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Conserved domains on  [gi|1905916|gb|AAB50173|]
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amyloid precursor-like protein 1 [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
 46-211 3.58e-101

amyloid A4; amyloid A4 precursor of Alzheimers disease


:

Pssm-ID: 128326 [Multi-domain]  Cd Length: 165  Bit Score: 305.58  E-value: 3.58e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916      46 GAAEAPGSAQVAGLCGRLTLHRDLRTGRWEPDPQRSRRCLRDPQRVLEYCRQMYPELQIARVEQATQAIPMERWCGGSRS 125
Cdd:smart00006   1 GAAGALAEPQIAMLCGRLNMHMNVQTGRWETDPSRTKTCLRDKEDILQYCRKAYPELQITNVVEASQPVTIQNWCRRGRS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916     126 gSCAHPHHQVVPFRCLPGEFVSEALLVPEGCRFLHQERMDQCESSTRRHQEAQEACSSQGLILHGSGMLLPCGSDRFRGV 205
Cdd:smart00006  81 -QCKTHHHFVIPFRCLVGEFVSDALLVPEGCQFLHQERMDQCETHQRWHQEAKEACSEKGMILHSFGMLLPCGIDKFRGV 159


                   ....*.
gi 1905916     206 EYVCCP 211
Cdd:smart00006 160 EFVCCP 165
APP_E2 pfam12925
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ...
 285-467 7.18e-94

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: 287.70  E-value: 7.18e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916    285 TPTPRPTDGVDIYFGMPGEISEHEGFLRAKMDLEERRMRQINEVMREWAMADNQSKNLPKAD-------RQALNEHFQSI 357
Cdd:pfam12925   1 TTTPPPTDAVDPYFEHPDPRNEHESFKKAKKRLEEKHRERMTKVMKEWEEAEERYQNLPKADpkaaekfKKAMTARFQET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916    358 LQTLEEQVSGERQRLVETHATRVIALINDQRRAALEGFLAALQADPPQAERVLLALRRYLRAEQKEQRHTLRHYQHVAAV 437
Cdd:pfam12925  81 VEALEEEAAAERQQLVETHQQRVEAHLNDRRRDALECYLQALQENPPNPHRILKALKKLLRAEQKDRRHTLRHYRHLLAS 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1905916    438 DPEKAQQMRFQVHTHLQVIEERVNQSLGLL 467
Cdd:pfam12925 161 DPEKAEQMKPQVLTHLRVIDRRMNQSLTLL 190
JMTM_APLP1 cd21708
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 1 (APLP-1) and ...
 564-648 3.40e-42

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: 147.28  E-value: 3.40e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916  564 EIQRDELAPAGT-GVSREAVSGLLIMGAGGGSLIVLSMLLLRRKkPYGAISHGVVEVDPMLTLEEQQLRELQRHGYENPT 642
Cdd:cd21708   1 DIQRDELEPDTLvTFNRGALIGLLVVAVAVAMVIVISLLLVRRK-PYGTISHGIVEVDPMLTPEERQLSKMQNHGYENPT 79


                ....*.
gi 1905916  643 YRFLEE 648
Cdd:cd21708  80 YRFLEE 85
 
Name Accession Description Interval E-value
A4_EXTRA smart00006
amyloid A4; amyloid A4 precursor of Alzheimers disease
 46-211 3.58e-101

amyloid A4; amyloid A4 precursor of Alzheimers disease


Pssm-ID: 128326 [Multi-domain]  Cd Length: 165  Bit Score: 305.58  E-value: 3.58e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916      46 GAAEAPGSAQVAGLCGRLTLHRDLRTGRWEPDPQRSRRCLRDPQRVLEYCRQMYPELQIARVEQATQAIPMERWCGGSRS 125
Cdd:smart00006   1 GAAGALAEPQIAMLCGRLNMHMNVQTGRWETDPSRTKTCLRDKEDILQYCRKAYPELQITNVVEASQPVTIQNWCRRGRS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916     126 gSCAHPHHQVVPFRCLPGEFVSEALLVPEGCRFLHQERMDQCESSTRRHQEAQEACSSQGLILHGSGMLLPCGSDRFRGV 205
Cdd:smart00006  81 -QCKTHHHFVIPFRCLVGEFVSDALLVPEGCQFLHQERMDQCETHQRWHQEAKEACSEKGMILHSFGMLLPCGIDKFRGV 159


