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Conserved domains on  [gi|694958715|ref|XP_009427073|]
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1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 isoform X1 [Pan troglodytes]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 311-649 0e+00

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 2. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta2 is expressed at highest levels in cells of hematopoietic origin. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins.


:

Pssm-ID: 176561 [Multi-domain]  Cd Length: 261  Bit Score: 563.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08624     1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08624    81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtaYEEMSSLV 550
Cdd:cd08624   155 ------------------------------------------------------------------------YEEMSSLV 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08624   163 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVAL 242

                         330
                  ....*....|....*....
gi 694958715  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08624   243 NFQTMDLPMQQNMALFEFN 261
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 149-299 1.26e-102

EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2, or phospholipase C-beta-2 (PLC-beta2), is expressed at highest levels in cells of hematopoietic origin. It is activated by the heterotrimeric G protein alpha q subunits (G alpha(q)) through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins. PI-PLC-beta2 has two cellular binding partners, alpha- and gamma-synuclein. The binding of either alpha- and gamma-synuclein inhibits PI-PLC-beta2 activity through preventing the binding of its activator G alpha(q). However, the binding of gamma-synuclein to PI-PLC-beta2 does not affect its binding to G beta(gamma) subunits or small G proteins, but enhances these signals. Meanwhile, gamma-synuclein may protect PI-PLC-beta2 from protease degradation and contribute to its over-expression in breast cancer. In leukocytes, the G beta(gamma)-mediated activation of PI-PLC-beta2 can be promoted by a scaffolding protein WDR26, which is also required for the translocation of PI-PLC-beta2 from the cytosol to the membrane in polarized leukocytes. PI-PLC-beta2 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


:

Pssm-ID: 320039  Cd Length: 151  Bit Score: 321.06  E-value: 1.26e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  149 DKILVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEINEIFTSY 228
Cdd:cd16209     1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694958715  229 HAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16209    81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 1069-1210 3.74e-77

PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of phospholipase C beta.


:

Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 251.91  E-value: 3.74e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1069 EQISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMT 1148
Cdd:pfam08703   35 EQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEAKKRTSDKAAQERLKKEINNSHIQEVVQSIKQLE 114

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694958715  1149 ENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAEVKESVRACLRTCFPSE 1210
Cdd:pfam08703  115 EKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAEVRESVKSCLKEGFPDE 176
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-141 4.22e-69

PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C enzymes.


:

Pssm-ID: 465506  Cd Length: 131  Bit Score: 227.26  E-value: 4.22e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715    12 KVKAYLSQGERFIKWDDETTVASP-VILRVDPKGYYLYWTYQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVFNMDFP 90
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 694958715    91 DNSFLLKTLTVVSGPDMVDLTFHNFVSYKENVGKVWAEDVLALVKHPLTAN 141
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 681-802 9.43e-38

C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) to d-myo-inositol-1,4,5-trisphosphate (1,4,5-IP3) and sn-1,2-diacylglycerol (DAG). 1,4,5-IP3 and DAG are second messengers in eukaryotic signal transduction cascades. PLC is composed of a N-terminal PH domain followed by a series of EF hands, a catalytic TIM barrel and a C-terminal C2 domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology.


:

Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 137.67  E-value: 9.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  681 ATTLSITVISGQFLS------ERSVRTYVEVELFGLPGDPKRRYRTKLSPStNSINPVWkEEPFVFEKIlMPELASLRVA 754
Cdd:cd00275     1 PLTLTIKIISGQQLPkpkgdkGSIVDPYVEVEIHGLPADDSAKFKTKVVKN-NGFNPVW-NETFEFDVT-VPELAFLRFV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 694958715  755 VMEE---GNKFLGHRIIPINALNSGYHHLCLHSESNMPLTMPALFIFLEMK 802
Cdd:cd00275    78 VYDEdsgDDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
 
Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 311-649 0e+00

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 2. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta2 is expressed at highest levels in cells of hematopoietic origin. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins.


Pssm-ID: 176561 [Multi-domain]  Cd Length: 261  Bit Score: 563.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08624     1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08624    81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtaYEEMSSLV 550
Cdd:cd08624   155 ------------------------------------------------------------------------YEEMSSLV 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08624   163 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVAL 242

                         330
                  ....*....|....*....
gi 694958715  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08624   243 NFQTMDLPMQQNMALFEFN 261
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 149-299 1.26e-102

EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2, or phospholipase C-beta-2 (PLC-beta2), is expressed at highest levels in cells of hematopoietic origin. It is activated by the heterotrimeric G protein alpha q subunits (G alpha(q)) through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins. PI-PLC-beta2 has two cellular binding partners, alpha- and gamma-synuclein. The binding of either alpha- and gamma-synuclein inhibits PI-PLC-beta2 activity through preventing the binding of its activator G alpha(q). However, the binding of gamma-synuclein to PI-PLC-beta2 does not affect its binding to G beta(gamma) subunits or small G proteins, but enhances these signals. Meanwhile, gamma-synuclein may protect PI-PLC-beta2 from protease degradation and contribute to its over-expression in breast cancer. In leukocytes, the G beta(gamma)-mediated activation of PI-PLC-beta2 can be promoted by a scaffolding protein WDR26, which is also required for the translocation of PI-PLC-beta2 from the cytosol to the membrane in polarized leukocytes. PI-PLC-beta2 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


Pssm-ID: 320039  Cd Length: 151  Bit Score: 321.06  E-value: 1.26e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  149 DKILVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEINEIFTSY 228
Cdd:cd16209     1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694958715  229 HAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16209    81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 314-462 2.51e-79

Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to form a single structural unit.


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 256.66  E-value: 2.51e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715   314 MTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIAE 393
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694958715   394 SAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKN 462
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLD----DDLTELPSPEDLKGKILIKG 142
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 1069-1210 3.74e-77

PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of phospholipase C beta.


Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 251.91  E-value: 3.74e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1069 EQISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMT 1148
Cdd:pfam08703   35 EQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEAKKRTSDKAAQERLKKEINNSHIQEVVQSIKQLE 114

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694958715  1149 ENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAEVKESVRACLRTCFPSE 1210
Cdd:pfam08703  115 EKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAEVRESVKSCLKEGFPDE 176
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-141 4.22e-69

PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C enzymes.


Pssm-ID: 465506  Cd Length: 131  Bit Score: 227.26  E-value: 4.22e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715    12 KVKAYLSQGERFIKWDDETTVASP-VILRVDPKGYYLYWTYQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVFNMDFP 90
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 694958715    91 DNSFLLKTLTVVSGPDMVDLTFHNFVSYKENVGKVWAEDVLALVKHPLTAN 141
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 314-463 6.79e-65

Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. These enzymes contain 2 regions (X and Y) which together form a TIM barrel-like structure containing the active site residues. Phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The bacterial enzyme appears to be a homologue of the mammalian PLCs.


Pssm-ID: 197543 [Multi-domain]  Cd Length: 143  Bit Score: 215.99  E-value: 6.79e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715    314 MTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIAE 393
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDG--PDGEPVIYHGHTFTLPIKLSEVLEAIKD 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715    394 SAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKpgvpLPSPEDLRGKILIKNK 463
Cdd:smart00148   79 FAFVTSPYPVILSLENHC-SPDQQAKMAQMFKEIFGDMLYTPPLTSSLEV----LPSPEQLRGKILLKVR 143
PLN02228 PLN02228
Phosphoinositide phospholipase C
 217-786 3.30e-58

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 211.43  E-value: 3.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  217 PRPEINEIFTSYHAKAKpyMTKEHLTKFINQKQRDSRlnsllfppARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLC 296
Cdd:PLN02228   22 PPVSIKRLFEAYSRNGK--MSFDELLRFVSEVQGERH--------AGLDYVQDIFHSVKHHNVFHHHGLVHLNAFYRYLF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  297 GPENSVLAQDKLLlHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKgKPPDEEPIITHGF 376
Cdd:PLN02228   92 SDTNSPLPMSGQV-HHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWP-NPSGNAAEVRHGR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  377 TMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLL---TEPLEKFplkpgvplPSPED 453
Cdd:PLN02228  170 TLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHL-PPNLQAQVAKMLTKTFRGMLFrctSESTKHF--------PSPEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  454 LRGKILIKNKKNQFSGPTSSSKDTggeaegssppSAPAGEGTVWAGEEGTeleeeeveeeeeeesgnldEEEIKKMQSDE 533
Cdd:PLN02228  241 LKNKILISTKPPKEYLESKTVQTT----------RTPTVKETSWKRVADA-------------------ENKILEEYKDE 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  534 GTAGLEvtaYEEMSSL--VNYIQPTKFVsfeFSAQKNRSYVIsSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMD 611
Cdd:PLN02228  292 ESEAVG---YRDLIAIhaANCKDPLKDC---LSDDPEKPIRV-SMDEQWLETMVRTRGTDLVRFTQRNLVRIYPKGTRVD 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  612 SSNYMPQMFWNAGCQMVALNFQT--MDLPMQQNMavFEFNGQSGYLLKHEFMRRPDKQFNPFSvdriDVVVATTLSITVI 689
Cdd:PLN02228  365 SSNYDPHVGWTHGAQMVAFNMQGhgKQLWIMQGM--FRANGGCGYVKKPRILLDEHTLFDPCK----RLPIKTTLKVKIY 438

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  690 SGQ----------FLSERSVRTYVEVELFGLPGDPKrRYRTKLspSTNSINPVWKEEPFVFEkILMPELASLRVAVME-- 757
Cdd:PLN02228  439 TGEgwdldfhlthFDQYSPPDFFVKIGIAGVPRDTV-SYRTET--AVDQWFPIWGNDEFLFQ-LRVPELALLWFKVQDyd 514

                         570       580       590
                  ....*....|....*....|....*....|.
gi 694958715  758 --EGNKFLGHRIIPINALNSGYHHLCLHSES 786
Cdd:PLN02228  515 ndTQNDFAGQTCLPLPELKSGVRAVRLHDRA 545
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-144 4.73e-56

Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is regulated by heterotrimeric G protein-coupled receptors through their C2 domain and long C-terminal extension which forms an autoinhibitory helix. There are four isoforms: PLC-beta1-4. The PH domain of PLC-beta2 and PLC-beta3 plays a dual role, much like PLC-delta1, by binding to the plasma membrane, as well as the interaction site for the catalytic activator. However, PLC-beta binds to the lipid surface independent of PIP2. PLC-beta1 seems to play unspecified roles in cellular proliferation and differentiation. PLC-beta consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves, a C2 domain and a C-terminal PDZ. Members of the Rho GTPase family (e.g., Rac1, Rac2, Rac3, and cdc42) have been implicated in their activation by binding to an alternate site on the N-terminal PH domain. A basic amino acid region within the enzyme's long C-terminal tail appears to function as a Nuclear Localization Signal for import into the nucleus. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). 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.the plasma membrane, but only a few (less than 10%) display strong specificity in binding inositol phosphates. 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 kinases, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, cytoskeletal associated molecules, and in lipid associated enzymes.


Pssm-ID: 270167  Cd Length: 127  Bit Score: 190.09  E-value: 4.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715   17 LSQGERFIKWDDETTVASPVILRVDPKGYYLYWTYQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVfNMDFPDNSFLL 96
Cdd:cd13361     1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 694958715   97 KTLTVVSGPDMVDLTFHNFVSYKENVGKVWAEDVLALVKHPLTANASR 144
Cdd:cd13361    80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 681-802 9.43e-38

C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) to d-myo-inositol-1,4,5-trisphosphate (1,4,5-IP3) and sn-1,2-diacylglycerol (DAG). 1,4,5-IP3 and DAG are second messengers in eukaryotic signal transduction cascades. PLC is composed of a N-terminal PH domain followed by a series of EF hands, a catalytic TIM barrel and a C-terminal C2 domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology.


Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 137.67  E-value: 9.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  681 ATTLSITVISGQFLS------ERSVRTYVEVELFGLPGDPKRRYRTKLSPStNSINPVWkEEPFVFEKIlMPELASLRVA 754
Cdd:cd00275     1 PLTLTIKIISGQQLPkpkgdkGSIVDPYVEVEIHGLPADDSAKFKTKVVKN-NGFNPVW-NETFEFDVT-VPELAFLRFV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 694958715  755 VMEE---GNKFLGHRIIPINALNSGYHHLCLHSESNMPLTMPALFIFLEMK 802
Cdd:cd00275    78 VYDEdsgDDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 683-779 7.43e-14

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: 68.67  E-value: 7.43e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715    683 TLSITVISGQFLSER----SVRTYVEVELFGlpgDPKRRYRTKLSPSTNsiNPVWKEEpFVFEkILMPELASLRVAVMEE 758
Cdd:smart00239    1 TLTVKIISARNLPPKdkggKSDPYVKVSLDG---DPKEKKKTKVVKNTL--NPVWNET-FEFE-VPPPELAELEIEVYDK 73

                            90       100
                    ....*....|....*....|....*
gi 694958715    759 ----GNKFLGHRIIPINALNSGYHH 779
Cdd:smart00239   74 drfgRDDFIGQVTIPLSDLLLGGRH 98
C2 pfam00168
C2 domain;
683-776 3.34e-10

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 58.48  E-value: 3.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715   683 TLSITVISGQFL----SERSVRTYVEVELfglpGDPKRRYRTKLSPstNSINPVWKEEpFVFEkILMPELASLRVAVMEE 758
Cdd:pfam00168    2 RLTVTVIEAKNLppkdGNGTSDPYVKVYL----LDGKQKKKTKVVK--NTLNPVWNET-FTFS-VPDPENAVLEIEVYDY 73

                           90       100
                   ....*....|....*....|..
gi 694958715   759 ----GNKFLGHRIIPINALNSG 776
Cdd:pfam00168   74 drfgRDDFIGEVRIPLSELDSG 95
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 215-303 3.01e-08

Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are predominantly found in phosphoinositide-specific phospholipase C. They adopt a structure consisting of a core of four alpha helices, in an EF like fold, and are required for functioning of the enzyme.


Pssm-ID: 401279 [Multi-domain]  Cd Length: 85  Bit Score: 52.25  E-value: 3.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715   215 LCPRPEINEIFTSYhAKAKPYMTKEHLTKFINQKQRDSRlnsllfppARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWF 294
Cdd:pfam09279    5 LTQREEIDEIFQEY-SGDGQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAMTKDGFLMY 75


                   ....*....
gi 694958715   295 LCGPENSVL 303
Cdd:pfam09279   76 LCSPDGSIF 84
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1076-1197 9.02e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.38  E-value: 9.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1076 ELAREKQAAE--LKALKETSEnDTKEMKKKLET------KRLERIQG-MTKVTTDKMAQ------ERLKREIN--NSHIQ 1138
Cdd:COG1579    35 ELEDELAALEarLEAAKTELE-DLEKEIKRLELeieeveARIKKYEEqLGNVRNNKEYEalqkeiESLKRRISdlEDEIL 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 694958715 1139 EVVQVIKQMTENLERHQEKLEEKQaaclEQIREMEKQFQkEALAEYEARMKGLEAEVKE 1197
Cdd:COG1579   114 ELMERIEELEEELAELEAELAELE----AELEEKKAELD-EELAELEAELEELEAEREE 167
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1057-1242 1.90e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 1.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1057 LQARSRQGLSQEEQISKM-MELAREKQAAELKALKETSENDTKEMKKKletkRLERIQGMTKVTTDKMA-----QERLKR 1130
Cdd:TIGR02168  791 IEQLKEELKALREALDELrAELTLLNEEAANLRERLESLERRIAATER----RLEDLEEQIEELSEDIEslaaeIEELEE 866

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1131 EINNSHIQ--EVVQVIKQMTENLERHQEKLEEKQaaclEQIREMEKQFQK---------EALAEYEARMKGLEAEVKEsv 1199
Cdd:TIGR02168  867 LIEELESEleALLNERASLEEALALLRSELEELS----EELRELESKRSElrreleelrEKLAQLELRLEGLEVRIDN-- 940

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 694958715  1200 racLRTCFPSEAKDKPERACECPPELceqDPLIAKADAQESRL 1242
Cdd:TIGR02168  941 ---LQERLSEEYSLTLEEAEALENKI---EDDEEEARRRLKRL 977
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1058-1180 5.18e-05

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 46.80  E-value: 5.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1058 QARSRQGLSQEEQISKMMElarEKQAAE---LKALKETSENDTKEMKKKLETKRLERIQGMTKVttDKMAQERLKREINN 1134
Cdd:cd16269   159 RQVPRKGVKAEEVLQEFLQ---SKEAEAeaiLQADQALTEKEKEIEAERAKAEAAEQERKLLEE--QQRELEQKLEDQER 233

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 694958715 1135 SHIQEVVQVIKQMTENLERHQEKLEEKQAACL-EQIREMEKQFQKEA 1180
Cdd:cd16269   234 SYEEHLRQLKEKMEEERENLLKEQERALESKLkEQEALLEEGFKEQA 280
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1068-1197 1.17e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1068 EEQISKMMELAR--EKQAAELkalkETSENDTKEMKKKLET--KRLERIQGMTKVTTD---KMAQ-ERLKREINNSHIQE 1139
Cdd:PRK03918  313 EKRLSRLEEEINgiEERIKEL----EEKEERLEELKKKLKEleKRLEELEERHELYEEakaKKEElERLKKRLTGLTPEK 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1140 vvqvIKQMTENLERHQEKLEEKQAACLEQIREMEK----------------------------QFQKEALAEYEARMKGL 1191
Cdd:PRK03918  389 ----LEKELEELEKAKEEIEEEISKITARIGELKKeikelkkaieelkkakgkcpvcgrelteEHRKELLEEYTAELKRI 464


                  ....*.
gi 694958715 1192 EAEVKE 1197
Cdd:PRK03918  465 EKELKE 470
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 1078-1175 2.77e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 39.71  E-value: 2.77e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715   1078 AREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMT--KVTTDKM---AQERLKREINNSHIQEvvqviKQMTENLE 1152
Cdd:smart01071   40 ARVERMEEIKNLKYELIMNDHLNKRIDKLLKGLREEELSpeTPTYNEMlaeLQDQLKKELEEANGDS-----EGLLEELK 114

                            90       100
                    ....*....|....*....|...
gi 694958715   1153 RHQEKLEEKQAACLEQIREMEKQ 1175
Cdd:smart01071  115 KHRDKLKKEQKELRKKLDELEKE 137
 
Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 311-649 0e+00

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 2. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta2 is expressed at highest levels in cells of hematopoietic origin. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins.


