd21708 | juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 1 (APLP-1) and ... |
840-884 | 5.34e-05 | |||||
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 1 (APLP-1) and similar proteins; Amyloid-like protein 1 (APLP-1), also called APLP, may play a role in postsynaptic function. It couples to JIP signal transduction through C-terminal binding. APLP-1 may interact with cellular G-protein signaling pathways. It can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of APLP-1, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region. Pssm-ID: 411991 Cd Length: 85 Bit Score: 42.50 E-value: 5.34e-05
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| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
410-684 | 4.83e-04 | |||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 4.83e-04
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| DDRGK | pfam09756 | DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
632-682 | 6.63e-04 | |||||
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif. Pssm-ID: 370664 [Multi-domain] Cd Length: 188 Bit Score: 41.56 E-value: 6.63e-04
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| GBP_C | cd16269 | Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
629-682 | 6.40e-03 | |||||
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines. Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.48 E-value: 6.40e-03
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| Name | Accession | Description | Interval | E-value | |||||
| APP_E2 | pfam12925 | E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ... |
388-580 | 2.41e-99 | |||||
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains of the amyloid precursor protein. The structure of E2 consists of two coiled-coil sub-structures connected through a continuous helix, and bears an unexpected resemblance to the spectrin family of protein structures.E 2 can reversibly dimerize in solution, and the dimerization occurs along the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against the C-terminal substructure of a second monomer. The high degree of conservation of residues at the putative dimer interface suggests that the E2 dimer observed in the crystal could be physiologically relevant. Heparin sulfate proteoglycans, the putative ligands for the precursor present in extracellular matrix, bind to E2 at a conserved and positively charged site near the dimer interface. Pssm-ID: 463752 Cd Length: 190 Bit Score: 307.73 E-value: 2.41e-99
|
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| A4_EXTRA | smart00006 | amyloid A4; amyloid A4 precursor of Alzheimers disease |
26-198 | 1.75e-95 | |||||
amyloid A4; amyloid A4 precursor of Alzheimers disease Pssm-ID: 128326 [Multi-domain] Cd Length: 165 Bit Score: 296.72 E-value: 1.75e-95
|
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| APP_N | pfam02177 | Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor ... |
33-141 | 6.30e-45 | |||||
Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor protein, is the heparin-binding domain of the protein. this region is also responsible for stimulation of neurite outgrowth. The structure reveals both a highly charged basic surface that may interact with glycosaminoglycans in the brain and an abutting hydrophobic surface that is proposed to play an important functional role such as in dimerization or ligand-binding. Structural similarities with cysteine-rich growth factors, taken together with its known growth-promoting properties, suggest the APP N-terminal domain could function as a growth factor in vivo. Pssm-ID: 460474 Cd Length: 100 Bit Score: 156.69 E-value: 6.30e-45
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| APP_Cu_bd | pfam12924 | Copper-binding of amyloid precursor, CuBD; This short domain, part of the extra-cellular ... |
143-198 | 2.30e-29 | |||||
Copper-binding of amyloid precursor, CuBD; This short domain, part of the extra-cellular N-terminus of the amyloid precursor protein, APP, can bind both copper and zinc, CuBD. The structure of Cu2+-bound CuBD reveals that the metal ligands are His147, His151, Tyr168 and two water molecules, which are arranged in a square pyramidal geometry. The structure of Cu+-bound CuBD is almost identical to the Cu2+-bound structure except for the loss of one of the water ligands. The geometry of the site is unfavourable for Cu+, thus providing a mechanism by which CuBD could readily transfer Cu ions to other proteins. Pssm-ID: 463751 Cd Length: 56 Bit Score: 110.83 E-value: 2.30e-29
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| APP_amyloid | pfam10515 | Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the ... |
835-884 | 1.08e-19 | |||||
Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the beta-Amyloid precursor protein (APP) which is a conserved and ubiquitous transmembrane glycoprotein strongly implicated in the pathogenesis of Alzheimer's disease but whose normal biological function is unknown. The C-terminal 100 residues are released and aggregate into amyloid deposits which are strongly implicated in the pathology of Alzheimer's disease plaque-formation. The domain is associated with family A4_EXTRA, pfam02177, further towards the N-terminus. Pssm-ID: 463129 Cd Length: 52 Bit Score: 83.15 E-value: 1.08e-19
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| JMTM_APLP1 | cd21708 | juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 1 (APLP-1) and ... |
840-884 | 5.34e-05 | |||||
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 1 (APLP-1) and similar proteins; Amyloid-like protein 1 (APLP-1), also called APLP, may play a role in postsynaptic function. It couples to JIP signal transduction through C-terminal binding. APLP-1 may interact with cellular G-protein signaling pathways. It can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of APLP-1, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region. Pssm-ID: 411991 Cd Length: 85 Bit Score: 42.50 E-value: 5.34e-05
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| JMTM_APLP2 | cd21709 | juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and ... |
844-884 | 1.53e-04 | |||||
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and similar proteins; Amyloid-like protein 2 (APLP-2), also called amyloid protein homolog (APPH), or CDEI box-binding protein (CDEBP), may play a role in the regulation of hemostasis. Its soluble form may have inhibitory properties towards coagulation factors. APLP-2 may bind to the DNA 5'-GTCACATG-3'(CDEI box). It inhibits trypsin, chymotrypsin, plasmin, factor XIA, and plasma and glandular kallikrein. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APLP-2, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region. Pssm-ID: 411992 Cd Length: 81 Bit Score: 41.07 E-value: 1.53e-04
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| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
410-684 | 4.83e-04 | |||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 4.83e-04
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| DDRGK | pfam09756 | DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
632-682 | 6.63e-04 | |||||
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif. Pssm-ID: 370664 [Multi-domain] Cd Length: 188 Bit Score: 41.56 E-value: 6.63e-04
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| CCDC47 | pfam07946 | PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
625-682 | 8.43e-04 | |||||
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway. Pssm-ID: 462322 Cd Length: 323 Bit Score: 42.55 E-value: 8.43e-04
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| RIB43A | pfam05914 | RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ... |
613-684 | 3.93e-03 | |||||
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells. Pssm-ID: 461780 [Multi-domain] Cd Length: 372 Bit Score: 40.65 E-value: 3.93e-03
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| GBP_C | cd16269 | Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
629-682 | 6.40e-03 | |||||
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines. Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.48 E-value: 6.40e-03
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| Blast search parameters | ||||
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