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Conserved domains on  [gi|530386648|ref|XP_005250761|]
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calcium-dependent secretion activator 2 isoform X9 [Homo sapiens]

Protein Classification

calcium-dependent secretion activator 2( domain architecture ID 10644074)

calcium-dependent secretion activator 2 (CADPS2) is a calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MUN pfam06292
MUN domain; This entry corresponds to the MUN domain found in Munc13 proteins. These ...
801-1214 3.99e-171

MUN domain; This entry corresponds to the MUN domain found in Munc13 proteins. These constitute a family of three highly homologous molecules (Munc13-1, Munc13-2 and Munc13-3) with homology to Caenorhabditis elegans unc-13p. Munc13 proteins contain a phorbol ester-binding C1 domain and two C2 domains, which are Ca2+/phospholipid binding domains. Sequence analyses have uncovered two regions called Munc13 homology domains 1 (MHD1) and 2 (MHD2) that are arranged between two flanking C2 domains. MHD1 and MHD2 domains are present in a wide variety of proteins from Arabidopsis thaliana, C. elegans, Drosophila melanogaster, mouse, rat and human, some of which may function in a Munc13-like manner to regulate membrane trafficking. Structural studies have defined MHD1 and MHD2 to be part of the larger MUN domain which forms an elongated structure composed of any pairs of alpha helices.


:

Pssm-ID: 461870  Cd Length: 473  Bit Score: 515.80  E-value: 3.99e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648   801 KVVRKCLEKAALINYTRLTEYA-------KIEGPAEKETETMNQASPARKLEEILHLAELCIEVLQQNEEHHA---EAFA 870
Cdd:pfam06292    1 QVVKDCLKAAALSNYQRLFENAyelsrefKIEDKESIPEESQGLGPSEKRLDFWIKLIELCVSVLQQDKEHYApvlNQFP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648   871 WWPDLLAEHAEKFWALFTVDMDTALEAQ------PQDSWDS--FPLFQLLNNFLRNDTLLCNGKFHKHLQEIFVPLVVRY 942
Cdd:pfam06292   81 WELDLGAEHAEIFWSLFAVDMDAALEEHeqhrlcKPDSWMNlhFKVKWLLNDYLRDDPTLKNGKFHPHYPDWFEPFVMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648   943 VDLMESSIAQSIHRGFEQETWQPV------NNGSATSEDLFWKLDALQMFVFDLHWPEQEFAHHLEQRLKLMASDMLEAC 1016
Cdd:pfam06292  161 LDLNESSIAQSLHGGFERDKKDGFqqssehALFSSSVVDLFWKLNQLQDFIKKLEWPDPEFAAHLEKRFKLMASDMLLAY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  1017 VKRTRTAFELKLQKaskttdlriPASVCTMFNVLVDAKKQSTK--LCAldGGQEFGSQWQQYHSKIDDLIDNSVKEIISL 1094
Cdd:pfam06292  241 AKRTRKAFDSKLKK---------PRTACTMMNNIQQARVQLEKmfLCM--GGDELDGEAHQYLTELQVLLEGVLDEMSSI 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  1095 LVSKFVSVLEGVLSKLSR--------------YDEGTFFSSILSFtvkaaakyvdvpkpgmdLADTYIMFVRQNQDILRE 1160
Cdd:pfam06292  310 FADSFEPVLESVLSKLSRllqqikgsnrnnaaYDEGTLLSPLMDF-----------------LDGNLSLFARICEKTVLK 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  1161 KVNEEMY-----------------------------------------------IEKLFDQWYSSSMKVICVWLTDRLDL 1193
Cdd:pfam06292  373 RVLKELWkivmntlektvvlpplsdqsgsqlkllmslegaknltpkqcaildaaLETIFQYFHAGGNGLKKTWLEKSPEL 452
                          490       500
                   ....*....|....*....|.
gi 530386648  1194 QLHIYQLKTLIKIVKKTYRDF 1214
Cdd:pfam06292  453 QLLRYALSLYTQTTDKLIKDF 473
PH_CADPS cd01234
Ca2+-dependent activator protein (also called CAPS) Pleckstrin homology (PH) domain; CADPS ...
481-600 9.28e-82