Pssm-ID: 176561 [Multi-domain]  Cd Length: 261  Bit Score: 563.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08624     1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08624    81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtaYEEMSSLV 550
Cdd:cd08624   155 ------------------------------------------------------------------------YEEMSSLV 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08624   163 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVAL 242

                         330
                  ....*....|....*....
gi 694958715  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08624   243 NFQTMDLPMQQNMALFEFN 261
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
 311-649 0e+00

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are four PLC-beta isozymes (1-4). They are activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. The beta-gamma subunits of heterotrimeric G proteins are known to activate the PLC-beta2 and -beta3 isozymes only. Aside from four PLC-beta isozymes identified in mammals, some eukaryotic PLC-beta homologs have been classified into this subfamily, such as NorpA and PLC-21 from Drosophila and PLC-beta from turkey, Xenopus, sponge, and hydra.


Pssm-ID: 176533 [Multi-domain]  Cd Length: 257  Bit Score: 546.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08591     1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVDSPrQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08591    81 IAETAFKTSEYPVILSFENHCSSK-QQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSLV 550
Cdd:cd08591   154 ---------------------------------------------------------------------------LSSLV 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08591   159 NYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQLSRIYPKGTRVDSSNYMPQIFWNAGCQMVAL 238

                         330
                  ....*....|....*....
gi 694958715  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08591   239 NFQTPDLPMQLNQGKFEYN 257
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
 313-649 1.27e-148

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 3. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta3 is widely expressed at highest levels in brain, liver, and parotid gland. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins.


Pssm-ID: 176562 [Multi-domain]  Cd Length: 258  Bit Score: 447.96  E-value: 1.27e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  313 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEAIA 392
Cdd:cd08625     3 DMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEAIA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  393 ESAFKTSPYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgpts 472
Cdd:cd08625    83 ESAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK-------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  473 sskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSLVNY 552
Cdd:cd08625   155 -------------------------------------------------------------------------MSTLVNY 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  553 IQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVALNF 632
Cdd:cd08625   162 IEPVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPMEFVEYNKKQLSRIYPKGTRVDSSNYMPQLFWNVGCQMVALNF 241

                         330
                  ....*....|....*..
gi 694958715  633 QTMDLPMQQNMAVFEFN 649
Cdd:cd08625   242 QTLDLAMQLNMGVFEYN 258
PI-PLCc_eukaryota cd08558
Catalytic domain of eukaryotic phosphoinositide-specific phospholipase C and similar proteins; ...
 311-649 2.85e-135

Catalytic domain of eukaryotic phosphoinositide-specific phospholipase C and similar proteins; This family corresponds to the catalytic domain present in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) and similar proteins. The higher eukaryotic PI-PLCs play a critical role in most signal transduction pathways, controlling numerous cellular events such as cell growth, proliferation, excitation and secretion. They strictly require Ca2+ for the catalytic activity. They display a clear preference towards the hydrolysis of the more highly phosphorylated membrane phospholipids PI-analogues, phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidylinositol-4-phosphate (PIP), to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. The eukaryotic PI-PLCs have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains, such as the pleckstrin homology (PH) domain, EF-hand motif, and C2 domain. The catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a linker region. The catalytic mechanism of eukaryotic PI-PLCs is based on general base and acid catalysis utilizing two well conserved histidines and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. The mammalian PI-PLCs consist of 13 isozymes, which are classified into six-subfamilies, PI-PLC-delta (1,3 and 4), -beta(1-4), -gamma(1,2), -epsilon, -zeta, and -eta (1,2). Ca2+ is required for the activation of all forms of mammalian PI-PLCs, and the concentration of calcium influences substrate specificity. This family also includes metazoan phospholipase C related but catalytically inactive proteins (PRIP), which belong to a group of novel inositol trisphosphate binding proteins. Due to the replacement of critical catalytic residues, PRIP does not have PLC enzymatic activity.


Pssm-ID: 176501 [Multi-domain]  Cd Length: 226  Bit Score: 411.07  E-value: 2.85e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08558     1 YQDMTQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGHTLTSKILFKDVIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEKFPlkpgVPLPSPEDLRGKILIKNKKNQfsgp 470
Cdd:cd08558    79 IKEYAFVTSPYPVILSLENHC-SLEQQKKMAQILKEIFGDKLLTPPLDENP----VQLPSPEQLKGKILIKGKKYH---- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeemsslv 550
Cdd:cd08558       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  551 nyiqptkfvsfefsaqknrsyvISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08558   150 ----------------------MSSFSETKALKLLKESPEEFVKYNKRQLSRVYPKGTRVDSSNYNPQPFWNAGCQMVAL 207

                         330
                  ....*....|....*....
gi 694958715  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08558   208 NYQTPDLPMQLNQGKFEQN 226
PI-PLCc_beta1 cd08623
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1; This subfamily ...
 313-649 1.21e-132

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 1. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta1 is expressed at highest levels in specific regions of the brain. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension.


Pssm-ID: 176560 [Multi-domain]  Cd Length: 258  Bit Score: 405.62  E-value: 1.21e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  313 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEAIA 392
Cdd:cd08623     3 DMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  393 ESAFKTSPYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgpts 472
Cdd:cd08623    83 ECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKK-------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  473 sskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSLVNY 552
Cdd:cd08623   155 -------------------------------------------------------------------------MSNLVNY 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  553 IQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVALNF 632
Cdd:cd08623   162 IQPVKFESFEASKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNF 241

                         330
                  ....*....|....*..
gi 694958715  633 QTMDLPMQQNMAVFEFN 649
Cdd:cd08623   242 QTVDLSMQINMGMYEYN 258
PI-PLCc_beta4 cd08626
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4; This subfamily ...
 311-649 1.53e-130

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 4. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta4 is expressed in high concentrations in cerebellar Purkinje and granule cells, the median geniculate body, and the lateral geniculate nucleus. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension.


Pssm-ID: 176563 [Multi-domain]  Cd Length: 257  Bit Score: 400.29  E-value: 1.53e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08626     1 YQDMDQPLAHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCIELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVDSPrQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08626    81 IKDTAFVTSDYPVILSFENHCSKP-QQYKLAKYCEEIFGDLLLTKPLESHPLEPGVPLPSPNKLKRKILIKNKR------ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSLV 550
Cdd:cd08626   154 ---------------------------------------------------------------------------LSSLV 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08626   159 NYAQPVKFQGFDVAEERNIHFNMSSFNESVGLGYLKTSAIEFVNYNKRQMSRIYPKGTRVDSSNYMPQIFWNAGCQMVSL 238

                         330
                  ....*....|....*....
gi 694958715  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08626   239 NFQTPDLGMQLNQGKFEYN 257
PI-PLCc_delta cd08593
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta; This subfamily ...
 311-649 4.52e-112

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-delta isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-delta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C-terminal C2 domain. This CD corresponds to the catalytic domain which is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1,3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. Aside from three PI-PLC-delta isozymes identified in mammals, some eukaryotic PI-PLC-delta homologs have been classified to this CD.


Pssm-ID: 176535 [Multi-domain]  Cd Length: 257  Bit Score: 350.87  E-value: 4.52e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08593     1 YQDMTQPLSHYFIASSHNTYLLEDQLKGPSSTEAYIRALKKGCRCVELDCWDG--PDGEPIIYHGHTLTSKILFKDVIQA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKNKKNQFSgp 470
Cdd:cd08593    79 IREYAFKVSPYPVILSLENHC-SVEQQKVMAQHLKSILGDKLLTQPLD----GVLTALPSPEELKGKILVKGKKLKLA-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSLV 550
Cdd:cd08593   152 -------------------------------------------------------------------------KELSDLV 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08593   159 IYCKSVHFKSFEHSKENYHFYEMSSFSESKALKLAQESGNEFVRHNKRQLSRIYPAGLRTDSSNYDPQEMWNVGCQIVAL 238

                         330
                  ....*....|....*....
gi 694958715  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08593   239 NFQTPGEEMDLNDGLFRQN 257
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 311-649 1.33e-110

Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This subfamily corresponds to the catalytic domain present in prokaryotic and eukaryotic phosphoinositide-specific phospholipase C (PI-PLC), which is a ubiquitous enzyme catalyzing the cleavage of the sn3-phosphodiester bond in the membrane phosphoinositides (phosphatidylinositol, PI; Phosphatidylinositol-4-phosphate, PIP; phosphatidylinositol 4,5-bisphosphate, PIP2) to yield inositol phosphates (inositol monosphosphate, InsP; inositol diphosphate, InsP2; inositol trisphosphate, InsP3) and diacylglycerol (DAG). The higher eukaryotic PI-PLCs (EC 3.1.4.11) have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. They play a critical role in most signal transduction pathways, controlling numerous cellular events, such as cell growth, proliferation, excitation and secretion. These PI-PLCs strictly require Ca2+ for their catalytic activity. They display a clear preference towards the hydrolysis of the more highly phosphorylated PI-analogues, PIP2 and PIP, to generate two important second messengers, InsP3 and DAG. InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. In contrast, bacterial PI-PLCs contain a single catalytic domain. Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. They participate in Ca2+-independent PI metabolism. They are characterized as phosphatidylinositol-specific phospholipase C (EC 4.6.1.13) that selectively hydrolyze PI, not PIP or PIP2. The TIM-barrel type catalytic domain in bacterial PI-PLCs is very similar to the one in eukaryotic PI-PLCs, in which the catalytic domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. The catalytic mechanism of both prokaryotic and eukaryotic PI-PLCs is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This superfamily also includes a distinctly different type of eukaryotic PLC, glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC), an integral membrane protein characterized in the protozoan parasite Trypanosoma brucei. T. brucei GPI-PLC hydrolyzes the GPI-anchor on the variant specific glycoprotein (VSG), releasing dimyristyl glycerol (DMG), which may facilitate the evasion of the protozoan to the host#s immune system. It does not require Ca2+ for its activity and is more closely related to bacterial PI-PLCs, but not mammalian PI-PLCs.


Pssm-ID: 176497 [Multi-domain]  Cd Length: 274  Bit Score: 347.71  E-value: 1.33e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFS-----GLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTtDIFFK 385
Cdd:cd00137     1 HHPDTQPLAHYSIPGTHDTYLTAGQFTikqvwGLTQTEMYRQQLLSGCRCVDIRCWDG--KPEEPIIYHGPTFL-DIFLK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  386 EAIEAIAESAFKTSPYPIILSFENHVDS-PRQQAKMAEYCRTIFGDMLLTeplekFPLKPGVPLPSPEDLRGKILIKNKK 464
Cdd:cd00137    78 EVIEAIAQFLKKNPPETIIMSLKNEVDSmDSFQAKMAEYCRTIFGDMLLT-----PPLKPTVPLPSLEDLRGKILLLNKK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  465 NQFSGPTSSSKDTGgeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtaye 544
Cdd:cd00137   153 NGFSGPTGSSNDTG------------------------------------------------------------------ 166

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  545 emsslvnyiqptkFVSFEFSAQKNRSYVISSFTELKAYD----LLSKASVQFVDYNKRQMSRIYPKGTR---------MD 611
Cdd:cd00137   167 -------------FVSFEFSTQKNRSYNISSQDEYKAYDdekvKLIKATVQFVDYNKNQLSRNYPSGTSggtawyyyaMD 233

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 694958715  612 SSNYMPQMFWN---AGCQMVALNFQTMDLPMQQNMAVFEFN 649
Cdd:cd00137   234 SNNYMPQMFWNanpAGCGIVILDFQTMDLPMQQYMAVIEFN 274
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 149-299 1.26e-102

EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2, or phospholipase C-beta-2 (PLC-beta2), is expressed at highest levels in cells of hematopoietic origin. It is activated by the heterotrimeric G protein alpha q subunits (G alpha(q)) through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins. PI-PLC-beta2 has two cellular binding partners, alpha- and gamma-synuclein. The binding of either alpha- and gamma-synuclein inhibits PI-PLC-beta2 activity through preventing the binding of its activator G alpha(q). However, the binding of gamma-synuclein to PI-PLC-beta2 does not affect its binding to G beta(gamma) subunits or small G proteins, but enhances these signals. Meanwhile, gamma-synuclein may protect PI-PLC-beta2 from protease degradation and contribute to its over-expression in breast cancer. In leukocytes, the G beta(gamma)-mediated activation of PI-PLC-beta2 can be promoted by a scaffolding protein WDR26, which is also required for the translocation of PI-PLC-beta2 from the cytosol to the membrane in polarized leukocytes. PI-PLC-beta2 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


Pssm-ID: 320039  Cd Length: 151  Bit Score: 321.06  E-value: 1.26e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  149 DKILVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEINEIFTSY 228
Cdd:cd16209     1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694958715  229 HAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16209    81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PI-PLCc_PRIP_metazoa cd08597
Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein; This ...
 311-649 1.34e-91

Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein; This family corresponds to the catalytic domain present in metazoan phospholipase C related, but catalytically inactive proteins (PRIP), which belong to a group of novel Inositol 1,4,5-trisphosphate (InsP3) binding protein. PRIP has a primary structure and domain architecture, incorporating a pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain with highly conserved X- and Y-regions split by a linker sequence, and a C-terminal C2 domain, similar to phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11)-delta isoforms. Due to replacement of critical catalytic residues, PRIP do not have PLC enzymatic activity. PRIP consists of two subfamilies, PRIP-1(previously known as p130 or PLC-1), which is predominantly expressed in the brain, and PRIP-2 (previously known as PLC-2), which exhibits a relatively ubiquitous expression. Experiments show both, PRIP-1 and PRIP-2, are involved in InsP3-mediated calcium signaling pathway and GABA(A)receptor-mediated signaling pathway. In addition, PRIP-2 acts as a negative regulator of B-cell receptor signaling and immune responses.


Pssm-ID: 176539 [Multi-domain]  Cd Length: 260  Bit Score: 295.48  E-value: 1.34e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08597     1 CQDMTQPLSHYFIASSHNTYLIEDQLRGPSSVEGYVRALQRGCRCVELDCWDG--PNGEPVIYHGHTLTSKISFRSVIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPlekfPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08597    79 INEYAFVASEYPLILCIENHC-SEKQQLVMAQYLKEIFGDKLYTEP----PNEGESYLPSPHDLKGKIIIKGKK------ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeIKKMQsdegtaglevtAYEEMSSLV 550
Cdd:cd08597   148 -------------------------------------------------------LKRRK-----------LCKELSDLV 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08597   162 SLCKSVRFQDFPTSAQNQKYWEVCSFSENLARRLANEFPEDFVNYNKKFLSRVYPSPMRVDSSNYNPQDFWNCGCQIVAM 241

                         330
                  ....*....|....*....
gi 694958715  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08597   242 NYQTPGLMMDLNTGKFLEN 260
PI-PLC1c_yeast cd08598
Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This ...
 312-646 5.41e-88

Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This family corresponds to the catalytic domain present in a group of putative phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) encoded by PLC1 genes from yeasts, which are homologs of the delta isoforms of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The prototype of this CD is protein Plc1p encoded by PLC1 genes from Saccharomyces cerevisiae. Plc1p contains both highly conserved X- and Y- regions of PLC catalytic core domain, as well as a presumptive EF-hand like calcium binding motif. Experiments show that Plc1p displays calcium dependent catalytic properties with high similarity to those of the mammalian PLCs, and plays multiple roles in modulating the membrane/protein interactions in filamentation control. CaPlc1p encoded by CAPLC1 from the closely related yeast Candida albicans, an orthologue of S. cerevisiae Plc1p, is also included in this group. Like Plc1p, CaPlc1p has conserved presumptive catalytic domain, shows PLC activity when expressed in E. coli, and is involved in multiple cellular processes. There are two other gene copies of CAPLC1 in C. albicans, CAPLC2 (also named as PIPLC) and CAPLC3. Experiments show CaPlc1p is the only enzyme in C. albicans which functions as PLC. The biological functions of CAPLC2 and CAPLC3 gene products must be clearly different from CaPlc1p, but their exact roles remain unclear. Moreover, CAPLC2 and CAPLC3 gene products are more similar to extracellular bacterial PI-PLC than to the eukaryotic PI-PLC, and they are not included in this subfamily.


