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Conserved domains on  [gi|1622908110|ref|XP_028700164|]
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calcium-dependent secretion activator 1 isoform X33 [Macaca mulatta]

Protein Classification

PH_CADPS and DUF1041 domain-containing protein( domain architecture ID 10100714)

PH_CADPS and DUF1041 domain-containing protein

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 ...
836-1241 8.07e-168

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: 507.71  E-value: 8.07e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  836 TVIRKCLEQAALVNYSRLSEYA-------------KIEENVGRLITPAKKLEDTIRLAELVIEVLQQNEEHHAEGKEAFA 902
Cdd:pfam06292    1 QVVKDCLKAAALSNYQRLFENAyelsrefkiedkeSIPEESQGLGPSEKRLDFWIKLIELCVSVLQQDKEHYAPVLNQFP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  903 WWSDLMVEHAETFLSLFAVDMDAALEVQ------PPDTWDS--FPLFQLLNDFLRTDYNLRNGKFHKHLQDLFAPLVVRY 974
Cdd:pfam06292   81 WELDLGAEHAEIFWSLFAVDMDAALEEHeqhrlcKPDSWMNlhFKVKWLLNDYLRDDPTLKNGKFHPHYPDWFEPFVMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  975 VDLMESSIAQSIHRGFERESWEPV------NNGSGTSEDLFWKLDALQTFIRDLHWPEEEFGKHLEQRLKLMASDMIESC 1048
Cdd:pfam06292  161 LDLNESSIAQSLHGGFERDKKDGFqqssehALFSSSVVDLFWKLNQLQDFIKKLEWPDPEFAAHLEKRFKLMASDMLLAY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110 1049 VKRTRIAFEVKLQKtsrstdfrvPQSICTMFNVMVDAKAQSTK--LC---SMEMGQEHQYHSKIDELIEETVKEMITLLV 1123
Cdd:pfam06292  241 AKRTRKAFDSKLKK---------PRTACTMMNNIQQARVQLEKmfLCmggDELDGEAHQYLTELQVLLEGVLDEMSSIFA 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110 1124 AKFVTILEGVLAKLSR--------------YDEGTLFSSFLSFtvkaaskyvdvpkpgmdVADAYVTFVRHSQDVLRDKV 1189
Cdd:pfam06292  312 DSFEPVLESVLSKLSRllqqikgsnrnnaaYDEGTLLSPLMDF-----------------LDGNLSLFARICEKTVLKRV 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110 1190 NEEMY-----------------------------------------------IERLFDQWYNSSMNVICTWLTDRMDLQL 1222
Cdd:pfam06292  375 LKELWkivmntlektvvlpplsdqsgsqlkllmslegaknltpkqcaildaaLETIFQYFHAGGNGLKKTWLEKSPELQL 454
                          490
                   ....*....|....*....
gi 1622908110 1223 HIYQLKTLIRMVKKTYRDF 1241
Cdd:pfam06292  455 LRYALSLYTQTTDKLIKDF 473
PH_CADPS cd01234
Ca2+-dependent activator protein (also called CAPS) Pleckstrin homology (PH) domain; CADPS ...
515-634 1.77e-86

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: 276.17  E-value: 1.77e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  515 RMDKPQNMKHSGYLWAIGKNVWKRWKKRFFVLVQVSQYTFAMCSYREKKAEPQELLQLDGYTVDYTDPQP--GLEGGRAF 592
Cdd:cd01234      1 RMDKPQNMKHCGYLYALGKSVWKKWKKRYFVLVQVSQYTFAMCSYREKKSEPQEMMQLDGYTVDYTDPQPdlGLEGGRFF 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622908110  593 FNAVKEGDTVIFASDDEQDRILWVQAMYRATGQSHKPVPPTQ 634
Cdd:cd01234     81 FNAVKEGDSVIFASDDENDRQLWVQALYRATGQSHKPVPPTQ 122
 
Name Accession Description Interval E-value
MUN pfam06292
MUN domain; This entry corresponds to the MUN domain found in Munc13 proteins. These ...
836-1241 8.07e-168