Ca2+-dependent activator protein (also called CAPS) Pleckstrin homology (PH) domain; CADPS/CAPS consists of two members, CAPS1 which regulates catecholamine release from neuroendocrine cells and CAPS2 which is involved in the release of two neurotrophins, brain-derived neurotrophic factor (BDNF) and neurotrophin-3 (NT-3) from cerebellar granule cells. CADPS plays an important role in vesicle exocytosis in neurons and endocrine cells where it functions to prime the exocytic machinery for Ca2+-triggered fusion. Priming involves the assembly of trans SNARE complexes. The initial interaction of vesicles with target membranes is mediated by diverse stage-specific tethering factors or multi-subunit tethering complexes. CADPS and Munc13 proteins are proposed to be the functional homologs of the stage-specific tethering factors that prime membrane fusion. Interestingly, regions in the C-terminal half of CADPS are similar to the C-terminal region of Munc13-1 that was reported to bind syntaxin-1. CADPS has independent interactions with each of the SNARE proteins (Q-SNARE and R-SNARE) required for vesicle fusion. CADPS interacts with Q-SNARE proteins syntaxin-1 (H3 SNARE) and SNAP-25 (SN1) and might promote Q-SNARE heterodimer formation. Through its N-terminal R-SNARE VAMP-2 interactions, CADPS bound to heterodimeric Q-SNARE complexes could be involved in catalyzing the zippering of VAMP-2 into recipient complexes. It also contains a central PH domain that binds to phosphoinositide 4,5 bisphosphate containing liposomes. Membrane association may also be mediated by binding to phosphatidlyserine via general electrostatic interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269940  Cd Length: 122  Bit Score: 262.69  E-value: 9.28e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  481 RMDKPAHMKHSGYLYALGQKVWKRWKKRYFVLVQVSQYTFAMCSYREKKSEPQELMQLEGYTVDYTDPHP--GLQGGCMF 558
Cdd:cd01234     1 RMDKPQNMKHCGYLYALGKSVWKKWKKRYFVLVQVSQYTFAMCSYREKKSEPQEMMQLDGYTVDYTDPQPdlGLEGGRFF 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 530386648  559 FNAVKEGDTVIFASDDEQDRILWVQAMYRATGQSYKPVPAIQ 600
Cdd:cd01234    81 FNAVKEGDSVIFASDDENDRQLWVQALYRATGQSHKPVPPTQ 122
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
366-448 2.93e-03

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


:

Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 38.62  E-value: 2.93e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648    366 TLEIVIMEVQGLKSVAPNRIV--YCTMEVEG---EKLQTDQAEASR-PQWGTQGDFTTTHP-RPVVKVKLFTESTGvlaL 438
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGKSdpYVKVSLDGdpkEKKKTKVVKNTLnPVWNETFEFEVPPPeLAELEIEVYDKDRF---G 77
                            90
                    ....*....|
gi 530386648    439 EDKELGRVIL 448
Cdd:smart00239   78 RDDFIGQVTI 87
 
Name Accession Description Interval E-value
MUN pfam06292
MUN domain; This entry corresponds to the MUN domain found in Munc13 proteins. These ...
801-1214 3.99e-171

MUN domain; This entry corresponds to the MUN domain found in Munc13 proteins. These constitute a family of three highly homologous molecules (Munc13-1, Munc13-2 and Munc13-3) with homology to Caenorhabditis elegans unc-13p. Munc13 proteins contain a phorbol ester-binding C1 domain and two C2 domains, which are Ca2+/phospholipid binding domains. Sequence analyses have uncovered two regions called Munc13 homology domains 1 (MHD1) and 2 (MHD2) that are arranged between two flanking C2 domains. MHD1 and MHD2 domains are present in a wide variety of proteins from Arabidopsis thaliana, C. elegans, Drosophila melanogaster, mouse, rat and human, some of which may function in a Munc13-like manner to regulate membrane trafficking. Structural studies have defined MHD1 and MHD2 to be part of the larger MUN domain which forms an elongated structure composed of any pairs of alpha helices.