Pssm-ID: 176540 [Multi-domain]  Cd Length: 231  Bit Score: 284.52  E-value: 5.41e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  312 HDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAI 391
Cdd:cd08598     2 EDLSRPLNEYFISSSHNTYLLGRQLAGDSSVEGYIRALQRGCRCVEIDVWDG--DDGEPVVTHGYTLTSSVPFRDVCRAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  392 AESAFKTSPYPIILSFENHVDsPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKpgvpLPSPEDLRGKILIKNKKNqfsgpt 471
Cdd:cd08598    80 KKYAFVTSPYPLILSLEVHCD-AEQQERMVEIMKETFGDLLVTEPLDGLEDE----LPSPEELRGKILIKVKKE------ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  472 ssskdtggeaegSSPPSApagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeemsslvn 551
Cdd:cd08598   149 ------------SKTPNH-------------------------------------------------------------- 154

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  552 yiqptkfvsfefsaqknrsyvISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVALN 631
Cdd:cd08598   155 ---------------------IFSLSERSLLKLLKDKRAALDKHNRRHLMRVYPSGTRISSSNFNPLPFWRAGVQMVALN 213

                         330
                  ....*....|....*
gi 694958715  632 FQTMDLPMQQNMAVF 646
Cdd:cd08598   214 WQTYDLGMQLNEAMF 228
PI-PLCc_gamma cd08592
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma; This family ...
 312-649 8.92e-88

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma; This family corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-gamma isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-gamma represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C2 domain.The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unique to PI-PLC-gamma, a second PH domain, two SH2 (Src homology 2) regions, and one SH3 (Src homology 3) region is present within this linker region. There are two PI-PLC-gamma isozymes (1-2). They are activated by receptor and non-receptor tyrosine kinases due to the presence of two SH2 and a single SH3 domain within the linker region. Aside from the two PI-PLC-gamma isozymes identified in mammals, some eukaryotic PI-PLC-gamma homologs have been classified with this subfamily.


Pssm-ID: 176534 [Multi-domain]  Cd Length: 229  Bit Score: 283.93  E-value: 8.92e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  312 HDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAI 391
Cdd:cd08592     2 QDMNNPLSHYWIASSHNTYLTGDQLSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPIIYHGHTLTSKIKFMDVLKTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  392 AESAFKTSPYPIILSFENHVDSPrQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKNKKnqfsgpt 471
Cdd:cd08592    80 KEHAFVTSEYPVILSIENHCSLP-QQRNMAQAFKEVFGDMLLTQPVD----RNADQLPSPNQLKRKIIIKHKK------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  472 ssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMsslvn 551
Cdd:cd08592   148 ----------------------------------------------------------------------LFYEM----- 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  552 yiqptkfvsfefsaqknrsyviSSFTELKAYDLLSKA-SVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08592   153 ----------------------SSFPETKAEKYLNRQkGKIFLKYNRRQLSRVYPKGQRVDSSNYDPVPMWNCGSQMVAL 210

                         330
                  ....*....|....*....
gi 694958715  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08592   211 NFQTPDKPMQLNQALFMLN 229
PI-PLCc_delta3 cd08630
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily ...
 311-649 3.52e-86

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-delta3 isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-delta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C-terminal C2 domain. This family corresponds to the catalytic domain which is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1,3 and 4). Unlike PI-PLC-delta 4, PI-PLC-delta1 and 3 possess a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1 and 3 from the cell nucleus.


Pssm-ID: 176567 [Multi-domain]  Cd Length: 258  Bit Score: 280.37  E-value: 3.52e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08630     1 FQDMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEG--PGGEPVIYHGHTLTSKILFRDVIQA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKpgvPLPSPEDLRGKILIKNKKNQFSgp 470
Cdd:cd08630    79 VRQHAFTASPYPVILSLENHC-GLEQQAAMARHLQTILGDMLVTQPLDSLNPE---ELPSPEELKGRVLVKGKKLQIS-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSLV 550
Cdd:cd08630   153 -------------------------------------------------------------------------PELSALA 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08630   160 VYCQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQEMWNSGCQLVAL 239

                         330
                  ....*....|....*....
gi 694958715  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08630   240 NFQTPGYEMDLNAGRFLVN 258
PI-PLCc_zeta cd08595
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta; This family ...
 311-649 4.40e-83

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta; This family corresponds to the catalytic domain presenting in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-zeta isozyme. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-zeta represents a class of sperm-specific PI-PLC that has an N-terminal EF-hand domain, a PLC catalytic core domain, and a C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There is one PLC-zeta isozyme (1). PLC-zeta plays a fundamental role in vertebrate fertilization by initiating intracellular calcium oscillations that trigger the embryo development. However, the mechanism of its activation still remains unclear. Aside from PI-PLC-zeta identified in mammals, its eukaryotic homologs have been classified with this family.


Pssm-ID: 176537 [Multi-domain]  Cd Length: 257  Bit Score: 271.81  E-value: 4.40e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKppDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08595     1 YQDMDHPLSDYFISSSHNTYLVSDQLVGPSDLDGYVSALRKGCRCLEIDCWDGA--DNEPVVYHGYTLTSKILFKEVITT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKpgvPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08595    79 VEKYAFEKSDYPVVLSLENHC-STEQQEIMAHYLVSILGEKLLRAPIDDPATG---ELPSPEALKFKILVKNKK------ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeEIKKMQSDegtaglevtayeemssLV 550
Cdd:cd08595   149 ------------------------------------------------------KIAKALSD----------------LV 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08595   159 IYTKSEKFCSFTHSRDNQHSYENNSIGENKARKLLKSSGADFVGHTQRFITRIYPKGTRASSSNYNPQEFWNVGCQMVAL 238

                         330
                  ....*....|....*....
gi 694958715  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08595   239 NFQTLGAPMDLQNGKFLDN 257
PI-PLCc_delta1 cd08629
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily ...
 311-649 2.38e-82

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-delta1 isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-delta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C-terminal C2 domain. This subfamily corresponds to the catalytic domain which is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1,3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Unlike PI-PLC-delta 4, PI-PLC-delta1 and 3 possess a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1and 3 from the cell nucleus. Experiments show PI-PLC-delta1 is essential for normal hair formation.


Pssm-ID: 176566 [Multi-domain]  Cd Length: 258  Bit Score: 269.98  E-value: 2.38e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08629     1 YQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDG--PNQEPIIYHGYTFTSKILFCDVLRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKNKKNQFSgp 470
Cdd:cd08629    79 IRDYAFKASPYPVILSLENHC-SLEQQRVMARHLRAILGPILLDQPLD----GVTTSLPSPEQLKGKILLKGKKLKLV-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSLV 550
Cdd:cd08629   152 -------------------------------------------------------------------------PELSDMI 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  551 NYIQPTKFVSFEFSAQKNRS-YVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVA 629
Cdd:cd08629   159 IYCKSVHFGGFSSPGTSGQAfYEMASFSESRALRLLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVA 238

                         330       340
                  ....*....|....*....|
gi 694958715  630 LNFQTMDLPMQQNMAVFEFN 649
Cdd:cd08629   239 LNFQTPGPEMDVYLGCFQDN 258
PI-PLCc_delta4 cd08631
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4; This subfamily ...
 311-649 3.48e-82

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-delta4 isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-delta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C-terminal C2 domain. This CD corresponds to the catalytic domain which is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1,3 and 4). Unlike PI-PLC-delta 1 and 3, a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1 and 3 from the cell nucleus, is not present in PI-PLC-delta4. Experiments show PI-PLC-delta4 is required for the acrosome reaction in fertilization.


Pssm-ID: 176568 [Multi-domain]  Cd Length: 258  Bit Score: 269.51  E-value: 3.48e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08631     1 YQDMTQPLCHYFICSSHNTYLMEDQLRGQSSVEGYIRALKRGCRCVEVDVWDG--PNGEPIVYHGHTFTSKILFKDVVAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLE-KFPlkpgVPLPSPEDLRGKILIKNKKNQFSg 469
Cdd:cd08631    79 VAQYAFQVSDYPVILSLENHC-GVEQQQTMAQHLTEILGEKLLSTTLDgVLP----TQLPSPEELRGKILLKGKKIRLS- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  470 ptssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSL 549
Cdd:cd08631   153 --------------------------------------------------------------------------PELSDC 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  550 VNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVA 629
Cdd:cd08631   159 VIYCKSVSFRSFTHSREHYHFYEISSFTETKARKLIREAGNEFVQHNTWQLSRVYPSGLRTDSSNYNPQEMWNAGCQMVA 238

                         330       340
                  ....*....|....*....|
gi 694958715  630 LNFQTMDLPMQQNMAVFEFN 649
Cdd:cd08631   239 LNFQTAGLEMDLNDGLFRQN 258
PI-PLCc_epsilon cd08596
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon; This family ...
 313-649 2.61e-80

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon; This family corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-epsilon isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-epsilon represents a class of mammalian PI-PLC that has an N-terminal CDC25 homology domain with a guanyl-nucleotide exchange factor (GFF) activity, a pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and two predicted RA (Ras association) domains that are implicated in the binding of small GTPases, such as Ras or Rap, from the Ras family. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There is one PI-PLC-epsilon isozyme (1). PI-PLC-epsilon is activated by G alpha(12/13), G beta gamma, and activated members of Ras and Rho small GTPases. Aside from PI-PLC-epsilon identified in mammals, its eukaryotic homologs have been classified with this family.


Pssm-ID: 176538 [Multi-domain]  Cd Length: 254  Bit Score: 264.02  E-value: 2.61e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  313 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKppDEEPIITHGFTMTTDIFFKEAIEAIA 392
Cdd:cd08596     3 DLQYPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLTGCRCVELDCWDGD--DGMPIIYHGHTLTTKIPFKDVVEAIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  393 ESAFKTSPYPIILSFENHVDSPrQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgpts 472
Cdd:cd08596    81 RSAFITSDYPVILSIENHCSLQ-QQRKMAEIFKTVFGEKLVTKFLFESDFSDDPSLPSPLQLKNKILLKNKK-------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  473 sskdtggeaegssppsAPagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeEMSSLVNY 552
Cdd:cd08596   152 ----------------AP------------------------------------------------------ELSDLVIY 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  553 IQPTKFVSFEFSaqknRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVALNF 632
Cdd:cd08596   162 CQAVKFPGLSTP----KCYHISSLNENAAKRLCRRYPQKLVQHTRCQLLRTYPAATRIDSSNPNPLIFWLHGLQLVALNY 237

                         330
                  ....*....|....*..
gi 694958715  633 QTMDLPMQQNMAVFEFN 649
Cdd:cd08596   238 QTDDLPMHLNAAMFEAN 254
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 314-462 2.51e-79

Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to form a single structural unit.


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 256.66  E-value: 2.51e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715   314 MTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIAE 393
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694958715   394 SAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKN 462
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLD----DDLTELPSPEDLKGKILIKG 142
PI-PLCc_eta cd08594
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta; This family ...
 311-649 1.24e-77

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta; This family corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-eta isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-eta represents a class of neuron-speific PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are two PI-PLC-eta isozymes (1-2), both neuron-specific enzymes. They function as calcium sensors that are activated by small increases in intracellular calcium concentrations. The PI-PLC-eta isozymes are also activated through GPCR stimulation. Aside from the PI-PLC-eta isozymes identified in mammals, their eukaryotic homologs are also present in this family.


Pssm-ID: 176536 [Multi-domain]  Cd Length: 227  Bit Score: 255.50  E-value: 1.24e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08594     1 NQDMTQPLSHYFIASSHNTYLTGDQLLSQSRVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKILFRDVIET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLtepLEKFPLKPGVPLPSPEDLRGKILIKNKKNQfsgp 470
Cdd:cd08594    79 INKYAFIKNEYPVILSIENHC-SVQQQKKMAQYLKEILGDKLD---LSSVISGDSKQLPSPQSLKGKILIKGKKWQ---- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeemsslv 550
Cdd:cd08594       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  551 nyiqptkfvsfefsaqknrsyvISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08594   151 ----------------------VSSFSETRAHQIVQQKAAQFLRFNQRQLSRIYPSAYRIDSSNFNPQPYWNAGCQLVAL 208

                         330
                  ....*....|....*....
gi 694958715  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08594   209 NYQTEGRMLQLNRAKFRAN 227
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 1069-1210 3.74e-77

PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of phospholipase C beta.


Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 251.91  E-value: 3.74e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1069 EQISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMT 1148
Cdd:pfam08703   35 EQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEAKKRTSDKAAQERLKKEINNSHIQEVVQSIKQLE 114

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694958715  1149 ENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAEVKESVRACLRTCFPSE 1210
Cdd:pfam08703  115 EKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAEVRESVKSCLKEGFPDE 176
PI-PLCc_eta2 cd08633
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily ...
 311-649 6.71e-76

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-eta isozyme 2. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-eta represents a class of neuron-speific PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-eta2 is a neuron-specific enzyme and expressed in the brain. It may in part function downstream of G-protein-coupled receptors and play an important role in the formation and maintenance of the neuronal network in the postnatal brain.


Pssm-ID: 176570 [Multi-domain]  Cd Length: 254  Bit Score: 251.88  E-value: 6.71e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08633     1 NQDMTQPLSHYFITSSHNTYLSGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDG--PDGEPIVHHGYTLTSKILFKDVIET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVDSPrQQAKMAEYCRTIFGDMLltePLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08633    79 INKYAFIKNEYPVILSIENHCSVP-QQKKMAQYLTEILGDKL---DLSSVISNDCTRLPSPEILKGKILVKGKK------ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMSSLV 550
Cdd:cd08633   149 -----------------------------------------------------------------------LSRALSDLV 157

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  551 NYiqpTKFVSF-EFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVA 629
Cdd:cd08633   158 KY---TKSVRVhDIETEATSSWQVSSFSETKAHQILQQKPAQYLRFNQRQLSRIYPSSYRVDSSNYNPQPFWNAGCQMVA 234

                         330       340
                  ....*....|....*....|
gi 694958715  630 LNFQTMDLPMQQNMAVFEFN 649
Cdd:cd08633   235 LNYQSEGRMLQLNRAKFSAN 254
PI-PLCc_gamma2 cd08628
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2; This subfamily ...
 313-649 1.08e-73

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-gamma isozyme 2. PI-PLC is a signaling enzyme that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-gamma represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unique to PI-PLC-gamma2, a second PH domain, two SH2 (Src homology 2) regions, and one SH3 (Src homology 3) region is present within this linker region. PI-PLC-gamma2 is highly expressed in cells of hematopoietic origin. It is activated by receptor and non-receptor tyrosine kinases due to the presence of two SH2 and a single SH3 domain within the linker region. Unlike PI-PLC-gamma1, the activation of PI-PLC-gamma2 may require concurrent stimulation of PI 3-kinase.


Pssm-ID: 176565 [Multi-domain]  Cd Length: 254  Bit Score: 245.35  E-value: 1.08e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  313 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIA 392
Cdd:cd08628     3 DMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRMGCRCIELDCWDG--PDGKPIIYHGWTRTTKIKFDDVVQAIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  393 ESAFKTSPYPIILSFENHVDSpRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKNKKnqfsgpts 472
Cdd:cd08628    81 DHAFVTSEYPVILSIEEHCSV-EQQRHMAKVFKEVFGDKLLMKPLE----ASADQLPSPTQLKEKIIIKHKK-------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  473 sskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevTAYEEMSSLVNY 552
Cdd:cd08628   148 --------------------------------------------------------------------LIAIELSDLVVY 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  553 IQPTkfvSFEFSAQKNRSYV-ISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVALN 631
Cdd:cd08628   160 CKPT---SKTKDNLENPDFKeIRSFVETKAPSIIRQKPVQLLKYNRKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALN 236

                         330
                  ....*....|....*...
gi 694958715  632 FQTMDLPMQQNMAVFEFN 649
Cdd:cd08628   237 FQTADKYMQLNHALFSLN 254
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-141 4.22e-69

PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C enzymes.


Pssm-ID: 465506  Cd Length: 131  Bit Score: 227.26  E-value: 4.22e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715    12 KVKAYLSQGERFIKWDDETTVASP-VILRVDPKGYYLYWTYQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVFNMDFP 90
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 694958715    91 DNSFLLKTLTVVSGPDMVDLTFHNFVSYKENVGKVWAEDVLALVKHPLTAN 141
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
PI-PLCc_eta1 cd08632
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily ...
 311-649 4.35e-69

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-eta isozyme 1. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-eta represents a class of neuron-speific PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-eta1 is a neuron-specific enzyme and expressed in only nerve tissues such as the brain and spinal cord. It may perform a fundamental role in the brain.