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: 507.71  E-value: 8.07e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  836 TVIRKCLEQAALVNYSRLSEYA-------------KIEENVGRLITPAKKLEDTIRLAELVIEVLQQNEEHHAEGKEAFA 902
Cdd:pfam06292    1 QVVKDCLKAAALSNYQRLFENAyelsrefkiedkeSIPEESQGLGPSEKRLDFWIKLIELCVSVLQQDKEHYAPVLNQFP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  903 WWSDLMVEHAETFLSLFAVDMDAALEVQ------PPDTWDS--FPLFQLLNDFLRTDYNLRNGKFHKHLQDLFAPLVVRY 974
Cdd:pfam06292   81 WELDLGAEHAEIFWSLFAVDMDAALEEHeqhrlcKPDSWMNlhFKVKWLLNDYLRDDPTLKNGKFHPHYPDWFEPFVMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  975 VDLMESSIAQSIHRGFERESWEPV------NNGSGTSEDLFWKLDALQTFIRDLHWPEEEFGKHLEQRLKLMASDMIESC 1048
Cdd:pfam06292  161 LDLNESSIAQSLHGGFERDKKDGFqqssehALFSSSVVDLFWKLNQLQDFIKKLEWPDPEFAAHLEKRFKLMASDMLLAY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110 1049 VKRTRIAFEVKLQKtsrstdfrvPQSICTMFNVMVDAKAQSTK--LC---SMEMGQEHQYHSKIDELIEETVKEMITLLV 1123
Cdd:pfam06292  241 AKRTRKAFDSKLKK---------PRTACTMMNNIQQARVQLEKmfLCmggDELDGEAHQYLTELQVLLEGVLDEMSSIFA 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110 1124 AKFVTILEGVLAKLSR--------------YDEGTLFSSFLSFtvkaaskyvdvpkpgmdVADAYVTFVRHSQDVLRDKV 1189
Cdd:pfam06292  312 DSFEPVLESVLSKLSRllqqikgsnrnnaaYDEGTLLSPLMDF-----------------LDGNLSLFARICEKTVLKRV 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110 1190 NEEMY-----------------------------------------------IERLFDQWYNSSMNVICTWLTDRMDLQL 1222
Cdd:pfam06292  375 LKELWkivmntlektvvlpplsdqsgsqlkllmslegaknltpkqcaildaaLETIFQYFHAGGNGLKKTWLEKSPELQL 454
                          490
                   ....*....|....*....
gi 1622908110 1223 HIYQLKTLIRMVKKTYRDF 1241
Cdd:pfam06292  455 LRYALSLYTQTTDKLIKDF 473
PH_CADPS cd01234
Ca2+-dependent activator protein (also called CAPS) Pleckstrin homology (PH) domain; CADPS ...
515-634 1.77e-86

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: 276.17  E-value: 1.77e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  515 RMDKPQNMKHSGYLWAIGKNVWKRWKKRFFVLVQVSQYTFAMCSYREKKAEPQELLQLDGYTVDYTDPQP--GLEGGRAF 592
Cdd:cd01234      1 RMDKPQNMKHCGYLYALGKSVWKKWKKRYFVLVQVSQYTFAMCSYREKKSEPQEMMQLDGYTVDYTDPQPdlGLEGGRFF 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622908110  593 FNAVKEGDTVIFASDDEQDRILWVQAMYRATGQSHKPVPPTQ 634
Cdd:cd01234     81 FNAVKEGDSVIFASDDENDRQLWVQALYRATGQSHKPVPPTQ 122
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
522-623 1.74e-11

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: 61.80  E-value: 1.74e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110   522 MKHSGYLWAIGKNVWKRWKKRFFVLvqvsqYTFAMCSYREKKA----EPQELLQLDGYTVDYTDPQPGLEGGRAFFNAVK 597
Cdd:smart00233    1 VIKEGWLYKKSGGGKKSWKKRYFVL-----FNSTLLYYKSKKDkksyKPKGSIDLSGCTVREAPDPDSSKKPHCFEIKTS 75
                            90       100
                    ....*....|....*....|....*.
gi 1622908110   598 EGDTVIFASDDEQDRILWVQAMYRAT 623
Cdd:smart00233   76 DRKTLLLQAESEEEREKWVEALRKAI 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
523-622 9.20e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 54.49  E-value: 9.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  523 KHSGYLWAIGKNVWKRWKKRFFVLVQVSQYTFAmCSYREKKAEPQELLQLDGYTVDYTDPQPglEGGRAF-----FNAVK 597
Cdd:pfam00169    2 VKEGWLLKKGGGKKKSWKKRYFVLFDGSLLYYK-DDKSGKSKEPKGSISLSGCEVVEVVASD--SPKRKFcfelrTGERT 78
                           90       100
                   ....*....|....*....|....*
gi 1622908110  598 EGDTVIFASDDEQDRILWVQAMYRA 622
Cdd:pfam00169   79 GKRTYLLQAESEEERKDWIKAIQSA 103
 