Pssm-ID: 461870  Cd Length: 473  Bit Score: 515.80  E-value: 3.99e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648   801 KVVRKCLEKAALINYTRLTEYA-------KIEGPAEKETETMNQASPARKLEEILHLAELCIEVLQQNEEHHA---EAFA 870
Cdd:pfam06292    1 QVVKDCLKAAALSNYQRLFENAyelsrefKIEDKESIPEESQGLGPSEKRLDFWIKLIELCVSVLQQDKEHYApvlNQFP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648   871 WWPDLLAEHAEKFWALFTVDMDTALEAQ------PQDSWDS--FPLFQLLNNFLRNDTLLCNGKFHKHLQEIFVPLVVRY 942
Cdd:pfam06292   81 WELDLGAEHAEIFWSLFAVDMDAALEEHeqhrlcKPDSWMNlhFKVKWLLNDYLRDDPTLKNGKFHPHYPDWFEPFVMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648   943 VDLMESSIAQSIHRGFEQETWQPV------NNGSATSEDLFWKLDALQMFVFDLHWPEQEFAHHLEQRLKLMASDMLEAC 1016
Cdd:pfam06292  161 LDLNESSIAQSLHGGFERDKKDGFqqssehALFSSSVVDLFWKLNQLQDFIKKLEWPDPEFAAHLEKRFKLMASDMLLAY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  1017 VKRTRTAFELKLQKaskttdlriPASVCTMFNVLVDAKKQSTK--LCAldGGQEFGSQWQQYHSKIDDLIDNSVKEIISL 1094
Cdd:pfam06292  241 AKRTRKAFDSKLKK---------PRTACTMMNNIQQARVQLEKmfLCM--GGDELDGEAHQYLTELQVLLEGVLDEMSSI 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  1095 LVSKFVSVLEGVLSKLSR--------------YDEGTFFSSILSFtvkaaakyvdvpkpgmdLADTYIMFVRQNQDILRE 1160
Cdd:pfam06292  310 FADSFEPVLESVLSKLSRllqqikgsnrnnaaYDEGTLLSPLMDF-----------------LDGNLSLFARICEKTVLK 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  1161 KVNEEMY-----------------------------------------------IEKLFDQWYSSSMKVICVWLTDRLDL 1193
Cdd:pfam06292  373 RVLKELWkivmntlektvvlpplsdqsgsqlkllmslegaknltpkqcaildaaLETIFQYFHAGGNGLKKTWLEKSPEL 452
                          490       500
                   ....*....|....*....|.
gi 530386648  1194 QLHIYQLKTLIKIVKKTYRDF 1214
Cdd:pfam06292  453 QLLRYALSLYTQTTDKLIKDF 473
PH_CADPS cd01234
Ca2+-dependent activator protein (also called CAPS) Pleckstrin homology (PH) domain; CADPS ...
481-600 9.28e-82

Ca2+-dependent activator protein (also called CAPS) Pleckstrin homology (PH) domain; CADPS/CAPS consists of two members, CAPS1 which regulates catecholamine release from neuroendocrine cells and CAPS2 which is involved in the release of two neurotrophins, brain-derived neurotrophic factor (BDNF) and neurotrophin-3 (NT-3) from cerebellar granule cells. CADPS plays an important role in vesicle exocytosis in neurons and endocrine cells where it functions to prime the exocytic machinery for Ca2+-triggered fusion. Priming involves the assembly of trans SNARE complexes. The initial interaction of vesicles with target membranes is mediated by diverse stage-specific tethering factors or multi-subunit tethering complexes. CADPS and Munc13 proteins are proposed to be the functional homologs of the stage-specific tethering factors that prime membrane fusion. Interestingly, regions in the C-terminal half of CADPS are similar to the C-terminal region of Munc13-1 that was reported to bind syntaxin-1. CADPS has independent interactions with each of the SNARE proteins (Q-SNARE and R-SNARE) required for vesicle fusion. CADPS interacts with Q-SNARE proteins syntaxin-1 (H3 SNARE) and SNAP-25 (SN1) and might promote Q-SNARE heterodimer formation. Through its N-terminal R-SNARE VAMP-2 interactions, CADPS bound to heterodimeric Q-SNARE complexes could be involved in catalyzing the zippering of VAMP-2 into recipient complexes. It also contains a central PH domain that binds to phosphoinositide 4,5 bisphosphate containing liposomes. Membrane association may also be mediated by binding to phosphatidlyserine via general electrostatic interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269940  Cd Length: 122  Bit Score: 262.69  E-value: 9.28e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  481 RMDKPAHMKHSGYLYALGQKVWKRWKKRYFVLVQVSQYTFAMCSYREKKSEPQELMQLEGYTVDYTDPHP--GLQGGCMF 558
Cdd:cd01234     1 RMDKPQNMKHCGYLYALGKSVWKKWKKRYFVLVQVSQYTFAMCSYREKKSEPQEMMQLDGYTVDYTDPQPdlGLEGGRFF 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 530386648  559 FNAVKEGDTVIFASDDEQDRILWVQAMYRATGQSYKPVPAIQ 600
Cdd:cd01234    81 FNAVKEGDSVIFASDDENDRQLWVQALYRATGQSHKPVPPTQ 122
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
488-589 2.14e-12