Pssm-ID: 176569 [Multi-domain]  Cd Length: 253  Bit Score: 232.61  E-value: 4.35e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08632     1 NQDMDQPLCNYFIASSHNTYLTGDQLLSQSKVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKITFRDVIET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDML-LTEPLEKFPLKpgvpLPSPEDLRGKILIKNKKnqfsg 469
Cdd:cd08632    79 INKYAFVKNEFPVILSIENHC-SIQQQKKIAQYLKEIFGDKLdLSSVLTGDPKQ----LPSPQLLKGKILVKGKK----- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  470 ptssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMSSL 549
Cdd:cd08632   149 ------------------------------------------------------------------------LCRDLSDL 156

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  550 VNYiqpTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVA 629
Cdd:cd08632   157 VVY---TNSVAAQDIVDDGSTGNVLSFSETRAHQLVQQKAEQFMTYNQKQLTRIYPSAYRIDSSNFNPLPYWNVGCQLVA 233

                         330       340
                  ....*....|....*....|
gi 694958715  630 LNFQTMDLPMQQNMAVFEFN 649
Cdd:cd08632   234 LNYQSEGRMMQLNRAKFMVN 253
PI-PLCc_gamma1 cd08627
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily ...
 313-649 3.40e-68

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-gamma isozyme 1. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-gamma represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unique to PI-PLC-gamma1, a second PH domain, two SH2 (Src homology 2) regions, and one SH3 (Src homology 3) region is present within this linker region. PI-PLC-gamma1 is ubiquitously expressed. It is activated by receptor and non-receptor tyrosine kinases due to the presence of two SH2 and a single SH3 domain within the linker region.


Pssm-ID: 176564 [Multi-domain]  Cd Length: 229  Bit Score: 228.76  E-value: 3.40e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  313 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIA 392
Cdd:cd08627     3 EMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPVIYHGHTLTTKIKFSDVLHTIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  393 ESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKNKKnqfsgpts 472
Cdd:cd08627    81 EHAFVTSEYPIILSIEDHC-SIVQQRNMAQHFKKVFGDMLLTKPVD----INADGLPSPNQLKRKILIKHKK-------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  473 sskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMsslvny 552
Cdd:cd08627   148 ---------------------------------------------------------------------LYRDM------ 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  553 iqptkfvsfefsaqknrsyviSSFTELKAYDLLSKAS-VQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVALN 631
Cdd:cd08627   153 ---------------------SSFPETKAEKYVNRSKgKKFLQYNRRQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALN 211

                         330
                  ....*....|....*...
gi 694958715  632 FQTMDLPMQQNMAVFEFN 649
Cdd:cd08627   212 FQTPDKPMQMNQALFMLG 229
EFh_PI-PLCbeta cd16200
EF-hand motif found in metazoan phosphoinositide-specific phospholipase C (PI-PLC)-beta ...
 149-299 7.27e-66

EF-hand motif found in metazoan phosphoinositide-specific phospholipase C (PI-PLC)-beta isozymes; PI-PLC-beta isozymes represent a class of metazoan PI-PLCs that hydrolyze the membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2) to propagate diverse intracellular responses that underlie the physiological action of many hormones, neurotransmitters, and growth factors (EC 3.1.4.11). They have been implicated in numerous processes relevant to central nervous system (CNS), including chemotaxis, cardiovascular function, neuronal signaling, and opioid sensitivity. Like other PI-PLC isozymes, PI-PLC-beta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, they have a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are four PI-PLC-beta isozymes (1-4). PI-PLC-beta1 and PI-PLC-beta3 are expressed in a wide range of tissues and cell types, whereas PI-PLC-beta2 and PI-PLC-beta4 have been found only in hematopoietic and neuronal tissues, respectively. All PI-PLC-beta isozymes are activated by the heterotrimeric G protein alpha subunits of the Gq class through their C2 domain and long C-terminal extension. They are GTPase-activating proteins (GAPs) for these G alpha(q) proteins. PI-PLC-beta2 and PI-PLC-beta3 can also be activated by beta-gamma subunits of the G alpha(i/o) family of heterotrimeric G proteins and the small GTPases such as Rac and Cdc42. This family also includes two invertebrate homologs of PI-PLC-beta, PLC21 from cephalopod retina and No receptor potential A protein (NorpA) from Drosophila melanogaster.


Pssm-ID: 320030 [Multi-domain]  Cd Length: 153  Bit Score: 219.04  E-value: 7.27e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  149 DKILVKLKMQLNSEGKIPVKNFFQMFPAD--RKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEINEIFT 226
Cdd:cd16200     1 KKLYTKLKLSVNITGKIPVKNIIKCFSSDkkRKRVLKALKALGLPDGKNDEIDPEDFTFEKFFKLYNKLCPRPDIDEIFK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694958715  227 SYHAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16200    81 ELGGKRKPYLTLEQLVDFLNEEQRDPRLNEILFPFHTKEQAKKLIDKYEPNEKNKKKGQLTLEGFLRYLMSDE 153
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 314-463 6.79e-65

Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. These enzymes contain 2 regions (X and Y) which together form a TIM barrel-like structure containing the active site residues. Phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The bacterial enzyme appears to be a homologue of the mammalian PLCs.


Pssm-ID: 197543 [Multi-domain]  Cd Length: 143  Bit Score: 215.99  E-value: 6.79e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715    314 MTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIAE 393
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDG--PDGEPVIYHGHTFTLPIKLSEVLEAIKD 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715    394 SAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKpgvpLPSPEDLRGKILIKNK 463
Cdd:smart00148   79 FAFVTSPYPVILSLENHC-SPDQQAKMAQMFKEIFGDMLYTPPLTSSLEV----LPSPEQLRGKILLKVR 143
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 547-661 6.52e-63

Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. These enzymes contain 2 regions (X and Y) which together form a TIM barrel-like structure containing the active site residues. Phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The bacterial enzyme appears to be a homologue of the mammalian PLCs.


Pssm-ID: 128454 [Multi-domain]  Cd Length: 115  Bit Score: 209.02  E-value: 6.52e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715    547 SSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQ 626
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 694958715    627 MVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFM 661
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
PI-PLCc_plant cd08599
Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family ...
 311-649 5.59e-60

Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family corresponds to the catalytic domain present in a group of phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11) encoded by PLC genes from higher plants, which are homologs of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The domain arrangement of plant PI-PLCs is structurally similar to the mammalian PLC-zeta isoform, which lacks the N-terminal pleckstrin homology (PH) domain, but contains EF-hand like motifs (which are absent in a few plant PLCs), a PLC catalytic core domain with X- and Y- highly conserved regions split by a linker sequence, and a C2 domain. However, at the sequence level, the plant PI-PLCs are closely related to the mammalian PLC-delta isoform. Experiments show that plant PLCs display calcium dependent PLC catalytic properties, although they lack some of the N-terminal motifs found in their mammalian counterparts. A putative calcium binding site may be located at the region spanning the X- and Y- domains.


Pssm-ID: 176541 [Multi-domain]  Cd Length: 228  Bit Score: 205.30  E-value: 5.59e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDeePIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08599     1 HHDMTAPLSHYFIFSSHNSYLTGNQLSSRSSTAPIIEALLRGCRVIELDLWPGGRGD--ICVLHGGTLTKPVKFEDCIKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPlekfPLKPGVPLPSPEDLRGKILIKNKknqfsgp 470
Cdd:cd08599    79 IKENAFTASEYPVIITLENHL-SPELQAKAAQILRETLGDKLFYPD----SEDLPEEFPSPEELKGKILISDK------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  471 tssskdtggeaegssPPsapagegtvwageegteleeeeveeeeeEESGNLDEEEIKKMQSDEGTAGLevtayeemsslv 550
Cdd:cd08599   147 ---------------PP----------------------------VIRNSLSETQLKKVIEGEHPTDL------------ 171

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  551 nyiqptkfvsfefsaqknrsyvissftelkaydllskasvqfVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08599   172 ------------------------------------------IEFTQKNLLRVYPAGLRITSSNYDPMLAWMHGAQMVAL 209

                         330
                  ....*....|....*....
gi 694958715  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08599   210 NMQGYDRPLWLNRGKFRAN 228
EFh_PI-PLCbeta1 cd16208
EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1); PI-PLC-beta1, ...
 149-299 3.67e-59

EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1); PI-PLC-beta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1, or PLC-154, or phospholipase C-I (PLC-I), or phospholipase C-beta-1 (PLC-beta1), is expressed at highest levels in specific regions of the brain, as well as in the cardiovascular system. It has two splice variants, PI-PLC-beta1a and PI-PLC-beta1b, both of which are present within the nucleus. Nuclear PI-PLC-beta1 is a key molecule for nuclear inositide signaling, where it plays a role in cell cycle progression, proliferation and differentiation. It also contributes to generate cell-specific Ca2+ signals evoked by G protein-coupled receptor stimulation. PI-PLC-beta1 acts as an effector and a GTPase activating protein (GAP) specifically activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It regulates neuronal activity in the cerebral cortex and hippocampus, and has been implicated for participations in diverse critical functions related to forebrain diseases such as schizophrenia. It may play an important role in maintenance of the status epilepticus, and in osteosarcoma-related signal transduction pathways. PI-PLC-beta1 also functions as a regulator of erythropoiesis in kinamycin F, a potent inducer of gamma-globin production in K562 cells. The G protein activation and the degradation of PI-PLC-beta1 can be regulated by the interaction of alpha-synuclein. As a result, it may reduce cell damage under oxidative stress. Moreover, PI-PLC-beta1 works as a new intermediate in the HIV-1 gp120-triggered phosphatidylcholine-specific phospholipase C (PC-PLC)-driven signal transduction pathway leading to cytoplasmic CCL2 secretion in macrophages. PI-PLC-beta1 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


Pssm-ID: 320038  Cd Length: 151  Bit Score: 200.10  E-value: 3.67e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  149 DKILVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEINEIFTSY 228
Cdd:cd16208     1 EKAYTKLKLQVNPEGRIPVKNIYRLFSADRKRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDHIFSEF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694958715  229 HAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16208    81 GAKSKPYLSVDQMTEFINSKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSTLAKKGQISVDGFMRYLSGEE 151
PLN02228 PLN02228
Phosphoinositide phospholipase C
 217-786 3.30e-58

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 211.43  E-value: 3.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  217 PRPEINEIFTSYHAKAKpyMTKEHLTKFINQKQRDSRlnsllfppARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLC 296
Cdd:PLN02228   22 PPVSIKRLFEAYSRNGK--MSFDELLRFVSEVQGERH--------AGLDYVQDIFHSVKHHNVFHHHGLVHLNAFYRYLF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  297 GPENSVLAQDKLLlHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKgKPPDEEPIITHGF 376
Cdd:PLN02228   92 SDTNSPLPMSGQV-HHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWP-NPSGNAAEVRHGR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  377 TMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLL---TEPLEKFplkpgvplPSPED 453
Cdd:PLN02228  170 TLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHL-PPNLQAQVAKMLTKTFRGMLFrctSESTKHF--------PSPEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  454 LRGKILIKNKKNQFSGPTSSSKDTggeaegssppSAPAGEGTVWAGEEGTeleeeeveeeeeeesgnldEEEIKKMQSDE 533
Cdd:PLN02228  241 LKNKILISTKPPKEYLESKTVQTT----------RTPTVKETSWKRVADA-------------------ENKILEEYKDE 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  534 GTAGLEvtaYEEMSSL--VNYIQPTKFVsfeFSAQKNRSYVIsSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMD 611
Cdd:PLN02228  292 ESEAVG---YRDLIAIhaANCKDPLKDC---LSDDPEKPIRV-SMDEQWLETMVRTRGTDLVRFTQRNLVRIYPKGTRVD 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  612 SSNYMPQMFWNAGCQMVALNFQT--MDLPMQQNMavFEFNGQSGYLLKHEFMRRPDKQFNPFSvdriDVVVATTLSITVI 689
Cdd:PLN02228  365 SSNYDPHVGWTHGAQMVAFNMQGhgKQLWIMQGM--FRANGGCGYVKKPRILLDEHTLFDPCK----RLPIKTTLKVKIY 438

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  690 SGQ----------FLSERSVRTYVEVELFGLPGDPKrRYRTKLspSTNSINPVWKEEPFVFEkILMPELASLRVAVME-- 757
Cdd:PLN02228  439 TGEgwdldfhlthFDQYSPPDFFVKIGIAGVPRDTV-SYRTET--AVDQWFPIWGNDEFLFQ-LRVPELALLWFKVQDyd 514

                         570       580       590
                  ....*....|....*....|....*....|.
gi 694958715  758 --EGNKFLGHRIIPINALNSGYHHLCLHSES 786
Cdd:PLN02228  515 ndTQNDFAGQTCLPLPELKSGVRAVRLHDRA 545
PLN02952 PLN02952
phosphoinositide phospholipase C
 310-783 3.39e-58

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 212.17  E-value: 3.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  310 LHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDeEPIITHGFTMTTDIFFKEAIE 389
Cdd:PLN02952  121 VHHDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGSTKD-EILVLHGRTLTTPVPLIKCLK 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  390 AIAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLteplekFPLKPG-VPLPSPEDLRGKILIKNKKnqfs 468
Cdd:PLN02952  200 SIRDYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLY------YPESDSlVQFPSPESLKHRIIISTKP---- 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  469 gPTSSSKDTGGEAEGSSPPSAPAGEGTvwageegteLEEEEVEEEEEEESGNLD-EEEIKKMQSDEGTAGLEVTAYEEMS 547
Cdd:PLN02952  269 -PKEYLESSGPIVIKKKNNVSPSGRNS---------SEETEEAQTLESMLFEQEaDSRSDSDQDDNKSGELQKPAYKRLI 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  548 SlVNYIQPTKFV--SFEFSAQKNRSYvisSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGC 625
Cdd:PLN02952  339 T-IHAGKPKGTLkdAMKVAVDKVRRL---SLSEQELEKAATTNGQDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGA 414

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  626 QMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFM--RRPDKQ-FNPfsvdRIDVVVATTLSITVISG----------Q 692
Cdd:PLN02952  415 QMIAFNMQGYGKSLWLMHGMFRANGGCGYLKKPDFLmkKGFHDEvFDP----KKKLPVKKTLKVKVYLGdgwrldfshtH 490

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  693 FLSERSVRTYVEVELFGLPGDPKRRyRTKLspSTNSINPVWKEEpFVFeKILMPELASLRVAV----MEEGNKFLGHRII 768
Cdd:PLN02952  491 FDSYSPPDFYTKMYIVGVPADNAKK-KTKI--IEDNWYPAWNEE-FSF-PLTVPELALLRIEVreydMSEKDDFGGQTCL 565

                         490
                  ....*....|....*
gi 694958715  769 PINALNSGYHHLCLH 783
Cdd:PLN02952  566 PVSELRPGIRSVPLH 580
PLN02222 PLN02222
phosphoinositide phospholipase C 2
 219-800 4.64e-58

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 211.43  E-value: 4.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  219 PEINEIFTSYHAKAkpYMTKEHLTKFINQKQRDSRlnsllfppARPDQVQGLIDKyepSGINAQRGQLSPEGMVWFLCGP 298
Cdd:PLN02222   25 REIKTIFEKYSENG--VMTVDHLHRFLIDVQKQDK--------ATREDAQSIINS---ASSLLHRNGLHLDAFFKYLFGD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  299 ENSVLAQDKLllHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIItHGFTM 378
Cdd:PLN02222   92 NNPPLALHEV--HHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSDKDDIDVL-HGMTL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  379 TTDIFFKEAIEAIAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEP----LEKFPlkpgvplpSPEDL 454
Cdd:PLN02222  169 TTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHL-TPDLQSKVAEMVTEIFGEILFTPPvgesLKEFP--------SPNSL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  455 RGKILIKNKknqfsgPTSSSKDtgGEAEGSSPPSAPAGEGTVWaGEEGTELEEEEVEEEEEEESGNLDEEEikkmqsDEG 534
Cdd:PLN02222  240 KKRIIISTK------PPKEYKE--GKDDEVVQKGKDLGDEEVW-GREVPSFIQRNKSVDKNDSNGDDDDDD------DDG 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  535 TAGLEVTAYEEMSSLV--NYIQPTKFVS--FEFSAQKNRSYVISSFTELKAYDLLSKasvQFVDYNKRQMSRIYPKGTRM 610
Cdd:PLN02222  305 EDKSKKNAPPQYKHLIaiHAGKPKGGITecLKVDPDKVRRLSLSEEQLEKAAEKYAK---QIVRFTQHNLLRIYPKGTRV 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  611 DSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFMRRPDKQFNPFSvDRIDVVVATTLSITVIS 690
Cdd:PLN02222  382 TSSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKKPDLLLKSGSDSDIFD-PKATLPVKTTLRVTIYM 460

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  691 GQ----------FLSERSVRTYVEVELFGLPGDPKRRyRTKlSPSTNSInPVWKEepfVFE-KILMPELASLRVAV---- 755
Cdd:PLN02222  461 GEgwyfdfrhthFDQYSPPDFYTRVGIAGVPGDTVMK-KTK-TLEDNWI-PAWDE---VFEfPLTVPELALLRLEVheyd 534

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 694958715  756 MEEGNKFLGHRIIPINALNSGYHHLCLHSESNMPLTMPALFIFLE 800
Cdd:PLN02222  535 MSEKDDFGGQTCLPVWELSQGIRAFPLHSRKGEKYKSVKLLVKVE 579
PI-PLC-Y pfam00387
Phosphatidylinositol-specific phospholipase C, Y domain; This associates with pfam00388 to ...
 546-660 1.37e-56

Phosphatidylinositol-specific phospholipase C, Y domain; This associates with pfam00388 to form a single structural unit.