                   ....*.
gi 1905916     206 EYVCCP 211
Cdd:smart00006 160 EFVCCP 165
APP_E2 pfam12925
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ...
 285-467 7.18e-94

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: 287.70  E-value: 7.18e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916    285 TPTPRPTDGVDIYFGMPGEISEHEGFLRAKMDLEERRMRQINEVMREWAMADNQSKNLPKAD-------RQALNEHFQSI 357
Cdd:pfam12925   1 TTTPPPTDAVDPYFEHPDPRNEHESFKKAKKRLEEKHRERMTKVMKEWEEAEERYQNLPKADpkaaekfKKAMTARFQET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916    358 LQTLEEQVSGERQRLVETHATRVIALINDQRRAALEGFLAALQADPPQAERVLLALRRYLRAEQKEQRHTLRHYQHVAAV 437
Cdd:pfam12925  81 VEALEEEAAAERQQLVETHQQRVEAHLNDRRRDALECYLQALQENPPNPHRILKALKKLLRAEQKDRRHTLRHYRHLLAS 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1905916    438 DPEKAQQMRFQVHTHLQVIEERVNQSLGLL 467
Cdd:pfam12925 161 DPEKAEQMKPQVLTHLRVIDRRMNQSLTLL 190
APP_N pfam02177
Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor ...
 55-154 1.17e-49

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: 167.87  E-value: 1.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916     55 QVAGLCGRLTLHRDLRTGRWEPDPQRSRRCLRDPQRVLEYCRQMYPELQIARVEQATQAIPMERWCGGSRsGSCAHpHHQ 134
Cdd:pfam02177   3 QVAMFCGKLNQHMDLETGRWEPDPSGKATCFKDKEEILDYCQKVYPELDITNIVEASQPVTIDNWCKKGR-KKCKG-HHI 80

                          90       100
                  ....*....|....*....|
gi 1905916    135 VVPFRCLPGEFVSEALLVPE 154
Cdd:pfam02177  81 VKPYRCLVGEFVSDALLVPE 100
JMTM_APLP1 cd21708
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 1 (APLP-1) and ...
 564-648 3.40e-42

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: 147.28  E-value: 3.40e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916  564 EIQRDELAPAGT-GVSREAVSGLLIMGAGGGSLIVLSMLLLRRKkPYGAISHGVVEVDPMLTLEEQQLRELQRHGYENPT 642
Cdd:cd21708   1 DIQRDELEPDTLvTFNRGALIGLLVVAVAVAMVIVISLLLVRRK-PYGTISHGIVEVDPMLTPEERQLSKMQNHGYENPT 79


                ....*.
gi 1905916  643 YRFLEE 648
Cdd:cd21708  80 YRFLEE 85
APP_amyloid pfam10515
Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the ...
 596-647 7.99e-23

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: 91.63  E-value: 7.99e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1905916    596 IVLSMLLLRRKKPYGAISHGVVEVDPMLTLEEQQLRELQRHGYENPTYRFLE 647
Cdd:pfam10515   1 IVVGMALLRRRAARSPSAHGFVEVDPNVTPEERHVANMQVNGYENPTYKYFE 52
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
311-425 8.62e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 8.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916  311 LRAKMDLEERRMRQINEVMREWAMADNQSKNLpKADRQALNEHfqsiLQTLEEQVSGERQRLVETHATRVIALinDQRRA 390
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEEL-EAELAELQEE----LEELLEQLSLATEEELQDLAEELEEL--QQRLA 209

                        90       100       110
                ....*....|....*....|....*....|....*
gi 1905916  391 ALEGFLAALQADPPQAERVLLALRRYLRAEQKEQR 425
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEER 244
 
