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Conserved domains on  [gi|1841445658|ref|NP_001369466|]
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amyloid beta precursor like protein 2 isoform 21 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
A4_EXTRA smart00006
amyloid A4; amyloid A4 precursor of Alzheimers disease
 42-204 3.59e-106

amyloid A4; amyloid A4 precursor of Alzheimers disease


:

Pssm-ID: 128326 [Multi-domain]  Cd Length: 165  Bit Score: 318.68  E-value: 3.59e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658   42 GTGFAVAEPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCFETKEEVLQYCQEMYPELQITNVMEANQRVSIDNWCRRDKK 121
Cdd:smart00006   1 GAAGALAEPQIAMLCGRLNMHMNVQTGRWETDPSRTKTCLRDKEDILQYCRKAYPELQITNVVEASQPVTIQNWCRRGRS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658  122 QCKS--RFVTPFKCLVGEFVSDVLLVPEKCQFFHKERMEVCENHQHWHTVVKEACLTQGMTLYSYGMLLPCGVDQFHGTE 199
Cdd:smart00006  81 QCKThhHFVIPFRCLVGEFVSDALLVPEGCQFLHQERMDQCETHQRWHQEAKEACSEKGMILHSFGMLLPCGIDKFRGVE 160


                   ....*
gi 1841445658  200 YVCCP 204
Cdd:smart00006 161 FVCCP 165
APP_E2 pfam12925
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ...
 309-464 6.06e-68

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: 220.29  E-value: 6.06e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658 309 PPTPLPTNDVDVYFETSADDNEHARFQKAKEQLEIRHRNRMDRVKKEWEEAELQAKNLPKAE-------RQTLIQHFQAM 381
Cdd:pfam12925   1 TTTPPPTDAVDPYFEHPDPRNEHESFKKAKKRLEEKHRERMTKVMKEWEEAEERYQNLPKADpkaaekfKKAMTARFQET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658 382 VKALEKEAASEKQQLVETHLARVEAMLNDRRRMALENYLAALQSDPP---------------------------RHVLAV 434
Cdd:pfam12925  81 VEALEEEAAAERQQLVETHQQRVEAHLNDRRRDALECYLQALQENPPnphrilkalkkllraeqkdrrhtlrhyRHLLAS 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1841445658 435 DPEKAAQMKSQVMTHLHVIEERRNQSLSLL 464
Cdd:pfam12925 161 DPEKAEQMKPQVLTHLRVIDRRMNQSLTLL 190
JMTM_APLP2 cd21709
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and ...
 585-665 5.10e-53

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: 176.66  E-value: 5.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658 585 SVGPLREDFSLSSSALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 664
Cdd:cd21709     1 SDGPLRDDFSFSSSALIGLLVIAVAIATVIVISLVLLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 80


                  .
gi 1841445658 665 Q 665
Cdd:cd21709    81 Q 81
 
Name Accession Description Interval E-value
A4_EXTRA smart00006
amyloid A4; amyloid A4 precursor of Alzheimers disease
 42-204 3.59e-106

amyloid A4; amyloid A4 precursor of Alzheimers disease


Pssm-ID: 128326 [Multi-domain]  Cd Length: 165  Bit Score: 318.68  E-value: 3.59e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658   42 GTGFAVAEPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCFETKEEVLQYCQEMYPELQITNVMEANQRVSIDNWCRRDKK 121
Cdd:smart00006   1 GAAGALAEPQIAMLCGRLNMHMNVQTGRWETDPSRTKTCLRDKEDILQYCRKAYPELQITNVVEASQPVTIQNWCRRGRS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658  122 QCKS--RFVTPFKCLVGEFVSDVLLVPEKCQFFHKERMEVCENHQHWHTVVKEACLTQGMTLYSYGMLLPCGVDQFHGTE 199
Cdd:smart00006  81 QCKThhHFVIPFRCLVGEFVSDALLVPEGCQFLHQERMDQCETHQRWHQEAKEACSEKGMILHSFGMLLPCGIDKFRGVE 160


                   ....*
gi 1841445658  200 YVCCP 204
Cdd:smart00006 161 FVCCP 165
APP_E2 pfam12925
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ...
 309-464 6.06e-68