Pssm-ID: 459794  Cd Length: 114  Bit Score: 191.14  E-value: 1.37e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715   546 MSSLVNYIQPTKFVSFEfSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGC 625
Cdd:pfam00387    1 LSDLVVYTQSVKFKSFS-TPESKTPNHIFSFSESKALKLIKSSSAAFVKHNRRHLMRVYPKGTRVDSSNFNPQPFWNCGV 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 694958715   626 QMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEF 660
Cdd:pfam00387   80 QMVALNWQTPDEGMQLNEGMFADNGGCGYVLKPEF 114
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-144 4.73e-56

Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is regulated by heterotrimeric G protein-coupled receptors through their C2 domain and long C-terminal extension which forms an autoinhibitory helix. There are four isoforms: PLC-beta1-4. The PH domain of PLC-beta2 and PLC-beta3 plays a dual role, much like PLC-delta1, by binding to the plasma membrane, as well as the interaction site for the catalytic activator. However, PLC-beta binds to the lipid surface independent of PIP2. PLC-beta1 seems to play unspecified roles in cellular proliferation and differentiation. PLC-beta consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves, a C2 domain and a C-terminal PDZ. Members of the Rho GTPase family (e.g., Rac1, Rac2, Rac3, and cdc42) have been implicated in their activation by binding to an alternate site on the N-terminal PH domain. A basic amino acid region within the enzyme's long C-terminal tail appears to function as a Nuclear Localization Signal for import into the nucleus. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). 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.the plasma membrane, but only a few (less than 10%) display strong specificity in binding inositol phosphates. 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 kinases, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, cytoskeletal associated molecules, and in lipid associated enzymes.


Pssm-ID: 270167  Cd Length: 127  Bit Score: 190.09  E-value: 4.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715   17 LSQGERFIKWDDETTVASPVILRVDPKGYYLYWTYQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVfNMDFPDNSFLL 96
Cdd:cd13361     1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 694958715   97 KTLTVVSGPDMVDLTFHNFVSYKENVGKVWAEDVLALVKHPLTANASR 144
Cdd:cd13361    80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
EFh_PI-PLCbeta3 cd16210
EF-hand motif found in phosphoinositide phospholipase C beta 3 (PI-PLC-beta3); PI-PLC-beta3, ...
 150-299 2.71e-50

EF-hand motif found in phosphoinositide phospholipase C beta 3 (PI-PLC-beta3); PI-PLC-beta3, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3, or phospholipase C-beta-3 (PLC-beta3), is widely expressed at highest levels in brain, liver, and parotid gland. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins. PI-PLC-beta3 associates with CXC chemokine receptor 2 (CXCR2) and Na+/H+ exchanger regulatory factor-1 (NHERF1) to form macromolecular complexes at the plasma membrane of pancreatic cancer cells, which functionally couple chemokine signaling to PI-PLC-beta3-mediated signaling cascade. Moreover, PI-PLC-beta3 directly interacts with the M3 muscarinic receptor (M3R), a prototypical G alpha-q-coupled receptor that promotes PI-PLC-beta3 localization to the plasma membrane. This binding can alter G alpha-q-dependent PLC activation. Furthermore, PI-PLC-beta3 inhibits the proliferation of hematopoietic stem cells (HSCs) and myeloid cells through the interaction of SH2-domain-containing protein phosphatase 1 (SHP-1) and signal transducer and activator of transcription 5 (Stat5), and the augment of the dephosphorylating activity of SHP-1 toward Stat5, leading to the inactivation of Stat5. It is also involved in atopic dermatitis (AD) pathogenesis via regulating the expression of periostin in fibroblasts and thymic stromal lymphopoietin (TSLP) in keratinocytes. In addition, PI-PLC-beta3 mediates the thrombin-induced Ca2+ response in glial cells. PI-PLC-beta3 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


Pssm-ID: 320040  Cd Length: 151  Bit Score: 174.72  E-value: 2.71e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  150 KILVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEINEIFTSYH 229
Cdd:cd16210     2 KAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILLEIG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  230 AKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16210    82 AKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQVRQLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 151
PLN02230 PLN02230
phosphoinositide phospholipase C 4
 217-800 3.53e-49

phosphoinositide phospholipase C 4


Pssm-ID: 177875 [Multi-domain]  Cd Length: 598  Bit Score: 185.29  E-value: 3.53e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  217 PRPEINEIFTSYhAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQV---QGLIDKYepsginaQRGQLSPEGMVW 293
Cdd:PLN02230   27 PVADVRDLFEKY-ADGDAHMSPEQLQKLMAEEGGGEGETSLEEAERIVDEVlrrKHHIAKF-------TRRNLTLDDFNY 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  294 FLCGPENSVLAQDKLllHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDeePIIT 373
Cdd:PLN02230   99 YLFSTDLNPPIADQV--HQNMDAPLSHYFIFTGHNSYLTGNQLSSNCSELPIADALRRGVRVVELDLWPRGTDD--VCVK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  374 HGFTMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLL---TEPLEKFPlkpgvplpS 450
Cdd:PLN02230  175 HGRTLTKEVKLGKCLDSIKANAFAISKYPVIITLEDHL-TPKLQFKVAKMITQTFGDMLYyhdSEGCQEFP--------S 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  451 PEDLRGKILIKNK--KNQFSGPTSSSKDTGGEAEGSsppsapagEGTVWAGEEGTELEEEEVEEEEEEESGNL--DEEEI 526
Cdd:PLN02230  246 PEELKEKILISTKppKEYLEANDAKEKDNGEKGKDS--------DEDVWGKEPEDLISTQSDLDKVTSSVNDLnqDDEER 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  527 KKMQSDEgTAGLEVTAYEEMSSlVNYIQPTKFVSFEFSAQKNRSYVISSftelkAYDLLSKASVQF----VDYNKRQMSR 602
Cdd:PLN02230  318 GSCESDT-SCQLQAPEYKRLIA-IHAGKPKGGLRMALKVDPNKIRRLSL-----SEQLLEKAVASYgadvIRFTQKNFLR 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  603 IYPKGTRMDSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFMRRPDKQFNPFsVDRIDVVVAT 682
Cdd:PLN02230  391 IYPKGTRFNSSNYKPQIGWMSGAQMIAFNMQGYGRALWLMEGMFRANGGCGYVKKPDFLMDAGPNGQDF-YPKDNSCPKK 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  683 TLSITVISGQF----LSERSVRTYVEVELF---GLPGDPKRRYRTKLSPSTNSINPVWKEEpFVFeKILMPELASLRVAV 755
Cdd:PLN02230  470 TLKVKVCMGDGwlldFKKTHFDSYSPPDFFvrvGIAGAPVDEVMEKTKIEYDTWTPIWNKE-FIF-PLAVPELALLRVEV 547

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 694958715  756 ME----EGNKFLGHRIIPINALNSGYHHLCLHSESNMPLTMPALFIFLE 800
Cdd:PLN02230  548 HEhdinEKDDFGGQTCLPVSEIRQGIHAVPLFNRKGVKYSSTRLLMRFE 596
EFh_PI-PLC21 cd16213
EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family ...
 150-295 2.00e-48

EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family includes invertebrate homologs of phosphoinositide phospholipase C beta (PI-PLC-beta) named PLC21 from cephalopod retina. It also includes PLC21 encoded by plc-21 gene, which is expressed in the central nervous system of Drosophila. Like beta-class of vertebrate PI-PLCs, PLC21 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


Pssm-ID: 320043  Cd Length: 154  Bit Score: 169.40  E-value: 2.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  150 KILVKLKMQLNSEGKIPVKNFFQMFPA---DRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEINEIFT 226
Cdd:cd16213     2 KAYTKLTLQTDKEGKIPVKNIVKMFAQhkdDRKRVEKALEAIGLPSGKNDAIDPKKFTFEDFFNFYRRLTGRQEVEKIFD 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694958715  227 SYHAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFL 295
Cdd:cd16213    82 ELGAKKKPYLTTEQFVDFLNKTQRDPRLNEILYPYANPKRARDLINQYEPNKSFAKKGHLSVEGFLRYL 150
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 681-802 9.43e-38

C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) to d-myo-inositol-1,4,5-trisphosphate (1,4,5-IP3) and sn-1,2-diacylglycerol (DAG). 1,4,5-IP3 and DAG are second messengers in eukaryotic signal transduction cascades. PLC is composed of a N-terminal PH domain followed by a series of EF hands, a catalytic TIM barrel and a C-terminal C2 domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology.


Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 137.67  E-value: 9.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  681 ATTLSITVISGQFLS------ERSVRTYVEVELFGLPGDPKRRYRTKLSPStNSINPVWkEEPFVFEKIlMPELASLRVA 754
Cdd:cd00275     1 PLTLTIKIISGQQLPkpkgdkGSIVDPYVEVEIHGLPADDSAKFKTKVVKN-NGFNPVW-NETFEFDVT-VPELAFLRFV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 694958715  755 VMEE---GNKFLGHRIIPINALNSGYHHLCLHSESNMPLTMPALFIFLEMK 802
Cdd:cd00275    78 VYDEdsgDDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
 154-295 1.72e-28

EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4, or phospholipase C-beta-4 (PLC-beta4), is expressed in high concentrations in cerebellar Purkinje and granule cells, the median geniculate body, and the lateral geniculate nucleus. It may play a critical role in linking anxiety behaviors and theta rhythm heterogeneity. PI-PLC-beta4 is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It contributes to generate cell-specific Ca2+ signals evoked by G protein-coupled receptor stimulation. PI-PLC-beta4 functions as a downstream signaling molecule of type 1 metabotropic glutamate receptors (mGluR1s). The thalamic mGluR1-PI-PLC-beta4 cascade is essential for formalin-induced inflammatory pain by regulating the response of ventral posterolateral thalamic nucleus (VPL) neurons. Moreover, PI-PLC-beta4 is essential for long-term depression (LTD) in the rostral cerebellum, which may be required for the acquisition of the conditioned eyeblink response. Besides, PI-PLC-beta4 may play an important role in maintenance of the status epilepticus. The mutations of PI-PLC-beta4 has been identified as the major cause of autosomal dominant auriculocondylar syndrome (ACS). PI-PLC-beta4 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


Pssm-ID: 320041  Cd Length: 153  Bit Score: 112.13  E-value: 1.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  154 KLKMQLNSEGKIPVKNFFQMFPADR--KRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEINEIFTSYHAK 231
Cdd:cd16211     6 RLCFLVNPNGKIPVRSITRTFASGKteKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFKKINGD 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694958715  232 AKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFL 295
Cdd:cd16211    86 KKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYL 149
PLN02223 PLN02223
phosphoinositide phospholipase C
 311-791 9.60e-27

phosphoinositide phospholipase C


Pssm-ID: 165867 [Multi-domain]  Cd Length: 537  Bit Score: 116.28  E-value: 9.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  311 HHDMTQPLNHYFINSSHNTYLTAGQ-FSGLSSAEMYRQVLLSGCRCVELDCWkgkPPDEEPI-ITHGFTMTTDIFFKEAI 388
Cdd:PLN02223  105 HHDMHAPLSHYFIHTSLKSYFTGNNvFGKLYSIEPIIDALEQGVRVVELDLL---PDGKDGIcVRPKWNFEKPLELQECL 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  389 EAIAESAF-KTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTE----PLEKFplkpgvplPSPEDLRGKILIKNK 463
Cdd:PLN02223  182 DAIKEHAFtKCRSYPLIITFKDGL-KPDLQSKATQMIDQTFGDMVYHEdpqhSLEEF--------PSPAELQNKILISRR 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  464 knqfsgptssskdtggeaegssPPS----APAGEGTVwageegteleeeeveeeeeeesGNLDEEEIKKMQSDEGtagle 539
Cdd:PLN02223  253 ----------------------PPKellyAKADDGGV----------------------GVRNELEIQEGPADKN----- 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  540 vtaYEEMSSLvNYIQPTKFVSFEFSAQKNRSYVISSFTElkayDLLSKASVQFVDYN-KRQMSRIYPKgtrmdssnYMPQ 618
Cdd:PLN02223  284 ---YQSLVGF-HAVEPRGMLQKALTGKADDIQQPGWYER----DIISFTQKKFLRTRpKKKNLLINAP--------YKPQ 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  619 MFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFMRR--PDKQFNPfsvdRIDVVVATTLSITVISGQF--- 693
Cdd:PLN02223  348 RAWMHGAQLIALSRKDDKEKLWLMQGMFRANGGCGYVKKPDFLLNagPSGVFYP----TENPVVVKILKVKIYMGDGwiv 423

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  694 -LSERSVR-----TYVEVELFGLPGDPKrryRTKLSPSTNSINPVWKEEpFVFeKILMPELASLRVAV----MEEGNKFL 763
Cdd:PLN02223  424 dFKKRIGRlskpdLYVRISIAGVPHDEK---IMKTTVKNNEWKPTWGEE-FTF-PLTYPDLALISFEVydyeVSTADAFC 498

                         490       500       510
                  ....*....|....*....|....*....|....
gi 694958715  764 GHRIIPINALNSGYHHLCLHSE------SNMPLT 791
Cdd:PLN02223  499 GQTCLPVSELIEGIRAVPLYDErgkacsSTMLLT 532
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 324-632 2.13e-26

Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases superfamily; The PI-PLC-like phosphodiesterases superfamily represents the catalytic domains of bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11), glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.41) from spider venom, SMases D-like proteins, and phospholipase D (PLD) from several pathogenic bacteria, as well as their uncharacterized homologs found in organisms ranging from bacteria and archaea to metazoans, plants, and fungi. PI-PLCs are ubiquitous enzymes hydrolyzing the membrane lipid phosphoinositides to yield two important second messengers, inositol phosphates and diacylglycerol (DAG). GP-GDEs play essential roles in glycerol metabolism and catalyze the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols that are major sources of carbon and phosphate. Both, PI-PLCs and GP-GDEs, can hydrolyze the 3'-5' phosphodiester bonds in different substrates, and utilize a similar mechanism of general base and acid catalysis with conserved histidine residues, which consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This superfamily also includes Neurospora crassa ankyrin repeat protein NUC-2 and its Saccharomyces cerevisiae counterpart, Phosphate system positive regulatory protein PHO81, glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs). The residues essential for enzyme activities and metal binding are not conserved in these sequence homologs, which might suggest that the function of catalytic domains in these proteins might be distinct from those in typical PLC-like phosphodiesterases.


Pssm-ID: 176498 [Multi-domain]  Cd Length: 179  Bit Score: 107.14  E-value: 2.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  324 NSSHNTYLTAGQfsgLSSAEMYRQVLLSGCRCVELDCWKGKppDEEPIITHGFTMT------TDIFFKEAIEAIAESAFk 397
Cdd:cd08555     1 VLSHRGYSQNGQ---ENTLEAFYRALDAGARGLELDVRLTK--DGELVVYHGPTLDrttagiLPPTLEEVLELIADYLK- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  398 TSPYPIILSFENHVDS---PRQQAKMAEYCRTIFGDmllteplekfplkpgvplpspeDLRGKILIKnkknqfsgptsss 474
Cdd:cd08555    75 NPDYTIILSLEIKQDSpeyDEFLAKVLKELRVYFDY----------------------DLRGKVVLS------------- 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  475 kdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeemsslvnyiq 554
Cdd:cd08555       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694958715  555 ptkfvsfefsaqknrSYVISSFTELKAYDLLSKASVQFVDYNK-RQMSRIYPKGTrmdsSNYMPQMFWNAGCQMVALNF 632
Cdd:cd08555   120 ---------------SFNALGVDYYNFSSKLIKDTELIASANKlGLLSRIWTVND----NNEIINKFLNLGVDGLITDF 179
EFh_NorpA_like cd16212
EF-hand motif found in Drosophila melanogaster No receptor potential A protein (NorpA) and ...
 153-299 2.15e-23

EF-hand motif found in Drosophila melanogaster No receptor potential A protein (NorpA) and similar proteins; NorpA, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase, is an eye-specific phosphoinositide phospholipase C (PI-PLC) encoded by norpA gene in Drosophila. It is expressed predominantly in photoreceptors and plays an essential role in the phototransduction pathway of Drosophila. A mutation within the norpA gene can render the fly blind without affecting any of the obvious structures of the eye. Like beta-class of vertebrate PI-PLCs, NorpA contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


Pssm-ID: 320042 [Multi-domain]  Cd Length: 153  Bit Score: 97.62  E-value: 2.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  153 VKLKMQLNSEGKIPVKNFFQMFPADR--KRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEINEIFTSYHA 230
Cdd:cd16212     5 MRLGFMVDSGGKIPVKHIARTFASGKteKLVYQCLAEMGLPSGKGDSIEKEDFTFEKFYALYHKICPRNDIEELFTSITK 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694958715  231 KAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16212    85 GKGEHISLAQLINFMNDKQRDPRLNEILYPLYDEKRCTEIIKAYEQNEENIKNKRMSKDGFIRYLMSDE 153
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 683-779 7.43e-14

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: 68.67  E-value: 7.43e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715    683 TLSITVISGQFLSER----SVRTYVEVELFGlpgDPKRRYRTKLSPSTNsiNPVWKEEpFVFEkILMPELASLRVAVMEE 758
Cdd:smart00239    1 TLTVKIISARNLPPKdkggKSDPYVKVSLDG---DPKEKKKTKVVKNTL--NPVWNET-FEFE-VPPPELAELEIEVYDK 73