Name Accession Description Interval E-value
A4_EXTRA smart00006
amyloid A4; amyloid A4 precursor of Alzheimers disease
 46-211 3.58e-101

amyloid A4; amyloid A4 precursor of Alzheimers disease


Pssm-ID: 128326 [Multi-domain]  Cd Length: 165  Bit Score: 305.58  E-value: 3.58e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916      46 GAAEAPGSAQVAGLCGRLTLHRDLRTGRWEPDPQRSRRCLRDPQRVLEYCRQMYPELQIARVEQATQAIPMERWCGGSRS 125
Cdd:smart00006   1 GAAGALAEPQIAMLCGRLNMHMNVQTGRWETDPSRTKTCLRDKEDILQYCRKAYPELQITNVVEASQPVTIQNWCRRGRS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916     126 gSCAHPHHQVVPFRCLPGEFVSEALLVPEGCRFLHQERMDQCESSTRRHQEAQEACSSQGLILHGSGMLLPCGSDRFRGV 205
Cdd:smart00006  81 -QCKTHHHFVIPFRCLVGEFVSDALLVPEGCQFLHQERMDQCETHQRWHQEAKEACSEKGMILHSFGMLLPCGIDKFRGV 159


                   ....*.
gi 1905916     206 EYVCCP 211
Cdd:smart00006 160 EFVCCP 165
APP_E2 pfam12925
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ...
 285-467 7.18e-94

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: 287.70  E-value: 7.18e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916    285 TPTPRPTDGVDIYFGMPGEISEHEGFLRAKMDLEERRMRQINEVMREWAMADNQSKNLPKAD-------RQALNEHFQSI 357
Cdd:pfam12925   1 TTTPPPTDAVDPYFEHPDPRNEHESFKKAKKRLEEKHRERMTKVMKEWEEAEERYQNLPKADpkaaekfKKAMTARFQET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916    358 LQTLEEQVSGERQRLVETHATRVIALINDQRRAALEGFLAALQADPPQAERVLLALRRYLRAEQKEQRHTLRHYQHVAAV 437
Cdd:pfam12925  81 VEALEEEAAAERQQLVETHQQRVEAHLNDRRRDALECYLQALQENPPNPHRILKALKKLLRAEQKDRRHTLRHYRHLLAS 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1905916    438 DPEKAQQMRFQVHTHLQVIEERVNQSLGLL 467
Cdd:pfam12925 161 DPEKAEQMKPQVLTHLRVIDRRMNQSLTLL 190
APP_N pfam02177
Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor ...
 55-154 1.17e-49

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: 167.87  E-value: 1.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916     55 QVAGLCGRLTLHRDLRTGRWEPDPQRSRRCLRDPQRVLEYCRQMYPELQIARVEQATQAIPMERWCGGSRsGSCAHpHHQ 134
Cdd:pfam02177   3 QVAMFCGKLNQHMDLETGRWEPDPSGKATCFKDKEEILDYCQKVYPELDITNIVEASQPVTIDNWCKKGR-KKCKG-HHI 80

                          90       100
                  ....*....|....*....|
gi 1905916    135 VVPFRCLPGEFVSEALLVPE 154
Cdd:pfam02177  81 VKPYRCLVGEFVSDALLVPE 100
JMTM_APLP1 cd21708
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 1 (APLP-1) and ...
 564-648 3.40e-42

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: 147.28  E-value: 3.40e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916  564 EIQRDELAPAGT-GVSREAVSGLLIMGAGGGSLIVLSMLLLRRKkPYGAISHGVVEVDPMLTLEEQQLRELQRHGYENPT 642
Cdd:cd21708   1 DIQRDELEPDTLvTFNRGALIGLLVVAVAVAMVIVISLLLVRRK-PYGTISHGIVEVDPMLTPEERQLSKMQNHGYENPT 79