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: 220.29  E-value: 6.06e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658 309 PPTPLPTNDVDVYFETSADDNEHARFQKAKEQLEIRHRNRMDRVKKEWEEAELQAKNLPKAE-------RQTLIQHFQAM 381
Cdd:pfam12925   1 TTTPPPTDAVDPYFEHPDPRNEHESFKKAKKRLEEKHRERMTKVMKEWEEAEERYQNLPKADpkaaekfKKAMTARFQET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658 382 VKALEKEAASEKQQLVETHLARVEAMLNDRRRMALENYLAALQSDPP---------------------------RHVLAV 434
Cdd:pfam12925  81 VEALEEEAAAERQQLVETHQQRVEAHLNDRRRDALECYLQALQENPPnphrilkalkkllraeqkdrrhtlrhyRHLLAS 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1841445658 435 DPEKAAQMKSQVMTHLHVIEERRNQSLSLL 464
Cdd:pfam12925 161 DPEKAEQMKPQVLTHLRVIDRRMNQSLTLL 190
APP_N pfam02177
Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor ...
 49-147 2.42e-59

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: 194.06  E-value: 2.42e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658  49 EPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCFETKEEVLQYCQEMYPELQITNVMEANQRVSIDNWCRRDKKQCK-SRF 127
Cdd:pfam02177   1 EPQVAMFCGKLNQHMDLETGRWEPDPSGKATCFKDKEEILDYCQKVYPELDITNIVEASQPVTIDNWCKKGRKKCKgHHI 80

                          90       100
                  ....*....|....*....|
gi 1841445658 128 VTPFKCLVGEFVSDVLLVPE 147
Cdd:pfam02177  81 VKPYRCLVGEFVSDALLVPE 100
JMTM_APLP2 cd21709
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and ...
 585-665 5.10e-53

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: 176.66  E-value: 5.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658 585 SVGPLREDFSLSSSALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 664
Cdd:cd21709     1 SDGPLRDDFSFSSSALIGLLVIAVAIATVIVISLVLLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 80


                  .
gi 1841445658 665 Q 665
Cdd:cd21709    81 Q 81
APP_amyloid pfam10515
Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the ...
 614-664 1.60e-25

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: 99.33  E-value: 1.60e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1841445658 614 IVISLVMLRKR-QYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 664
Cdd:pfam10515   1 IVVGMALLRRRaARSPSAHGFVEVDPNVTPEERHVANMQVNGYENPTYKYFE 52
PRK06991 PRK06991
electron transport complex subunit RsxB;
305-444 1.08e-03

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 41.32  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658 305 DVKVPPTPLptNDVDVYFETSADDNEHARFQKAKEQLEIRHRNRMDRVKKEWEEAELQAKNLPKAERQTLIQHFQAMVKA 384
Cdd:PRK06991  121 DLCVPPCPV--DCIDMVPVTGERTGWDAWSQAQADAARARHDARQARLRREREAAEARAAARAAASAAAAAAEASAAAAP 198

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658 385 LEKEAASEKQQLVETHLARVEAmlndrRRMALenylaALQSDPPRHVLAVDPEKAAQMKS 444
Cdd:PRK06991  199 AADDAEAKKRAIIAAALERARK-----KKEEL-----AAQGAGPKNTEGVSAAVQAQIDA 248
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
330-487 6.99e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 6.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658  330 EHARFQKAKEQLEiRHRNRMDRVKKEWEEAELQAKNLpKAERQTLIQHFQAMVKALEKEAASEKQQLvETHLARVEAMLN 409
Cdd:COG4913    279 AALRLWFAQRRLE-LLEAELEELRAELARLEAELERL-EARLDALREELDELEAQIRGNGGDRLEQL-EREIERLERELE 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658  410 DR--RRMALENYLAALQSDPPrhvlaVDPEKAAQMKSQVMTHLHVIEERRNQSLSLLYKVPYVAQEIQEEIDELLQEQRA 487
Cdd:COG4913    356 ERerRRARLEALLAALGLPLP-----ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
 