                            90       100
                    ....*....|....*....|....*
gi 694958715    759 ----GNKFLGHRIIPINALNSGYHH 779
Cdd:smart00239   74 drfgRDDFIGQVTIPLSDLLLGGRH 98
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 195-299 1.01e-12

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 66.48  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  195 NDAINPEDFPEpvyksFLMSLCPRPEINEIFTSYhAKAKPYMTKEHLTKFINQKQRdsrlnsllFPPARPDQVQGLIDKY 274
Cdd:cd16202    50 EDVLDEEEFVQ-----FYNRLTKRPEIEELFKKY-SGDDEALTVEELRRFLQEEQK--------VKDVTLEWAEQLIETY 115

                          90       100
                  ....*....|....*....|....*
gi 694958715  275 EPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16202   116 EPSEDLKAQGLMSLDGFTLFLLSPD 140
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 155-299 5.72e-12

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 64.23  E-value: 5.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  155 LKMQLNSEGKIPVKNFFQM-----FPADRKRVEAALSACHlpKGKNDAINPEDFpepvyKSFLMSLCPRPEINEIFTSYH 229
Cdd:cd15898     7 IKADKDGDGKLSLKEIKKLlkrlnIRVSEKELKKLFKEVD--TNGDGTLTFDEF-----EELYKSLTERPELEPIFKKYA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  230 AKAKPYMTKEHLTKFINQKQRDSRlnsllfppaRPDQVQGLIDKYEPSGinaQRGQLSPEGMVWFLCGPE 299
Cdd:cd15898    80 GTNRDYMTLEEFIRFLREEQGENV---------SEEECEELIEKYEPER---ENRQLSFEGFTNFLLSPE 137
C2 pfam00168
C2 domain;
683-776 3.34e-10

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 58.48  E-value: 3.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715   683 TLSITVISGQFL----SERSVRTYVEVELfglpGDPKRRYRTKLSPstNSINPVWKEEpFVFEkILMPELASLRVAVMEE 758
Cdd:pfam00168    2 RLTVTVIEAKNLppkdGNGTSDPYVKVYL----LDGKQKKKTKVVK--NTLNPVWNET-FTFS-VPDPENAVLEIEVYDY 73

                           90       100
                   ....*....|....*....|..
gi 694958715   759 ----GNKFLGHRIIPINALNSG 776
Cdd:pfam00168   74 drfgRDDFIGEVRIPLSELDSG 95
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 215-303 3.01e-08

Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are predominantly found in phosphoinositide-specific phospholipase C. They adopt a structure consisting of a core of four alpha helices, in an EF like fold, and are required for functioning of the enzyme.


Pssm-ID: 401279 [Multi-domain]  Cd Length: 85  Bit Score: 52.25  E-value: 3.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715   215 LCPRPEINEIFTSYhAKAKPYMTKEHLTKFINQKQRDSRlnsllfppARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWF 294
Cdd:pfam09279    5 LTQREEIDEIFQEY-SGDGQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAMTKDGFLMY 75


                   ....*....
gi 694958715   295 LCGPENSVL 303
Cdd:pfam09279   76 LCSPDGSIF 84
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 684-773 7.69e-07

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 48.60  E-value: 7.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  684 LSITVISGQFL----SERSVRTYVEVELfglpgDPKRRYRTKLSPstNSINPVWKEEpFVFEkILMPELASLRVAVMEE- 758
Cdd:cd00030     1 LRVTVIEARNLpakdLNGKSDPYVKVSL-----GGKQKFKTKVVK--NTLNPVWNET-FEFP-VLDPESDTLTVEVWDKd 71

                          90
                  ....*....|....*...
gi 694958715  759 ---GNKFLGHRIIPINAL 773
Cdd:cd00030    72 rfsKDDFLGEVEIPLSEL 89
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
 209-299 1.88e-06

EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 (PLCD1), or phospholipase C-III (PLC-III), or phospholipase C-delta-1 (PLC-delta-1), is present in high abundancy in the brain, heart, lung, skeletal muscle and testis. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. PI-PLC-delta1 is required for maintenance of homeostasis in skin and metabolic tissues. Moreover, it is essential in trophoblasts for placental development. Simultaneous loss of PI-PLC-delta1 may cause placental vascular defects, leading to embryonic lethality. PI-PLC-delta1 can be positively or negatively regulated by several binding partners, including p122/Rho GTPase activating protein (RhoGAP), Gha/Transglutaminase II, RalA, and calmodulin. It is involved in Alzheimer's disease and hypertension. Furthermore, PI-PLC-delta1 regulates cell proliferation and cell-cycle progression from G1- to S-phase by control of cyclin E-CDK2 activity and p27 levels. It can be activated by alpha1-adrenoreceptors (AR) in a calcium-dependent manner and may be important for G protein-coupled receptors (GPCR) responses in vascular smooth muscle (VSM). PI-PLC-delta1 may also be involved in noradrenaline (NA)-induced phosphatidylinositol-4,5-bisphosphate (PIP2) hydrolysis and modulate sustained contraction of mesenteric small arteries. In addition, it inhibits thermogenesis and induces lipid accumulation, and therefore contributes to the development of obesity. PI-PLC-delta1 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. In addition, PI-PLC-delta1 possesses a classical leucine-rich nuclear export sequence (NES) located in the EF hand motifs, as well as a nuclear localization signal within its linker region, both of which may be responsible for translocating PI-PLC-delta1 into and out of the cell nucleus.


Pssm-ID: 320047 [Multi-domain]  Cd Length: 139  Bit Score: 48.58  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  209 KSFLMSLCPRPEINEIFTSYhAKAKPYMTKEHLTKFINQKQRDsrlnsllfpPARPDQVQGLIDKYEPSGINAQRGQLSP 288
Cdd:cd16217    59 EEFYKLLTKREEIDVIFGEY-AKSDGTMSRNNLLNFLQEEQRE---------EVAPAYALSLIEKYEPDETAKAQRQMTK 128

                          90
                  ....*....|.
gi 694958715  289 EGMVWFLCGPE 299
Cdd:cd16217   129 DGFLMYLLSPE 139
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1058-1197 8.43e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 49.53  E-value: 8.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1058 QARSRQGLSQEEQISKMMELAREKQAAEL----KALKETSENDTKEMKKKLETKRLERIqgmtkvttdkMAQERLKREin 1133
Cdd:pfam13868   32 KRIKAEEKEEERRLDEMMEEERERALEEEeekeEERKEERKRYRQELEEQIEEREQKRQ----------EEYEEKLQE-- 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694958715  1134 NSHIQEVVQVI-----KQMTENLERHQEKLEEKQAACLEQI--REMEKQFQKEA---LAEY----EARMKGLEAEVKE 1197
Cdd:pfam13868  100 REQMDEIVERIqeedqAEAEEKLEKQRQLREEIDEFNEEQAewKELEKEEEREEderILEYlkekAEREEEREAEREE 177
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1076-1197 9.02e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.38  E-value: 9.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1076 ELAREKQAAE--LKALKETSEnDTKEMKKKLET------KRLERIQG-MTKVTTDKMAQ------ERLKREIN--NSHIQ 1138
Cdd:COG1579    35 ELEDELAALEarLEAAKTELE-DLEKEIKRLELeieeveARIKKYEEqLGNVRNNKEYEalqkeiESLKRRISdlEDEIL 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 694958715 1139 EVVQVIKQMTENLERHQEKLEEKQaaclEQIREMEKQFQkEALAEYEARMKGLEAEVKE 1197
Cdd:COG1579   114 ELMERIEELEEELAELEAELAELE----AELEEKKAELD-EELAELEAELEELEAEREE 167
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1057-1242 1.90e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 1.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1057 LQARSRQGLSQEEQISKM-MELAREKQAAELKALKETSENDTKEMKKKletkRLERIQGMTKVTTDKMA-----QERLKR 1130
Cdd:TIGR02168  791 IEQLKEELKALREALDELrAELTLLNEEAANLRERLESLERRIAATER----RLEDLEEQIEELSEDIEslaaeIEELEE 866

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1131 EINNSHIQ--EVVQVIKQMTENLERHQEKLEEKQaaclEQIREMEKQFQK---------EALAEYEARMKGLEAEVKEsv 1199
Cdd:TIGR02168  867 LIEELESEleALLNERASLEEALALLRSELEELS----EELRELESKRSElrreleelrEKLAQLELRLEGLEVRIDN-- 940

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 694958715  1200 racLRTCFPSEAKDKPERACECPPELceqDPLIAKADAQESRL 1242
Cdd:TIGR02168  941 ---LQERLSEEYSLTLEEAEALENKI---EDDEEEARRRLKRL 977
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1055-1201 2.32e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1055 RGLQARSRQGLSQEEQISKMMELAREKQA---AELKALKETSENDTKEMKKKLE-----TKRLERIQGMTKVTTDKMAQE 1126
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAeleAELEELRLELEELELELEEAQAeeyelLAELARLEQDIARLEERRREL 314

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694958715 1127 RLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAAcLEQIREMEKQfQKEALAEYEARMKGLEAEVKESVRA 1201
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEE-LEEAEAELAE-AEEALLEAEAELAEAEEELEELAEE 387
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 1055-1238 2.75e-05

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 48.60  E-value: 2.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1055 RGLQARSRQGLSQEEQISKMMELAREKQAAELKA-LKETSENDTKEMKKKLETKrLERiqgMTKVTTDKMAQERLKREI- 1132
Cdd:pfam09731  316 RALEKQKEELDKLAEELSARLEEVRAADEAQLRLeFEREREEIRESYEEKLRTE-LER---QAEAHEEHLKDVLVEQEIe 391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1133 -NNSHIQEVvqvIKQMTENLERHQEKLEEKQAacleQIREMEKQFQKEALAEYEAR-MKGLEAEVkESVRACLRTCFPSE 1210
Cdd:pfam09731  392 lQREFLQDI---KEKVEEERAGRLLKLNELLA----NLKGLEKATSSHSEVEDENRkAQQLWLAV-EALRSTLEDGSADS 463

                          170       180
                   ....*....|....*....|....*...
gi 694958715  1211 AKDKPERACECPPELCEQDPLIAKADAQ 1238
Cdd:pfam09731  464 RPRPLVRELKALKELASDDEVVKAALAS 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1077-1202 2.79e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 2.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1077 LAREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNshIQEVVQVIKQMTENLERHQE 1156
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA--LRKDLARLEAEVEQLEERIA 750

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 694958715  1157 KLEEKQAACLEQIREMEKQFQK--EALAEYEARMKGLEAEVKESVRAC 1202
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEaeEELAEAEAEIEELEAQIEQLKEEL 798
EFh_PI-PLCdelta4 cd16219
EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, ...
 211-299 3.34e-05

EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 (PLCD4), or phospholipase C-delta-4 (PLC-delta-4), is expressed in various tissues with the highest levels detected selectively in the brain, skeletal muscle, testis and kidney. It plays a significant role in cell growth, cell proliferation, tumorigenesis, and in an early stage of fertilization. PI-PLC-delta4 may function as a key enzyme in the regulation of PtdIns(4,5)P2 levels and Ca2+ metabolism in nuclei in response to growth factors, and its expression may be partially regulated by an increase in cytoplasmic Ca2+. Moreover, PI-PLC-delta4 binds glutamate receptor-interacting protein1 (GRIP1) in testis and is required for calcium mobilization essential for the zona pellucida-induced acrosome reaction in sperm. Overexpression or dysregulated expression of PLCdelta4 may initiate oncogenesis in certain tissues through upregulating erbB1/2 expression, extracellular signal-regulated kinase (ERK) signaling pathway, and proliferation in MCF-7 cells. PI-PLC-delta4 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, and a C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unlike PI-PLC-delta 1 and 3, a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1 and 3 from the cell nucleus, is not present in PI-PLC-delta4.


Pssm-ID: 320049 [Multi-domain]  Cd Length: 140  Bit Score: 45.22  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  211 FLMSLCPRPEINEIFTSYHAKAKPyMTKEHLTKFINQKQRDsrlnsllfPPARPDQVQGLIDKYEPSGINAQRGQLSPEG 290
Cdd:cd16219    61 FYKALTQREDVLKIFQDFSADGQK-LTLLEFVDFLQQEQLE--------RENTEELAMELIDRYEPSDTAKKLHALSIDG 131


                  ....*....
gi 694958715  291 MVWFLCGPE 299
Cdd:cd16219   132 FLMYLCSPE 140
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 1068-1199 3.37e-05

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 45.72  E-value: 3.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1068 EEQISKMMELAREKQAAELKALKETSENDTKEMKKKLE----------TKRLERIQGMTKVTTDKMaQERLKREInnSHI 1137
Cdd:pfam01442   17 QEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEpyleelqaklGQNVEELRQRLEPYTEEL-RKRLNADA--EEL 93

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1138 QEVV-QVIKQMTENLERHQEKLEEKQAACLEQIRE-MEKQFQ------KEALAEYEARMKGLEAEVKESV 1199
Cdd:pfam01442   94 QEKLaPYGEELRERLEQNVDALRARLAPYAEELRQkLAERLEelkeslAPYAEEVQAQLSQRLQELREKL 163
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 1064-1201 3.67e-05

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 48.03  E-value: 3.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1064 GLSQEEQISKMMELAREKQAAELKALKETSENDTKEMKKKLET----KRLERIQGMTKVTTDKMAQE----RLKREINNS 1135
Cdd:COG5185   269 KLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATesleEQLAAAEAEQELEESKRETEtgiqNLTAEIEQG 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1136 H--IQEVVQVIKQMTENL--ERHQEKLEEKQAACLEQIREMEKQFQ----------KEALAEYEARMKGLEAEVKESVRA 1201
Cdd:COG5185   349 QesLTENLEAIKEEIENIvgEVELSKSSEELDSFKDTIESTKESLDeipqnqrgyaQEILATLEDTLKAADRQIEELQRQ 428
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 1062-1193 4.78e-05

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 45.81  E-value: 4.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1062 RQGLSQEEQISKMMELAREKQAAELKALKETSENDTKEMKKKLEtkrlERIQGMTKVTTdKMAQERLK-----REINNSH 1136
Cdd:pfam15665   70 RQALTEFEQYKRRVEERELKAEAEHRQRVVELSREVEEAKRAFE----EKLESFEQLQA-QFEQEKRKaleelRAKHRQE 144

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1137 IQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREME---KQFQKEALAEYEARMKGLEA 1193
Cdd:pfam15665  145 IQELLTTQRAQSASSLAEQEKLEELHKAELESLRKEVedlRKEKKKLAEEYEQKLSKAQA 204
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1058-1180 5.18e-05

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 46.80  E-value: 5.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1058 QARSRQGLSQEEQISKMMElarEKQAAE---LKALKETSENDTKEMKKKLETKRLERIQGMTKVttDKMAQERLKREINN 1134
Cdd:cd16269   159 RQVPRKGVKAEEVLQEFLQ---SKEAEAeaiLQADQALTEKEKEIEAERAKAEAAEQERKLLEE--QQRELEQKLEDQER 233

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 694958715 1135 SHIQEVVQVIKQMTENLERHQEKLEEKQAACL-EQIREMEKQFQKEA 1180
Cdd:cd16269   234 SYEEHLRQLKEKMEEERENLLKEQERALESKLkEQEALLEEGFKEQA 280
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1060-1203 5.18e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.43  E-value: 5.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1060 RSRQGLSQEE---QISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLERIQgmtkvtTDKMAQERLKREINNSH 1136
Cdd:pfam17380  360 RELERIRQEEiamEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQ------QQKVEMEQIRAEQEEAR 433

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694958715  1137 IQEVVQVIKQMTENLERHQEKLEEKQAAcLEQIR-----------EMEKQFQKEALAEyEARMKGLEAEVKESVRACL 1203
Cdd:pfam17380  434 QREVRRLEEERAREMERVRLEEQERQQQ-VERLRqqeeerkrkklELEKEKRDRKRAE-EQRRKILEKELEERKQAMI 509
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1068-1197 1.17e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1068 EEQISKMMELAR--EKQAAELkalkETSENDTKEMKKKLET--KRLERIQGMTKVTTD---KMAQ-ERLKREINNSHIQE 1139
Cdd:PRK03918  313 EKRLSRLEEEINgiEERIKEL----EEKEERLEELKKKLKEleKRLEELEERHELYEEakaKKEElERLKKRLTGLTPEK 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1140 vvqvIKQMTENLERHQEKLEEKQAACLEQIREMEK----------------------------QFQKEALAEYEARMKGL 1191
Cdd:PRK03918  389 ----LEKELEELEKAKEEIEEEISKITARIGELKKeikelkkaieelkkakgkcpvcgrelteEHRKELLEEYTAELKRI 464


                  ....*.
gi 694958715 1192 EAEVKE 1197
Cdd:PRK03918  465 EKELKE 470
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1062-1199 1.36e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1062 RQGLSQEEQISKMMELAR---EKQAAELKALKE---TSENDTKEMKKKLE--TKRLERIQGMTKVTTDKMAQ-----ERL 1128
Cdd:COG4372    34 RKALFELDKLQEELEQLReelEQAREELEQLEEeleQARSELEQLEEELEelNEQLQAAQAELAQAQEELESlqeeaEEL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1129 KREIN--NSHIQEVVQVIKQMTENLERHQ----------EKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAEVK 1196
Cdd:COG4372   114 QEELEelQKERQDLEQQRKQLEAQIAELQseiaereeelKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193


                  ...
gi 694958715 1197 ESV 1199
Cdd:COG4372   194 RNA 196
BBP1_C pfam15272
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ...
 1055-1197 2.13e-04

Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge


Pssm-ID: 405864 [Multi-domain]  Cd Length: 183  Bit Score: 43.53  E-value: 2.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1055 RGLQARSRQGLSQEEQI-SKMMELaREKQAAELKALKETSENDTKEMKKKLETKrleriqgmtkvttdKMAQE--RLKRE 1131
Cdd:pfam15272   25 KDVRERDEHYQLQETSYkKKYLQT-RNELINELKQSKKLYDNYYKLYSKYQQLK--------------KISNEslDLQST 89

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694958715  1132 INNSHIQEVVQVIKQMTENLERHqEKLEEKQAACleqiREMEKQFQKEALAeYEARMKGLEAEVKE 1197
Cdd:pfam15272   90 ITNLESQLVDQAIDKDREIHNLN-EKILSLELRN----QELETKREIDKMK-YESRIDELERQLKE 149
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1058-1214 2.26e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.50  E-value: 2.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1058 QARSRQGLSQEEQISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLER------------IQGMTKVTTDKMAQ 1125
Cdd:pfam17380  431 EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRdrkraeeqrrkiLEKELEERKQAMIE 510

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1126 ERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQaacLEQIREMEKQFQKeaLAEYEARMKGLEAEvkesvRACLRT 1205
Cdd:pfam17380  511 EERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQE---MEERRRIQEQMRK--ATEERSRLEAMERE-----REMMRQ 580


                   ....*....
gi 694958715  1206 CFPSEAKDK 1214
Cdd:pfam17380  581 IVESEKARA 589
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
 1059-1188 2.36e-04

YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.