Name Accession Description Interval E-value
MUN pfam06292
MUN domain; This entry corresponds to the MUN domain found in Munc13 proteins. These ...
836-1241 8.07e-168

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: 507.71  E-value: 8.07e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  836 TVIRKCLEQAALVNYSRLSEYA-------------KIEENVGRLITPAKKLEDTIRLAELVIEVLQQNEEHHAEGKEAFA 902
Cdd:pfam06292    1 QVVKDCLKAAALSNYQRLFENAyelsrefkiedkeSIPEESQGLGPSEKRLDFWIKLIELCVSVLQQDKEHYAPVLNQFP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  903 WWSDLMVEHAETFLSLFAVDMDAALEVQ------PPDTWDS--FPLFQLLNDFLRTDYNLRNGKFHKHLQDLFAPLVVRY 974
Cdd:pfam06292   81 WELDLGAEHAEIFWSLFAVDMDAALEEHeqhrlcKPDSWMNlhFKVKWLLNDYLRDDPTLKNGKFHPHYPDWFEPFVMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  975 VDLMESSIAQSIHRGFERESWEPV------NNGSGTSEDLFWKLDALQTFIRDLHWPEEEFGKHLEQRLKLMASDMIESC 1048
Cdd:pfam06292  161 LDLNESSIAQSLHGGFERDKKDGFqqssehALFSSSVVDLFWKLNQLQDFIKKLEWPDPEFAAHLEKRFKLMASDMLLAY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110 1049 VKRTRIAFEVKLQKtsrstdfrvPQSICTMFNVMVDAKAQSTK--LC---SMEMGQEHQYHSKIDELIEETVKEMITLLV 1123
Cdd:pfam06292  241 AKRTRKAFDSKLKK---------PRTACTMMNNIQQARVQLEKmfLCmggDELDGEAHQYLTELQVLLEGVLDEMSSIFA 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110 1124 AKFVTILEGVLAKLSR--------------YDEGTLFSSFLSFtvkaaskyvdvpkpgmdVADAYVTFVRHSQDVLRDKV 1189
Cdd:pfam06292  312 DSFEPVLESVLSKLSRllqqikgsnrnnaaYDEGTLLSPLMDF-----------------LDGNLSLFARICEKTVLKRV 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110 1190 NEEMY-----------------------------------------------IERLFDQWYNSSMNVICTWLTDRMDLQL 1222
Cdd:pfam06292  375 LKELWkivmntlektvvlpplsdqsgsqlkllmslegaknltpkqcaildaaLETIFQYFHAGGNGLKKTWLEKSPELQL 454
                          490
                   ....*....|....*....
gi 1622908110 1223 HIYQLKTLIRMVKKTYRDF 1241
Cdd:pfam06292  455 LRYALSLYTQTTDKLIKDF 473
PH_CADPS cd01234
Ca2+-dependent activator protein (also called CAPS) Pleckstrin homology (PH) domain; CADPS ...
515-634 1.77e-86

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: 276.17  E-value: 1.77e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  515 RMDKPQNMKHSGYLWAIGKNVWKRWKKRFFVLVQVSQYTFAMCSYREKKAEPQELLQLDGYTVDYTDPQP--GLEGGRAF 592
Cdd:cd01234      1 RMDKPQNMKHCGYLYALGKSVWKKWKKRYFVLVQVSQYTFAMCSYREKKSEPQEMMQLDGYTVDYTDPQPdlGLEGGRFF 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622908110  593 FNAVKEGDTVIFASDDEQDRILWVQAMYRATGQSHKPVPPTQ 634
Cdd:cd01234     81 FNAVKEGDSVIFASDDENDRQLWVQALYRATGQSHKPVPPTQ 122
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
522-623 1.74e-11