Name Accession Description Interval E-value
A4_EXTRA smart00006
amyloid A4; amyloid A4 precursor of Alzheimers disease
 42-204 3.59e-106

amyloid A4; amyloid A4 precursor of Alzheimers disease


Pssm-ID: 128326 [Multi-domain]  Cd Length: 165  Bit Score: 318.68  E-value: 3.59e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658   42 GTGFAVAEPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCFETKEEVLQYCQEMYPELQITNVMEANQRVSIDNWCRRDKK 121
Cdd:smart00006   1 GAAGALAEPQIAMLCGRLNMHMNVQTGRWETDPSRTKTCLRDKEDILQYCRKAYPELQITNVVEASQPVTIQNWCRRGRS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658  122 QCKS--RFVTPFKCLVGEFVSDVLLVPEKCQFFHKERMEVCENHQHWHTVVKEACLTQGMTLYSYGMLLPCGVDQFHGTE 199
Cdd:smart00006  81 QCKThhHFVIPFRCLVGEFVSDALLVPEGCQFLHQERMDQCETHQRWHQEAKEACSEKGMILHSFGMLLPCGIDKFRGVE 160


                   ....*
gi 1841445658  200 YVCCP 204
Cdd:smart00006 161 FVCCP 165
APP_E2 pfam12925
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ...
 309-464 6.06e-68

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: 220.29  E-value: 6.06e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658 309 PPTPLPTNDVDVYFETSADDNEHARFQKAKEQLEIRHRNRMDRVKKEWEEAELQAKNLPKAE-------RQTLIQHFQAM 381
Cdd:pfam12925   1 TTTPPPTDAVDPYFEHPDPRNEHESFKKAKKRLEEKHRERMTKVMKEWEEAEERYQNLPKADpkaaekfKKAMTARFQET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658 382 VKALEKEAASEKQQLVETHLARVEAMLNDRRRMALENYLAALQSDPP---------------------------RHVLAV 434
Cdd:pfam12925  81 VEALEEEAAAERQQLVETHQQRVEAHLNDRRRDALECYLQALQENPPnphrilkalkkllraeqkdrrhtlrhyRHLLAS 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1841445658 435 DPEKAAQMKSQVMTHLHVIEERRNQSLSLL 464
Cdd:pfam12925 161 DPEKAEQMKPQVLTHLRVIDRRMNQSLTLL 190
APP_N pfam02177
Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor ...
 49-147 2.42e-59

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: 194.06  E-value: 2.42e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658  49 EPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCFETKEEVLQYCQEMYPELQITNVMEANQRVSIDNWCRRDKKQCK-SRF 127
Cdd:pfam02177   1 EPQVAMFCGKLNQHMDLETGRWEPDPSGKATCFKDKEEILDYCQKVYPELDITNIVEASQPVTIDNWCKKGRKKCKgHHI 80

                          90       100
                  ....*....|....*....|
gi 1841445658 128 VTPFKCLVGEFVSDVLLVPE 147
Cdd:pfam02177  81 VKPYRCLVGEFVSDALLVPE 100
JMTM_APLP2 cd21709
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and ...
 585-665 5.10e-53

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: 176.66  E-value: 5.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658 585 SVGPLREDFSLSSSALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 664
Cdd:cd21709     1 SDGPLRDDFSFSSSALIGLLVIAVAIATVIVISLVLLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 80


                  .
gi 1841445658 665 Q 665
Cdd:cd21709    81 Q 81
JMTM_APLP1 cd21708
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 1 (APLP-1) and ...
 594-665 7.12e-36

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: 129.94  E-value: 7.12e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841445658 594 SLSSSALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLEQ 665
Cdd:cd21708    14 TFNRGALIGLLVVAVAVAMVIVISLLLVRRKPYGTISHGIVEVDPMLTPEERQLSKMQNHGYENPTYRFLEE 85
APP_Cu_bd pfam12924
Copper-binding of amyloid precursor, CuBD; This short domain, part of the extra-cellular ...
 149-204 6.41e-33

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: 120.46  E-value: 6.41e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1841445658 149 CQFFHKERMEVCENHQHWHTVVKEACLTQGMTLYSYGMLLPCGVDQFHGTEYVCCP 204
Cdd:pfam12924   1 CKFDHKHNMDVCESHQHWHATAKEACAARGMVLHSFGMLLPCGIDLFTGVEFVCCP 56
APP_amyloid pfam10515
Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the ...
 614-664 1.60e-25