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 64.49  E-value: 2.14e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648    488 MKHSGYLYALGQKVWKRWKKRYFVLvqvsqYTFAMCSYREKK----SEPQELMQLEGYTVDYTDPHPGLQGGCMFFNAVK 563
Cdd:smart00233    1 VIKEGWLYKKSGGGKKSWKKRYFVL-----FNSTLLYYKSKKdkksYKPKGSIDLSGCTVREAPDPDSSKKPHCFEIKTS 75
                            90       100
                    ....*....|....*....|....*.
gi 530386648    564 EGDTVIFASDDEQDRILWVQAMYRAT 589
Cdd:smart00233   76 DRKTLLLQAESEEEREKWVEALRKAI 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
489-588 1.47e-10

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 59.50  E-value: 1.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648   489 KHSGYLYALGQKVWKRWKKRYFVLVQVSQYTFAmCSYREKKSEPQELMQLEGYTVDYTDPHPGLQGGCMF---FNAVKEG 565
Cdd:pfam00169    2 VKEGWLLKKGGGKKKSWKKRYFVLFDGSLLYYK-DDKSGKSKEPKGSISLSGCEVVEVVASDSPKRKFCFelrTGERTGK 80
                           90       100
                   ....*....|....*....|...
gi 530386648   566 DTVIFASDDEQDRILWVQAMYRA 588
Cdd:pfam00169   81 RTYLLQAESEEERKDWIKAIQSA 103
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
366-448 2.93e-03

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 38.62  E-value: 2.93e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648    366 TLEIVIMEVQGLKSVAPNRIV--YCTMEVEG---EKLQTDQAEASR-PQWGTQGDFTTTHP-RPVVKVKLFTESTGvlaL 438
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGKSdpYVKVSLDGdpkEKKKTKVVKNTLnPVWNETFEFEVPPPeLAELEIEVYDKDRF---G 77
                            90
                    ....*....|
gi 530386648    439 EDKELGRVIL 448
Cdd:smart00239   78 RDDFIGQVTI 87
 
Name Accession Description Interval E-value
MUN pfam06292
MUN domain; This entry corresponds to the MUN domain found in Munc13 proteins. These ...
801-1214 3.99e-171

MUN domain; This entry corresponds to the MUN domain found in Munc13 proteins. These constitute a family of three highly homologous molecules (Munc13-1, Munc13-2 and Munc13-3) with homology to Caenorhabditis elegans unc-13p. Munc13 proteins contain a phorbol ester-binding C1 domain and two C2 domains, which are Ca2+/phospholipid binding domains. Sequence analyses have uncovered two regions called Munc13 homology domains 1 (MHD1) and 2 (MHD2) that are arranged between two flanking C2 domains. MHD1 and MHD2 domains are present in a wide variety of proteins from Arabidopsis thaliana, C. elegans, Drosophila melanogaster, mouse, rat and human, some of which may function in a Munc13-like manner to regulate membrane trafficking. Structural studies have defined MHD1 and MHD2 to be part of the larger MUN domain which forms an elongated structure composed of any pairs of alpha helices.