                ....*.
gi 1905916  643 YRFLEE 648
Cdd:cd21708  80 YRFLEE 85
APP_Cu_bd pfam12924
Copper-binding of amyloid precursor, CuBD; This short domain, part of the extra-cellular ...
 156-211 2.14e-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: 110.44  E-value: 2.14e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1905916    156 CRFLHQERMDQCESSTRRHQEAQEACSSQGLILHGSGMLLPCGSDRFRGVEYVCCP 211
Cdd:pfam12924   1 CKFDHKHNMDVCESHQHWHATAKEACAARGMVLHSFGMLLPCGIDLFTGVEFVCCP 56
APP_amyloid pfam10515
Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the ...
 596-647 7.99e-23

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: 91.63  E-value: 7.99e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1905916    596 IVLSMLLLRRKKPYGAISHGVVEVDPMLTLEEQQLRELQRHGYENPTYRFLE 647
Cdd:pfam10515   1 IVVGMALLRRRAARSPSAHGFVEVDPNVTPEERHVANMQVNGYENPTYKYFE 52
JMTM_APLP2 cd21709
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and ...
 578-648 1.48e-22

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: 91.91  E-value: 1.48e-22
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1905916  578 SREAVSGLLIMGAGGGSLIVLSMLLLRrKKPYGAISHGVVEVDPMLTLEEQQLRELQRHGYENPTYRFLEE 648
Cdd:cd21709  12 SSSALIGLLVIAVAIATVIVISLVLLR-KRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLEQ 81
JMTM_APP_like cd21699
juxtamembrane and transmembrane (JMTM) domain found in the amyloid-beta precursor protein (APP) ...
 566-606 4.32e-10

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: 54.98  E-value: 4.32e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 1905916  566 QRDELAPAGTGVSREAVSGLLIMGAGGGSLIVLSMLLLRRK 606
Cdd:cd21699   1 ERVFLAEDSSNSSFGAVIGLAVGGVAVAIVIVVAVVMLRRR 41
HrpE pfam06188
HrpE/YscL/FliH and V-type ATPase subunit E; This is a prokaryotic family that contains ...
 298-470 5.72e-03

HrpE/YscL/FliH and V-type ATPase subunit E; This is a prokaryotic family that contains proteins of the FliH and HrpE/YscL family. These proteins are involved in type III secretion, which is the process that drives flagellar biosynthesis and mediates bacterial-eukaryotic interactions. This family also V-type ATPase subunit E. This subunit appears to form a tight interaction with subunit G in the F0 complex. Subunits E and G may act together as stators to prevent certain subunits from rotating with the central rotary element. pfam01991 also contains V-type ATPase subunit E proteins.


Pssm-ID: 368784  Cd Length: 187  Bit Score: 38.31  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916    298 FGMPGEISEHEGFLRAKMDLEERRMRQINEVMREWA-----MADNQSKNLPKADRQALNEHFQSILQTLEEqvsgERQRL 372
Cdd:pfam06188   7 FTLTGAAVLEEPILRRELLAESLRARELLAEARQQAeqllaQAHEQAQHLLDQAEAQFWSQANALLQGIQQ----ERESL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916    373 VETHATRVIALINDQrraalegfLAALQADPPQAERVLLALRRYLRAEQKEQRHTLRHYQHVAAVDPEKAQQMRFQVHTH 452
Cdd:pfam06188  83 QRDALTAVGQLLNDA--------LSHLLDETPLPERISALLRNLLVGQPGEARATLYCHPEAAADVAAWLQTHGFHLLWQ 154

                         170
                  ....*....|....*...
gi 1905916    453 LQVIEERVNQSLGLLDQN 470
Cdd:pfam06188 155 LQSDPALAPDSLRLSTAL 172
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
311-425 8.62e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 8.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905916  311 LRAKMDLEERRMRQINEVMREWAMADNQSKNLpKADRQALNEHfqsiLQTLEEQVSGERQRLVETHATRVIALinDQRRA 390
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEEL-EAELAELQEE----LEELLEQLSLATEEELQDLAEELEEL--QQRLA 209

                        90       100       110
                ....*....|....*....|....*....|....*
gi 1905916  391 ALEGFLAALQADPPQAERVLLALRRYLRAEQKEQR 425
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEER 244
 
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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