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: 61.80  E-value: 1.74e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110   522 MKHSGYLWAIGKNVWKRWKKRFFVLvqvsqYTFAMCSYREKKA----EPQELLQLDGYTVDYTDPQPGLEGGRAFFNAVK 597
Cdd:smart00233    1 VIKEGWLYKKSGGGKKSWKKRYFVL-----FNSTLLYYKSKKDkksyKPKGSIDLSGCTVREAPDPDSSKKPHCFEIKTS 75
                            90       100
                    ....*....|....*....|....*.
gi 1622908110   598 EGDTVIFASDDEQDRILWVQAMYRAT 623
Cdd:smart00233   76 DRKTLLLQAESEEEREKWVEALRKAI 101
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
525-622 4.10e-09

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: 55.36  E-value: 4.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  525 SGYLWAIGKNVWKRWKKRFFVLVQvsqytfaMCSYREKKAEPQELL---QLDGYTVdyTDPQPGLEGGRAF-FNAVKEG- 599
Cdd:cd13248     10 SGWLHKQGGSGLKNWRKRWFVLKD-------NCLYYYKDPEEEKALgsiLLPSYTI--SPAPPSDEISRKFaFKAEHANm 80
                           90       100
                   ....*....|....*....|...
gi 1622908110  600 DTVIFASDDEQDRILWVQAMYRA 622
Cdd:cd13248     81 RTYYFAADTAEEMEQWMNAMSLA 103
PH pfam00169
PH domain; PH stands for pleckstrin homology.
523-622 9.20e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 54.49  E-value: 9.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  523 KHSGYLWAIGKNVWKRWKKRFFVLVQVSQYTFAmCSYREKKAEPQELLQLDGYTVDYTDPQPglEGGRAF-----FNAVK 597
Cdd:pfam00169    2 VKEGWLLKKGGGKKKSWKKRYFVLFDGSLLYYK-DDKSGKSKEPKGSISLSGCEVVEVVASD--SPKRKFcfelrTGERT 78
                           90       100
                   ....*....|....*....|....*
gi 1622908110  598 EGDTVIFASDDEQDRILWVQAMYRA 622
Cdd:pfam00169   79 GKRTYLLQAESEEERKDWIKAIQSA 103
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
524-619 3.02e-05

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: 44.07  E-value: 3.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  524 HSGYLWAIGKNVWKRWKKRFFVLvqvSQYTFAMCSYR-EKKAEPQELLQLDGyTVDYTDPQPGlEGGRAFFNAVKEGDTV 602
Cdd:cd00821      1 KEGYLLKRGGGGLKSWKKRWFVL---FEGVLLYYKSKkDSSYKPKGSIPLSG-ILEVEEVSPK-ERPHCFELVTPDGRTY 75
                           90
                   ....*....|....*..
gi 1622908110  603 IFASDDEQDRILWVQAM 619
Cdd:cd00821     76 YLQADSEEERQEWLKAL 92
PH2_FGD5_FGD6 cd13237
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6 pleckstrin ...
525-619 2.64e-03

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: 38.16  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  525 SGYLWaIGKNVWKRWKKRFFVLVQVSQYTFAMcsyREKKAePQELLQLDGYTVDYTDPQPGLEGGRAFFNAVKEGDTVIF 604
Cdd:cd13237      2 SGYLQ-RRKKSKKSWKRLWFVLKDKVLYTYKA---SEDVV-ALESVPLLGFTVVTIDESFEEDESLVFQLLHKGQLPIIF 76
                           90
                   ....*....|....*
gi 1622908110  605 ASDDEQDRILWVQAM 619
Cdd:cd13237     77 RADDAETAQRWIEAL 91
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
520-624 3.24e-03

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: 38.90  E-value: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  520 QNMKHSGYLWAIGKNVwKRWKKRFFVLVQVSQYTFAmcsyREKKAEPQELLQLDGYTVDYTDPQPGlEGGRAFFNAVKEG 599
Cdd:cd13263      1 ERPIKSGWLKKQGSIV-KNWQQRWFVLRGDQLYYYK----DEDDTKPQGTIPLPGNKVKEVPFNPE-EPGKFLFEIIPGG 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1622908110  600 ---------DTVIFASDDEQDRILWVQAMYRATG 624
Cdd:cd13263     75 ggdrmtsnhDSYLLMANSQAEMEEWVKVIRRVIG 108
PH_Boi cd13316
Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally ...
524-623 4.26e-03

Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally redundant and important for cell growth with Boi mutants displaying defects in bud formation and in the maintenance of cell polarity.They appear to be linked to Rho-type GTPase, Cdc42 and Rho3. Boi1 and Boi2 display two-hybrid interactions with the GTP-bound ("active") form of Cdc42, while Rho3 can suppress of the lethality caused by deletion of Boi1 and Boi2. These findings suggest that Boi1 and Boi2 are targets of Cdc42 that promote cell growth in a manner that is regulated by Rho3. Boi proteins contain a N-terminal SH3 domain, followed by a SAM (sterile alpha motif) domain, a proline-rich region, which mediates binding to the second SH3 domain of Bem1, and C-terminal PH domain. The PH domain is essential for its function in cell growth and is important for localization to the bud, while the SH3 domain is needed for localization to the neck. 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: 270126  Cd Length: 97  Bit Score: 37.74  E-value: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  524 HSGYLWAIGKNvWKRWKKRFFVLVQVSQYTFamcsYREKKAEPQELLQLDGYTVdYTDPQPGLEGGRAFFNAV--KEGDT 601
Cdd:cd13316      2 HSGWMKKRGER-YGTWKTRYFVLKGTRLYYL----KSENDDKEKGLIDLTGHRV-VPDDSNSPFRGSYGFKLVppAVPKV 75
                           90       100
                   ....*....|....*....|..
gi 1622908110  602 VIFASDDEQDRILWVQAMYRAT 623
Cdd:cd13316     76 HYFAVDEKEELREWMKALMKAT 97
PH_SWAP-70 cd13273
Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called ...
526-622 4.58e-03

Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called Differentially expressed in FDCP 6/DEF-6 or IRF4-binding protein) functions in cellular signal transduction pathways (in conjunction with Rac), regulates cell motility through actin rearrangement, and contributes to the transformation and invasion activity of mouse embryo fibroblasts. Metazoan SWAP-70 is found in B lymphocytes, mast cells, and in a variety of organs. Metazoan SWAP-70 contains an N-terminal EF-hand motif, a centrally located PH domain, and a C-terminal coiled-coil domain. The PH domain of Metazoan SWAP-70 contains a phosphoinositide-binding site and a nuclear localization signal (NLS), which localize SWAP-70 to the plasma membrane and nucleus, respectively. The NLS is a sequence of four Lys residues located at the N-terminus of the C-terminal a-helix; this is a unique characteristic of the Metazoan SWAP-70 PH domain. The SWAP-70 PH domain binds PtdIns(3,4,5)P3 and PtdIns(4,5)P2 embedded in lipid bilayer vesicles. There are additional plant SWAP70 proteins, but these are not included in this hierarchy. Rice SWAP70 (OsSWAP70) exhibits GEF activity toward the its Rho GTPase, OsRac1, and regulates chitin-induced production of reactive oxygen species and defense gene expression in rice. Arabidopsis SWAP70 (AtSWAP70) plays a role in both PAMP- and effector-triggered immunity. Plant SWAP70 contains both DH and PH domains, but their arrangement is the reverse of that in typical DH-PH-type Rho GEFs, wherein the DH domain is flanked by a C-terminal 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: 270092  Cd Length: 110  Bit Score: 38.05  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  526 GYLWAIGkNVWKRWKKRFFVL--VQVSQYTFAMCsyREKKAEpqelLQLDGYTVdyTDPQPGLEGGRAFFnAVKEGDTV- 602
Cdd:cd13273     12 GYLWKKG-HLLPTWTERWFVLkpNSLSYYKSEDL--KEKKGE----IALDSNCC--VESLPDREGKKCRF-LVKTPDKTy 81
                           90       100
                   ....*....|....*....|.
gi 1622908110  603 -IFASDDEQdRILWVQAMYRA 622
Cdd:cd13273     82 eLSASDHKT-RQEWIAAIQTA 101
PH_3BP2 cd13308
SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes ...
524-627 5.75e-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: 38.16  E-value: 5.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908110  524 HSGYLWAIGKN--VWKRWKKRFFVLVQVSQYTFAmcsyREKKAEPQELLQLDGYTVdytDPQPGLEGGRAF----FNAVK 597
Cdd:cd13308     11 HSGTLTKKGGSqkTLQNWQLRYVIIHQGCVYYYK----NDQSAKPKGVFSLNGYNR---RAAEERTSKLKFvfkiIHLSP 83
                           90       100       110
                   ....*....|....*....|....*....|
gi 1622908110  598 EGDTVIFASDDEQDRILWVQAMYRATGQSH 627
Cdd:cd13308     84 DHRTWYFAAKSEDEMSEWMEYIRREIDHYC 113
 
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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