Pssm-ID: 461870  Cd Length: 473  Bit Score: 515.80  E-value: 3.99e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648   801 KVVRKCLEKAALINYTRLTEYA-------KIEGPAEKETETMNQASPARKLEEILHLAELCIEVLQQNEEHHA---EAFA 870
Cdd:pfam06292    1 QVVKDCLKAAALSNYQRLFENAyelsrefKIEDKESIPEESQGLGPSEKRLDFWIKLIELCVSVLQQDKEHYApvlNQFP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648   871 WWPDLLAEHAEKFWALFTVDMDTALEAQ------PQDSWDS--FPLFQLLNNFLRNDTLLCNGKFHKHLQEIFVPLVVRY 942
Cdd:pfam06292   81 WELDLGAEHAEIFWSLFAVDMDAALEEHeqhrlcKPDSWMNlhFKVKWLLNDYLRDDPTLKNGKFHPHYPDWFEPFVMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648   943 VDLMESSIAQSIHRGFEQETWQPV------NNGSATSEDLFWKLDALQMFVFDLHWPEQEFAHHLEQRLKLMASDMLEAC 1016
Cdd:pfam06292  161 LDLNESSIAQSLHGGFERDKKDGFqqssehALFSSSVVDLFWKLNQLQDFIKKLEWPDPEFAAHLEKRFKLMASDMLLAY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  1017 VKRTRTAFELKLQKaskttdlriPASVCTMFNVLVDAKKQSTK--LCAldGGQEFGSQWQQYHSKIDDLIDNSVKEIISL 1094
Cdd:pfam06292  241 AKRTRKAFDSKLKK---------PRTACTMMNNIQQARVQLEKmfLCM--GGDELDGEAHQYLTELQVLLEGVLDEMSSI 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  1095 LVSKFVSVLEGVLSKLSR--------------YDEGTFFSSILSFtvkaaakyvdvpkpgmdLADTYIMFVRQNQDILRE 1160
Cdd:pfam06292  310 FADSFEPVLESVLSKLSRllqqikgsnrnnaaYDEGTLLSPLMDF-----------------LDGNLSLFARICEKTVLK 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  1161 KVNEEMY-----------------------------------------------IEKLFDQWYSSSMKVICVWLTDRLDL 1193
Cdd:pfam06292  373 RVLKELWkivmntlektvvlpplsdqsgsqlkllmslegaknltpkqcaildaaLETIFQYFHAGGNGLKKTWLEKSPEL 452
                          490       500
                   ....*....|....*....|.
gi 530386648  1194 QLHIYQLKTLIKIVKKTYRDF 1214
Cdd:pfam06292  453 QLLRYALSLYTQTTDKLIKDF 473
PH_CADPS cd01234
Ca2+-dependent activator protein (also called CAPS) Pleckstrin homology (PH) domain; CADPS ...
481-600 9.28e-82

Ca2+-dependent activator protein (also called CAPS) Pleckstrin homology (PH) domain; CADPS/CAPS consists of two members, CAPS1 which regulates catecholamine release from neuroendocrine cells and CAPS2 which is involved in the release of two neurotrophins, brain-derived neurotrophic factor (BDNF) and neurotrophin-3 (NT-3) from cerebellar granule cells. CADPS plays an important role in vesicle exocytosis in neurons and endocrine cells where it functions to prime the exocytic machinery for Ca2+-triggered fusion. Priming involves the assembly of trans SNARE complexes. The initial interaction of vesicles with target membranes is mediated by diverse stage-specific tethering factors or multi-subunit tethering complexes. CADPS and Munc13 proteins are proposed to be the functional homologs of the stage-specific tethering factors that prime membrane fusion. Interestingly, regions in the C-terminal half of CADPS are similar to the C-terminal region of Munc13-1 that was reported to bind syntaxin-1. CADPS has independent interactions with each of the SNARE proteins (Q-SNARE and R-SNARE) required for vesicle fusion. CADPS interacts with Q-SNARE proteins syntaxin-1 (H3 SNARE) and SNAP-25 (SN1) and might promote Q-SNARE heterodimer formation. Through its N-terminal R-SNARE VAMP-2 interactions, CADPS bound to heterodimeric Q-SNARE complexes could be involved in catalyzing the zippering of VAMP-2 into recipient complexes. It also contains a central PH domain that binds to phosphoinositide 4,5 bisphosphate containing liposomes. Membrane association may also be mediated by binding to phosphatidlyserine via general electrostatic interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269940  Cd Length: 122  Bit Score: 262.69  E-value: 9.28e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  481 RMDKPAHMKHSGYLYALGQKVWKRWKKRYFVLVQVSQYTFAMCSYREKKSEPQELMQLEGYTVDYTDPHP--GLQGGCMF 558
Cdd:cd01234     1 RMDKPQNMKHCGYLYALGKSVWKKWKKRYFVLVQVSQYTFAMCSYREKKSEPQEMMQLDGYTVDYTDPQPdlGLEGGRFF 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 530386648  559 FNAVKEGDTVIFASDDEQDRILWVQAMYRATGQSYKPVPAIQ 600
Cdd:cd01234    81 FNAVKEGDSVIFASDDENDRQLWVQALYRATGQSHKPVPPTQ 122
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
488-589 2.14e-12