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: 99.33  E-value: 1.60e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1841445658 614 IVISLVMLRKR-QYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 664
Cdd:pfam10515   1 IVVGMALLRRRaARSPSAHGFVEVDPNVTPEERHVANMQVNGYENPTYKYFE 52
JMTM_APP_like cd21699
juxtamembrane and transmembrane (JMTM) domain found in the amyloid-beta precursor protein (APP) ...
 585-624 1.07e-09

juxtamembrane and transmembrane (JMTM) domain found in the amyloid-beta precursor protein (APP) family; The amyloid-beta precursor protein (APP) family includes amyloid-like proteins APLP-1 and APLP-2. APP (also called ABPP, APPI, Alzheimer disease (AD) amyloid protein, amyloid precursor protein, amyloid-beta A4 protein, cerebral vascular amyloid peptide (CVAP), PreA4, or protease nexin-II (PN-II)) functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity; they bind transient metals such as copper, zinc and iron. 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. 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 APP, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region. More than half of all familial APP mutations of Alzheimer's disease are seen in its JMTM domain region.


Pssm-ID: 411982  Cd Length: 41  Bit Score: 54.21  E-value: 1.07e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1841445658 585 SVGPLREDFS-LSSSALIGLLVIAVAIATVIVISLVMLRKR 624
Cdd:cd21699     1 ERVFLAEDSSnSSFGAVIGLAVGGVAVAIVIVVAVVMLRRR 41
JMTM_APP cd21707
juxtamembrane and transmembrane (JMTM) domain found in amyloid-beta precursor protein (APP) ...
 591-624 1.95e-04

juxtamembrane and transmembrane (JMTM) domain found in amyloid-beta precursor protein (APP) and similar proteins; Amyloid-beta precursor protein (APP), also called APPI, ABPP, Alzheimer disease amyloid protein, amyloid precursor protein, amyloid-beta A4 protein, cerebral vascular amyloid peptide (CVAP), PreA4, or protease nexin-II (PN-II), functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity; they bind transient metals such as copper, zinc and iron. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APP, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region. More than half of all familial APP mutations of Alzheimer's disease are seen in its JMTM domain region.


Pssm-ID: 411990  Cd Length: 40  Bit Score: 39.16  E-value: 1.95e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1841445658 591 EDFSLSSSALIGLLVIAVAIATVIVISLVMLRKR 624
Cdd:cd21707     7 EDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKK 40
PRK06991 PRK06991
electron transport complex subunit RsxB;
305-444 1.08e-03

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 41.32  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658 305 DVKVPPTPLptNDVDVYFETSADDNEHARFQKAKEQLEIRHRNRMDRVKKEWEEAELQAKNLPKAERQTLIQHFQAMVKA 384
Cdd:PRK06991  121 DLCVPPCPV--DCIDMVPVTGERTGWDAWSQAQADAARARHDARQARLRREREAAEARAAARAAASAAAAAAEASAAAAP 198

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658 385 LEKEAASEKQQLVETHLARVEAmlndrRRMALenylaALQSDPPRHVLAVDPEKAAQMKS 444
Cdd:PRK06991  199 AADDAEAKKRAIIAAALERARK-----KKEEL-----AAQGAGPKNTEGVSAAVQAQIDA 248
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
330-487 6.99e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 6.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658  330 EHARFQKAKEQLEiRHRNRMDRVKKEWEEAELQAKNLpKAERQTLIQHFQAMVKALEKEAASEKQQLvETHLARVEAMLN 409
Cdd:COG4913    279 AALRLWFAQRRLE-LLEAELEELRAELARLEAELERL-EARLDALREELDELEAQIRGNGGDRLEQL-EREIERLERELE 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445658  410 DR--RRMALENYLAALQSDPPrhvlaVDPEKAAQMKSQVMTHLHVIEERRNQSLSLLYKVPYVAQEIQEEIDELLQEQRA 487
Cdd:COG4913    356 ERerRRARLEALLAALGLPLP-----ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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