Pssm-ID: 435583 [Multi-domain]  Cd Length: 160  Bit Score: 42.90  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1059 ARSRQGLSQEEQISKMMELAREKQAAELKAlKETSENDtkEMKKKLETKRLERIQGMTKVTTDKMAQERLKREinnsHIQ 1138
Cdd:pfam16789   24 KDKKRALEKEKEKLAELEAERDKVRKHKKA-KMQQLRD--EMDRGTTSDKILQMKRYIKVVKERLKQEEKKVQ----DQK 96

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 694958715  1139 EVVQVIKQmteNLERHQEKLEEKQAAcLEQIREMEKQFQKEALAEYEARM 1188
Cdd:pfam16789   97 EQVRTAAR---NLEIAREELKKKRQE-VEKLEKHKKEWVKEMKKEEEDQE 142
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 312-460 2.41e-04

Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar proteins; This subfamily corresponds to the catalytic domain present in bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) and their sequence homologs found in eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Its catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. Eukaryotic homologs in this family are named as phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). They are distinct from the typical eukaryotic phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11), which have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, which is closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may be distinct from that of typical eukaryotic PI-PLCs. This family also includes a distinctly different type of eukaryotic PLC, glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC), an integral membrane protein characterized in the protozoan parasite Trypanosoma brucei. T. brucei GPI-PLC hydrolyzes the GPI-anchor on the variant specific glycoprotein (VSG), releasing dimyristyl glycerol (DMG), which may facilitate the evasion of the protozoan to the host's immune system. It does not require Ca2+ for its activity and is more closely related to bacterial PI-PLCs, but not mammalian PI-PLCs.


Pssm-ID: 176500 [Multi-domain]  Cd Length: 271  Bit Score: 44.39  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  312 HDMTQPLNHYFINSSHNTY-LTAGQFSGLSSA-----EMY-RQVLLSGCRCVELDCWKgKPPDEEPIITHGFTMTTDIFF 384
Cdd:cd08557     3 LLDDLPLSQLSIPGTHNSYaYTIDGNSPIVSKwsktqDLSiTDQLDAGVRYLDLRVAY-DPDDGDLYVCHGLFLLNGQTL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  385 KEAIEAIAesAF-KTSPY-PIILSFENHV--DSPRQQAKMAEYCRTIFGDMLLTeplekfPLKPGVPLPSPEDLR-GKIL 459
Cdd:cd08557    82 EDVLNEVK--DFlDAHPSeVVILDLEHEYggDNGEDHDELDALLRDVLGDPLYR------PPVRAGGWPTLGELRaGKRV 153


                  .
gi 694958715  460 I 460
Cdd:cd08557   154 L 154
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1058-1197 2.64e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.52  E-value: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1058 QARSRQGLSQEEQIskmMELAREKQAAELKALKETS----------ENDTKEMKKKLETKRLERiQGMTKVTTDKMAQER 1127
Cdd:pfam13868   69 EERKRYRQELEEQI---EEREQKRQEEYEEKLQEREqmdeiveriqEEDQAEAEEKLEKQRQLR-EEIDEFNEEQAEWKE 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1128 LKREINNSHIQEVVQVIKQMTENL--------------ERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEA 1193
Cdd:pfam13868  145 LEKEEEREEDERILEYLKEKAEREeereaereeieeekEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKER 224


                   ....
gi 694958715  1194 EVKE 1197
Cdd:pfam13868  225 EEAE 228
PRK12704 PRK12704
phosphodiesterase; Provisional
 1068-1197 3.02e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 3.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1068 EEQISKMMELARE-----KQAAELKA------LKETSENDTKEMKKKLEtKRLERIQgmtkvttdkMAQERLKREINNsh 1136
Cdd:PRK12704   37 EEEAKRILEEAKKeaeaiKKEALLEAkeeihkLRNEFEKELRERRNELQ-KLEKRLL---------QKEENLDRKLEL-- 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694958715 1137 IQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEA-LAEYEAR---MKGLEAEVKE 1197
Cdd:PRK12704  105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgLTAEEAKeilLEKVEEEARH 169
PRK12704 PRK12704
phosphodiesterase; Provisional
 1077-1197 4.83e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 4.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1077 LAREKQA-AELKALKETSENDTKEMKKKLET-KRLERIQGMTKVTTDKMAQERLKREINNsHIQEVVQVIKQMTENLERH 1154
Cdd:PRK12704   23 FVRKKIAeAKIKEAEEEAKRILEEAKKEAEAiKKEALLEAKEEIHKLRNEFEKELRERRN-ELQKLEKRLLQKEENLDRK 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 694958715 1155 QEKLEEKQAACLEQIREMEKqfQKEALAEYEARMKGLEAEVKE 1197
Cdd:PRK12704  102 LELLEKREEELEKKEKELEQ--KQQELEKKEEELEELIEEQLQ 142
EFh_PRIP cd16206
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ...
 197-299 5.16e-04

EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); This family represents a class of metazoan phospholipase C related, but catalytically inactive proteins (PRIP), which belong to a group of novel inositol 1,4,5-trisphosphate (InsP3) binding protein. PRIP has a primary structure and domain architecture, incorporating a pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain with highly conserved X- and Y-regions split by a linker sequence, and a C-terminal C2 domain, similar to phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11)-delta isoforms. Due to replacement of critical catalytic residues, PRIP do not have PLC enzymatic activity. PRIP consists of two subfamilies, PRIP-1(also known as p130 or PLC-L1), which is predominantly expressed in the brain, and PRIP-2 (also known as PLC-L2), which exhibits a relatively ubiquitous expression. Experiments show both, PRIP-1 and PRIP-2, are involved in InsP3-mediated calcium signaling pathway and GABA(A)receptor-mediated signaling pathway. In addition, PRIP-2 acts as a negative regulator of B-cell receptor signaling and immune responses.


Pssm-ID: 320036 [Multi-domain]  Cd Length: 143  Bit Score: 41.81  E-value: 5.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  197 AINPEDFPEpVYKSflmsLCPRPEINEIFTSYhAKAKPYMTKEHLTKFINQKQRDSRLNsllfpparPDQVQGLIDKYEP 276
Cdd:cd16206    55 RVSSDEFVE-LFKE----LATRPEIYFLLVRY-ASNKDYLTVDDLMLFLEAEQGMTGVT--------KEKCLEIINKYEP 120

                          90       100
                  ....*....|....*....|...
gi 694958715  277 SGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16206   121 SEEGREKGQLGIDGFTRYLLSEE 143
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 684-779 5.62e-04

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 41.41  E-value: 5.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  684 LSITVISGQFLSERSVR----TYVEVELFGlpgDPKRRYRTKLSPSTNSINPVWKEEpFVFEkilMP----ELASLRVAV 755
Cdd:cd00276    16 LTVVVLKARNLPPSDGKglsdPYVKVSLLQ---GGKKLKKKKTSVKKGTLNPVFNEA-FSFD---VPaeqlEEVSLVITV 88

                          90       100
                  ....*....|....*....|....*...
gi 694958715  756 MEEG----NKFLGHRIIPINALNSGYHH 779
Cdd:cd00276    89 VDKDsvgrNEVIGQVVLGPDSGGEELEH 116
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1058-1201 5.65e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.34  E-value: 5.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1058 QARSRQGLSQEEQISKMMELAREKqaaELKALKETSEndtKEMkKKLETKRLERIQGMTKVTTDKMAQERLKREInnshi 1137
Cdd:pfam17380  412 QRKIQQQKVEMEQIRAEQEEARQR---EVRRLEEERA---REM-ERVRLEEQERQQQVERLRQQEEERKRKKLEL----- 479

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694958715  1138 qevvqvikqmtENLERHQEKLEEKQAACLEQirEMEKqfQKEALAEYEARMKGLEAEVKESVRA 1201
Cdd:pfam17380  480 -----------EKEKRDRKRAEEQRRKILEK--ELEE--RKQAMIEEERKRKLLEKEMEERQKA 528
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
 202-295 5.76e-04

EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar proteins; This family represents a group of putative phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) encoded by PLC1 genes from yeasts, which are homologs of the delta isoforms of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The prototype of this family is protein Plc1p (also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1) encoded by PLC1 genes from Saccharomyces cerevisiae. ScPlc1p contains both highly conserved X- and Y- regions of PLC catalytic core domain, as well as a presumptive EF-hand like calcium binding motif. Experiments show that ScPlc1p displays calcium dependent catalytic properties with high similarity to those of the mammalian PLCs, and plays multiple roles in modulating the membrane/protein interactions in filamentation control. CaPlc1p encoded by CAPLC1 from the closely related yeast Candida albicans, an orthologue of S. cerevisiae Plc1p, is also included in this group. Like SCPlc1p, CaPlc1p has conserved presumptive catalytic domain, shows PLC activity when expressed in E. coli, and is involved in multiple cellular processes. There are two other gene copies of CAPLC1 in C. albicans, CAPLC2 (also named as PIPLC) and CAPLC3. Experiments show CaPlc1p is the only enzyme in C. albicans which functions as PLC. The biological functions of CAPLC2 and CAPLC3 gene products must be clearly different from CaPlc1p, but their exact roles remain unclear. Moreover, CAPLC2 and CAPLC3 gene products are more similar to extracellular bacterial PI-PLC than to the eukaryotic PI-PLC, and they are not included in this subfamily.


Pssm-ID: 320037 [Multi-domain]  Cd Length: 142  Bit Score: 41.47  E-value: 5.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  202 DFPEpvYKSFLMSLCPRPEINEIFTSYHAKAKPYMTKEHLTKFINQKQRDSRlnsllfppaRPDQVQGLIDKYEPSGINA 281
Cdd:cd16207    56 NFEE--FQEFVKLLKRRKDIKAIFKQLTKPGSDGLTLEEFLKFLRDVQKEDV---------DRETWEKIFEKFARRIDDS 124

                          90
                  ....*....|....
gi 694958715  282 QRGQLSPEGMVWFL 295
Cdd:cd16207   125 DSLTMTLEGFTSFL 138
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 684-776 5.95e-04

C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176060 [Multi-domain]  Cd Length: 126  Bit Score: 41.20  E-value: 5.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  684 LSITVISGQFLSER--SVRTYVEVELfglpGDPKRRYRTklSPSTNSINPVWkEEPFVFEkiLMPELASLRVAVMEEG-- 759
Cdd:cd08678     1 LLVKNIKANGLSEAagSSNPYCVLEM----DEPPQKYQS--STQKNTSNPFW-DEHFLFE--LSPNSKELLFEVYDNGkk 71

                          90
                  ....*....|....*....
gi 694958715  760 --NKFLGHRIIPINALNSG 776
Cdd:cd08678    72 sdSKFLGLAIVPFDELRKN 90
APP_E2 pfam12925
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ...
 1086-1228 6.10e-04

E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains of the amyloid precursor protein. The structure of E2 consists of two coiled-coil sub-structures connected through a continuous helix, and bears an unexpected resemblance to the spectrin family of protein structures.E 2 can reversibly dimerize in solution, and the dimerization occurs along the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against the C-terminal substructure of a second monomer. The high degree of conservation of residues at the putative dimer interface suggests that the E2 dimer observed in the crystal could be physiologically relevant. Heparin sulfate proteoglycans, the putative ligands for the precursor present in extracellular matrix, bind to E2 at a conserved and positively charged site near the dimer interface.


Pssm-ID: 463752  Cd Length: 190  Bit Score: 42.33  E-value: 6.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1086 LKALKETSENDT-KEMKKKLETKRLERiqgMTKVTTD-KMAQERLKrEINNSHIQEVVQVIKQMTENLERHQEKLEEKQA 1163
Cdd:pfam12925   14 FEHPDPRNEHESfKKAKKRLEEKHRER---MTKVMKEwEEAEERYQ-NLPKADPKAAEKFKKAMTARFQETVEALEEEAA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1164 ACLEQIREMEKQF--------QKEALAEYearMKGLEAEVK--ESVRACLRTCFPSEAKDKP------ERACECPPELCE 1227
Cdd:pfam12925   90 AERQQLVETHQQRveahlndrRRDALECY---LQALQENPPnpHRILKALKKLLRAEQKDRRhtlrhyRHLLASDPEKAE 166


                   .
gi 694958715  1228 Q 1228
Cdd:pfam12925  167 Q 167
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1078-1191 6.75e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 6.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1078 AREKQAAELKALKETSENDTKEMKKKLE--TKRLERI------QGMTK-VTTDKMAQERLKREINNSH--IQEVVQVIKQ 1146
Cdd:COG1579    49 AAKTELEDLEKEIKRLELEIEEVEARIKkyEEQLGNVrnnkeyEALQKeIESLKRRISDLEDEILELMerIEELEEELAE 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694958715 1147 MTENLERHQEKLEEKQA--------------ACLEQIREMEKQFQKEALAEYE---ARMKGL 1191
Cdd:COG1579   129 LEAELAELEAELEEKKAeldeelaeleaeleELEAEREELAAKIPPELLALYErirKRKNGL 190
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
 715-779 7.00e-04

C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit various effector proteins to organelles and vesicles. Rab11-family interacting proteins (FIPs) are involved in mediating the role of Rab11. FIPs can be divided into three classes: class I FIPs (Rip11a, Rip11b, RCP, and FIP2) which contain a C2 domain after N-terminus of the protein, class II FIPs (FIP3 and FIP4) which contain two EF-hands and a proline rich region, and class III FIPs (FIP1) which exhibits no homology to known protein domains. All FIP proteins contain a highly conserved, 20-amino acid motif at the C-terminus of the protein, known as Rab11/25 binding domain (RBD). Class I FIPs are thought to bind to endocytic membranes via their C2 domain, which interacts directly with phospholipids. Class II FIPs do not have any membrane binding domains leaving much to speculate about the mechanism involving FIP3 and FIP4 interactions with endocytic membranes. The members in this CD are class I FIPs. The exact function of the Rab11 and FIP interaction is unknown, but there is speculation that it involves the role of forming a targeting complex that recruits a group of proteins involved in membrane transport to organelles. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176064 [Multi-domain]  Cd Length: 126  Bit Score: 40.90  E-value: 7.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694958715  715 KRRYRTklSPSTNSINPVWKEE-PFVFEKILM--PELASLRVAVMEEGN----KFLGHRIIPINALNSGYHH 779
Cdd:cd08682    30 KEKYST--SVKEKTTSPVWKEEcSFELPGLLSgnGNRATLQLTVMHRNLlgldKFLGQVSIPLNDLDEDKGR 99
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1062-1192 7.34e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.37  E-value: 7.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1062 RQGLSQEEQISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLER------IQGMTKVTTDKMAQERL----KRE 1131
Cdd:pfam13868  207 RAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAereeeeFERMLRKQAEDEEIEQEeaekRRM 286

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694958715  1132 INNSHIQEVVQVIKqmtenlERHQEKLEEKQAACLEQIREMEKQFQKEALAEyEARMKGLE 1192
Cdd:pfam13868  287 KRLEHRRELEKQIE------EREEQRAAEREEELEEGERLREEEAERRERIE-EERQKKLK 340
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1060-1195 8.68e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.63  E-value: 8.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1060 RSRQGLSQ--EEQISKMMELAREKQAAE---------LKALKETSEND------------------TKEMKKKLETKRLE 1110
Cdd:pfam01576  685 RSKRALEQqvEEMKTQLEELEDELQATEdaklrlevnMQALKAQFERDlqardeqgeekrrqlvkqVRELEAELEDERKQ 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1111 RIQGMTKVTTDKMAQERLKREIN--NSHIQEVVQVIKQMTENLERHQEKLEEKQAAcleqiremekqfQKEALA---EYE 1185
Cdd:pfam01576  765 RAQAVAAKKKLELDLKELEAQIDaaNKGREEAVKQLKKLQAQMKDLQRELEEARAS------------RDEILAqskESE 832

                          170
                   ....*....|
gi 694958715  1186 ARMKGLEAEV 1195
Cdd:pfam01576  833 KKLKNLEAEL 842
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1064-1197 9.40e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 9.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1064 GLSQEEQISKMMELAREKQAAELKALKETSENDTKEmkKKLETKRLERIQGMTKVTTDKMAQERLKREIN--NSHIQEVV 1141
Cdd:TIGR02168  231 VLRLEELREELEELQEELKEAEEELEELTAELQELE--EKLEELRLEVSELEEEIEELQKELYALANEISrlEQQKQILR 308

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 694958715  1142 QVIKQMTENLERHQEKLEEKQAACLEQIREMEKqfQKEALAEYEARMKGLEAEVKE 1197
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAE--LEEKLEELKEELESLEAELEE 362
RNase_Y_N pfam12072
RNase Y N-terminal region;
1057-1157 9.90e-04

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 41.80  E-value: 9.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1057 LQARSRQGLSQEEQISKMMELAREKQAAELKALKETS--ENDTKEMKKKLET------KRLERIQGMTKvttdKMAQERL 1128
Cdd:pfam12072   80 LQRQERRLLQKEETLDRKDESLEKKEESLEKKEKELEaqQQQLEEKEEELEElieeqrQELERISGLTS----EEAKEIL 155

                           90       100
                   ....*....|....*....|....*....
gi 694958715  1129 KREINNSHIQEVVQVIKQMTENLERHQEK 1157
Cdd:pfam12072  156 LDEVEEELRHEAAVMIKEIEEEAKEEADK 184
DUF1978 pfam09321
Domain of unknown function (DUF1978); Members of this family are found in various hypothetical ...
 1054-1199 1.04e-03

Domain of unknown function (DUF1978); Members of this family are found in various hypothetical proteins produced by the bacterium Chlamydia pneumoniae. Their exact function has not, as yet, been identified.