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 64.49  E-value: 2.14e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648    488 MKHSGYLYALGQKVWKRWKKRYFVLvqvsqYTFAMCSYREKK----SEPQELMQLEGYTVDYTDPHPGLQGGCMFFNAVK 563
Cdd:smart00233    1 VIKEGWLYKKSGGGKKSWKKRYFVL-----FNSTLLYYKSKKdkksYKPKGSIDLSGCTVREAPDPDSSKKPHCFEIKTS 75
                            90       100
                    ....*....|....*....|....*.
gi 530386648    564 EGDTVIFASDDEQDRILWVQAMYRAT 589
Cdd:smart00233   76 DRKTLLLQAESEEEREKWVEALRKAI 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
489-588 1.47e-10

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 59.50  E-value: 1.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648   489 KHSGYLYALGQKVWKRWKKRYFVLVQVSQYTFAmCSYREKKSEPQELMQLEGYTVDYTDPHPGLQGGCMF---FNAVKEG 565
Cdd:pfam00169    2 VKEGWLLKKGGGKKKSWKKRYFVLFDGSLLYYK-DDKSGKSKEPKGSISLSGCEVVEVVASDSPKRKFCFelrTGERTGK 80
                           90       100
                   ....*....|....*....|...
gi 530386648   566 DTVIFASDDEQDRILWVQAMYRA 588
Cdd:pfam00169   81 RTYLLQAESEEERKDWIKAIQSA 103
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
491-588 2.01e-06

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270068  Cd Length: 104  Bit Score: 47.65  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  491 SGYLYALGQKVWKRWKKRYFVLVQvsqytfaMCSYREKKSEPQELM---QLEGYTVdyTDPHPGLQGGCMF-FNAVKEG- 565
Cdd:cd13248    10 SGWLHKQGGSGLKNWRKRWFVLKD-------NCLYYYKDPEEEKALgsiLLPSYTI--SPAPPSDEISRKFaFKAEHANm 80
                          90       100
                  ....*....|....*....|...
gi 530386648  566 DTVIFASDDEQDRILWVQAMYRA 588
Cdd:cd13248    81 RTYYFAADTAEEMEQWMNAMSLA 103
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
490-585 2.14e-06

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 47.15  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  490 HSGYLYALGQKVWKRWKKRYFVLvqvSQYTFAMCSYR-EKKSEPQELMQLEGyTVDYTDPHPGLQGGCMFFNaVKEGDTV 568
Cdd:cd00821     1 KEGYLLKRGGGGLKSWKKRWFVL---FEGVLLYYKSKkDSSYKPKGSIPLSG-ILEVEEVSPKERPHCFELV-TPDGRTY 75
                          90
                  ....*....|....*..
gi 530386648  569 IFASDDEQDRILWVQAM 585
Cdd:cd00821    76 YLQADSEEERQEWLKAL 92
PH2_FGD5_FGD6 cd13237
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6 pleckstrin ...
491-585 5.61e-05

FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6 pleckstrin homology (PH) domain, C-terminus; FGD5 regulates promotes angiogenesis of vascular endothelial growth factor (VEGF) in vascular endothelial cells, including network formation, permeability, directional movement, and proliferation. The specific function of FGD6 is unknown. In general, FGDs have a RhoGEF (DH) domain, followed by a PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activate the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the PH domain is involved in intracellular targeting of the DH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270057  Cd Length: 91  Bit Score: 43.17  E-value: 5.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  491 SGYLYaLGQKVWKRWKKRYFVLVQVSQYTFamcsyreKKSE---PQELMQLEGYTVDYTDPHPGLQGGCMFFNAVKEGDT 567
Cdd:cd13237     2 SGYLQ-RRKKSKKSWKRLWFVLKDKVLYTY-------KASEdvvALESVPLLGFTVVTIDESFEEDESLVFQLLHKGQLP 73
                          90
                  ....*....|....*...
gi 530386648  568 VIFASDDEQDRILWVQAM 585
Cdd:cd13237    74 IIFRADDAETAQRWIEAL 91
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
490-590 1.30e-04

Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; RhoGAP25 (also called ArhGap25) like other RhoGaps are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. This hierarchy contains RhoGAP22, RhoGAP24, and RhoGAP25. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270083  Cd Length: 114  Bit Score: 42.76  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  490 HSGYLYALGQKVwKRWKKRYFVLVQVSQYTFAmcsyREKKSEPQELMQLEGYTVDYTDPHPGLQGGCMF--------FNA 561
Cdd:cd13263     5 KSGWLKKQGSIV-KNWQQRWFVLRGDQLYYYK----DEDDTKPQGTIPLPGNKVKEVPFNPEEPGKFLFeiipggggDRM 79
                          90       100
                  ....*....|....*....|....*....
gi 530386648  562 VKEGDTVIFASDDEQDRILWVQAMYRATG 590
Cdd:cd13263    80 TSNHDSYLLMANSQAEMEEWVKVIRRVIG 108
PH1_PLEKHH1_PLEKHH2 cd13282
Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 ...
491-541 1.82e-03

Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 (PLEKHH1) PH domain, repeat 1; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241436  Cd Length: 96  Bit Score: 38.82  E-value: 1.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530386648  491 SGYLYALGQKVwKRWKKRYFVLVQvsQYTFAMCSYREKKSEPQELMQLEGY 541
Cdd:cd13282     2 AGYLTKLGGKV-KTWKRRWFVLKN--GELFYYKSPNDVIRKPQGQIALDGS 49
PH_3BP2 cd13308
SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes ...
490-591 2.59e-03

SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes the adaptor protein 3BP2), HD, ITU, IT10C3, and ADD1 are located near the Huntington's Disease Gene on Human Chromosome 4pl6.3. SH3BP2 lies in a region that is often missing in individuals with Wolf-Hirschhorn syndrome (WHS). Gain of function mutations in SH3BP2 causes enhanced B-cell antigen receptor (BCR)-mediated activation of nuclear factor of activated T cells (NFAT), resulting in a rare, genetic disorder called cherubism. This results in an increase in the signaling complex formation with Syk, phospholipase C-gamma2 (PLC-gamma2), and Vav1. It was recently discovered that Tankyrase regulates 3BP2 stability through ADP-ribosylation and ubiquitylation by the E3-ubiquitin ligase. Cherubism mutations uncouple 3BP2 from Tankyrase-mediated protein destruction, which results in its stabilization and subsequent hyperactivation of the Src, Syk, and Vav signaling pathways. SH3BP2 is also a potential negative regulator of the abl oncogene. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270118  Cd Length: 113  Bit Score: 38.93  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648  490 HSGYLYALG--QKVWKRWKKRYFVLVQVSQYTFAmcSYREKKsePQELMQLEGYTVDyTDPHPG--LQGGCMFFNAVKEG 565
Cdd:cd13308    11 HSGTLTKKGgsQKTLQNWQLRYVIIHQGCVYYYK--NDQSAK--PKGVFSLNGYNRR-AAEERTskLKFVFKIIHLSPDH 85
                          90       100
                  ....*....|....*....|....*.
gi 530386648  566 DTVIFASDDEQDRILWVQAMYRATGQ 591
Cdd:cd13308    86 RTWYFAAKSEDEMSEWMEYIRREIDH 111
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
366-448 2.93e-03

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 38.62  E-value: 2.93e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386648    366 TLEIVIMEVQGLKSVAPNRIV--YCTMEVEG---EKLQTDQAEASR-PQWGTQGDFTTTHP-RPVVKVKLFTESTGvlaL 438
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGKSdpYVKVSLDGdpkEKKKTKVVKNTLnPVWNETFEFEVPPPeLAELEIEVYDKDRF---G 77
                            90
                    ....*....|
gi 530386648    439 EDKELGRVIL 448
Cdd:smart00239   78 RDDFIGQVTI 87
 
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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