Pssm-ID: 312723 [Multi-domain]  Cd Length: 244  Bit Score: 42.22  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1054 CRGlqarSRQGLSQEEQISKMMELAREKQAAElKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKM--AQERLKR- 1130
Cdd:pfam09321   52 CRD----ALSEISRHELWEKKAHLKHLESLYT-QARDRFEKQSSKKNQKELEEAEQEYLSSWEDVKDQEIerVQERLQAl 126

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694958715  1131 -----EINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQ----IREMEKqfqKEALAEYEARMKGLEAEVKESV 1199
Cdd:pfam09321  127 qalypEVSVSEEETEGQETVTPTVDLETALGRIEESYRECVRDqedyWKEEES---KEVEMSAEFREEGGKKKSEEFQ 201
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1071-1197 1.09e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1071 ISKMMELAREKQAAELKAlKETSENDTKEMKKKLETKrLERIQGMTKVTTDKMAQ-ERLKREInnshiqEVVQVIKQMTE 1149
Cdd:PRK03918  170 VIKEIKRRIERLEKFIKR-TENIEELIKEKEKELEEV-LREINEISSELPELREElEKLEKEV------KELEELKEEIE 241

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 694958715 1150 NLERHQEKLEEKQAACLEQIREMEKQfqkeaLAEYEARMKGLEAEVKE 1197
Cdd:PRK03918  242 ELEKELESLEGSKRKLEEKIRELEER-----IEELKKEIEELEEKVKE 284
PTZ00121 PTZ00121
MAEBL; Provisional
 1058-1241 1.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1058 QARSRQGLSQEEQISKMMEL--AREKQAAELKALKETSENDTK---EMKKKLETKRLERIQGMTKVTTDKMAQERLKREI 1132
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1133 NNSHIQEV--VQVIKQMTENLERHQEklEEKQAAclEQIR--EMEKQFQKEALAEYEARMKGLEAEVKESvraclrtcfp 1208
Cdd:PTZ00121 1618 AKIKAEELkkAEEEKKKVEQLKKKEA--EEKKKA--EELKkaEEENKIKAAEEAKKAEEDKKKAEEAKKA---------- 1683

                         170       180       190
                  ....*....|....*....|....*....|...
gi 694958715 1209 SEAKDKPERACECPPELCEQDPLIAKADAQESR 1241
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1069-1197 1.48e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.21  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1069 EQISKMMELARE--KQAAELKALKETSENDTKEMKKKLETKRLERiqgmTKVTTDKMAQERLKREINN------------ 1134
Cdd:COG1340    57 EEAQELREKRDElnEKVKELKEERDELNEKLNELREELDELRKEL----AELNKAGGSIDKLRKEIERlewrqqtevlsp 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694958715 1135 SHIQEVVQVIKQMTENLERHQEKLEEKqaaclEQIREMEKQFQ--KEALAEYEARMKGLEAEVKE 1197
Cdd:COG1340   133 EEEKELVEKIKELEKELEKAKKALEKN-----EKLKELRAELKelRKEAEEIHKKIKELAEEAQE 192
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 1080-1193 1.54e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.93  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1080 EKQAAELKALKETSENDTKEMKKKLE--TKRLERIQG-----MTKVTTDKMAQERLKREINnshiqEVVQVIKQMTENLE 1152
Cdd:pfam07926    7 QSEIKRLKEEAADAEAQLQKLQEDLEkqAEIAREAQQnyereLVLHAEDIKALQALREELN-----ELKAEIAELKAEAE 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 694958715  1153 RHQEKLEEKQAACLEQiremEKQFQKEaLAEYEARMKGLEA 1193
Cdd:pfam07926   82 SAKAELEESEESWEEQ----KKELEKE-LSELEKRIEDLNE 117
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 1058-1195 1.77e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 42.42  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1058 QARSRQGLSQEEQISKMMELAREKQAAELKALKETSEND-TKEMKKKLE-TKRLERIQ---------------------- 1113
Cdd:pfam05557    4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQlDRESDRNQElQKRIRLLEkreaeaeealreqaelnrlkkk 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1114 ---GMTKVTTDKMAQER--------LKREINNSH--IQEVVQVIKQMTENLERHQEKLEEKQAAC--LEQIREmEKQFQK 1178
Cdd:pfam05557   84 yleALNKKLNEKESQLAdareviscLKNELSELRrqIQRAELELQSTNSELEELQERLDLLKAKAseAEQLRQ-NLEKQQ 162

                          170
                   ....*....|....*..
gi 694958715  1179 EALAEYEARMKGLEAEV 1195
Cdd:pfam05557  163 SSLAEAEQRIKELEFEI 179
CR6_interact pfam10147
Growth arrest and DNA-damage-inducible proteins-interacting protein 1; Members of this family ...
 1067-1188 2.00e-03

Growth arrest and DNA-damage-inducible proteins-interacting protein 1; Members of this family of proteins act as negative regulators of G1 to S cell cycle phase progression by inhibiting cyclin-dependent kinases. Inhibitory effects are additive with GADD45 proteins but occur also in the absence of GADD45 proteins. Furthermore, they act as a repressor of the orphan nuclear receptor NR4A1 by inhibiting AB domain-mediated transcriptional activity.


Pssm-ID: 431088 [Multi-domain]  Cd Length: 204  Bit Score: 40.99  E-value: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1067 QEEQISKMMELAREKQAAELKALKETSENDTKEMKK------KLETKRLERIQgmtKVTTDKMAQERLKREinnshIQEv 1140
Cdd:pfam10147   85 WYPSLAQMLESNRAQKAEKEARRQAREQEIAKKMAKmpqwiaDWNAQKAKREA---EAQAAKERKERLVAE-----ARE- 155

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 694958715  1141 vQVIKQMTENLERHQEKLEEKQAACLEQIREmEKQFQKEalaeyEARM 1188
Cdd:pfam10147  156 -HFGFKVDPRDERFKEMLQQKEKEDKKKVKE-AKRKEKE-----EKRM 196
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 1075-1197 2.12e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 39.13  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1075 MELAREKQAAELKaLKEtSENDTKEMKKKLEtkRLERiqgmtkvTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERH 1154
Cdd:pfam20492    2 EEAEREKQELEER-LKQ-YEEETKKAQEELE--ESEE-------TAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 694958715  1155 QEKLEEKQAACLEQIREMEKQFQK--EALAEYEARMKGLEAEVKE 1197
Cdd:pfam20492   71 AEMEAEEKEQLEAELAEAQEEIARleEEVERKEEEARRLQEELEE 115
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1058-1197 2.17e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1058 QARSRQGLSQEEQISKMMELAREKQAAELKALKetsENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNsHI 1137
Cdd:COG1196   327 ELEEELEELEEELEELEEELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA-QL 402

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1138 QEVVQVIKQMTENLERHQEKLEEKQAAcLEQIREMEKQfQKEALAEYEARMKGLEAEVKE 1197
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEA-LAELEEEEEE-EEEALEEAAEEEAELEEEEEA 460
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1058-1217 2.21e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1058 QARSRQGLSQEEQisKMMELAREKQAAELKALKETSEndtkEMKKKLETKRLERIQGMTKVTTDKMAQERLKREInnshi 1137
Cdd:TIGR02169  305 SLERSIAEKEREL--EDAEERLAKLEAEIDKLLAEIE----ELEREIEEERKRRDKLTEEYAELKEELEDLRAEL----- 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1138 QEVVQVIKQMTENLERHQEKLEEKQAACLEQIREM-----EKQFQKEALAEYEARMKGLEAEVKEsvraclrtcFPSEAK 1212
Cdd:TIGR02169  374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELdrlqeELQRLSEELADLNAAIAGIEAKINE---------LEEEKE 444


                   ....*
gi 694958715  1213 DKPER 1217
Cdd:TIGR02169  445 DKALE 449
RNase_Y_N pfam12072
RNase Y N-terminal region;
1068-1197 2.60e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.64  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1068 EEQISKMMELAR------EKQA------AELKA------LKETSENDTKEmkKKLETKRLER--IQgmTKVTTDKMAQER 1127
Cdd:pfam12072   26 EAKIGSAEELAKriieeaKKEAetkkkeALLEAkeeihkLRAEAERELKE--RRNELQRQERrlLQ--KEETLDRKDESL 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1128 LKREINnshIQEVVQVIKQMTENLERHQEKLEE---KQAACLEQI-------------REMEKQFQKEAlaeyeARM-KG 1190
Cdd:pfam12072  102 EKKEES---LEKKEKELEAQQQQLEEKEEELEElieEQRQELERIsgltseeakeillDEVEEELRHEA-----AVMiKE 173


                   ....*..
gi 694958715  1191 LEAEVKE 1197
Cdd:pfam12072  174 IEEEAKE 180
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1058-1197 2.62e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 2.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1058 QARSRQGLSQEEQISKMMELAREKQA--AELKALKETsendtKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNs 1135
Cdd:pfam13868  141 EWKELEKEEEREEDERILEYLKEKAEreEEREAEREE-----IEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEE- 214

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694958715  1136 hiQEVVQVIKQMTEnLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAEVKE 1197
Cdd:pfam13868  215 --QERKERQKEREE-AEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAED 273
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1076-1194 2.64e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1076 ELAR-EKQAAELKALKETSENDTKEMKKK---LETK-------------RLERIQGMTKVTTDKMAQERLKREInnshIQ 1138
Cdd:COG4913   686 DLAAlEEQLEELEAELEELEEELDELKGEigrLEKEleqaeeeldelqdRLEAAEDLARLELRALLEERFAAAL----GD 761

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694958715 1139 EVVQvikQMTENLERHQEKLEEKQAACLEQIREMEKQFQK-------------EALAEYEARMKGLEAE 1194
Cdd:COG4913   762 AVER---ELRENLEERIDALRARLNRAEEELERAMRAFNRewpaetadldadlESLPEYLALLDRLEED 827
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 1054-1173 2.64e-03

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 39.10  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1054 CRGLQARSRQGLSQEEQISKMMELAREKQAaELKALKETSENdTKEMKKKLETKRLERIQGMTKvttdkmaQERLKREIN 1133
Cdd:pfam18595   18 ARELQAKIDALQVVEKDLRSCIKLLEEIEA-ELAKLEEAKKK-LKELRDALEEKEIELRELERR-------EERLQRQLE 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 694958715  1134 NshiqevvqvikqMTENLERHQEKLEEKQAACLEQIREME 1173
Cdd:pfam18595   89 N------------AQEKLERLREQAEEKREAAQARLEELR 116
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 1078-1175 2.77e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 39.71  E-value: 2.77e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715   1078 AREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMT--KVTTDKM---AQERLKREINNSHIQEvvqviKQMTENLE 1152
Cdd:smart01071   40 ARVERMEEIKNLKYELIMNDHLNKRIDKLLKGLREEELSpeTPTYNEMlaeLQDQLKKELEEANGDS-----EGLLEELK 114

                            90       100
                    ....*....|....*....|...
gi 694958715   1153 RHQEKLEEKQAACLEQIREMEKQ 1175
Cdd:smart01071  115 KHRDKLKKEQKELRKKLDELEKE 137
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 684-758 2.79e-03

C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is present in cPLA2 which releases arachidonic acid from membranes initiating the biosynthesis of potent inflammatory mediators such as prostaglandins, leukotrienes, and platelet-activating factor. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members of this cd have a type-II topology.


Pssm-ID: 176001 [Multi-domain]  Cd Length: 119  Bit Score: 38.78  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  684 LSITVISGQFLSERSVRT----YVEVELfglPGDPKRRYRTKLSPstNSINPVWKEEpfvFEKILMPELAS-LRVAVMEE 758
Cdd:cd04036     2 LTVRVLRATNITKGDLLStpdcYVELWL---PTASDEKKRTKTIK--NSINPVWNET---FEFRIQSQVKNvLELTVMDE 73
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1060-1196 3.00e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 39.64  E-value: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1060 RSRQGLSQEEQISKMmeLAREKQAAELKALKETSENDTKEMKKKLETKRL------ERIQGMTKvtTDKMAQERLKRE-- 1131
Cdd:pfam05672    1 KPSAGTTDAEEAARI--LAEKRRQAREQREREEQERLEKEEEERLRKEELrrraeeERARREEE--ARRLEEERRREEee 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694958715  1132 INNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLE----QIREMEKQFQKEaLAEYEARMKGLEAEVK 1196
Cdd:pfam05672   77 RQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREeaerQRQEREKIMQQE-EQERLERKKRIEEIMK 144
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1065-1197 3.25e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1065 LSQEEQISKMMELAREKQA--AELKALKETSENDTKEMKKKLETKR--LERIQGMTKVTTDKMAQERLKREINN------ 1134
Cdd:COG4717    70 LKELKELEEELKEAEEKEEeyAELQEELEELEEELEELEAELEELReeLEKLEKLLQLLPLYQELEALEAELAElperle 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694958715 1135 ---SHIQEVVQV---IKQMTENLERHQEKLEEKQ----AACLEQIREMEKQFQK--EALAEYEARMKGLEAEVKE 1197
Cdd:COG4717   150 eleERLEELRELeeeLEELEAELAELQEELEELLeqlsLATEEELQDLAEELEElqQRLAELEEELEEAQEELEE 224
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1066-1193 3.92e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 3.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1066 SQEEQISKMMEL--AREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREIN---------- 1133
Cdd:TIGR02168  355 SLEAELEELEAEleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEellkkleeae 434

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694958715  1134 ----NSHIQEVVQVIKQMTENLERHQEKLEEKQAAcLEQIREMEKQFQKEaLAEYEARMKGLEA 1193
Cdd:TIGR02168  435 lkelQAELEELEEELEELQEELERLEEALEELREE-LEEAEQALDAAERE-LAQLQARLDSLER 496
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1057-1241 3.93e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1057 LQARSRQGLSQEEQISKMmelarEKQAAELKALKETSENDTKEMKKKLEtKRLERIQGMTKVTTDKM--AQERLKREINN 1134
Cdd:COG4942    64 IAALARRIRALEQELAAL-----EAELAELEKEIAELRAELEAQKEELA-ELLRALYRLGRQPPLALllSPEDFLDAVRR 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1135 SH-IQEVVQVIKQMTENLERHQEKLEEKQAAcLEQiremEKQFQKEALAEYEARMKGLEAEVKEsvRACLRTCFPSEAKD 1213
Cdd:COG4942   138 LQyLKYLAPARREQAEELRADLAELAALRAE-LEA----ERAELEALLAELEEERAALEALKAE--RQKLLARLEKELAE 210

                         170       180
                  ....*....|....*....|....*...
gi 694958715 1214 KPERACECPPELCEQDPLIAKADAQESR 1241
Cdd:COG4942   211 LAAELAELQQEAEELEALIARLEAEAAA 238
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1072-1201 4.61e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1072 SKMMELAREKQAAELKALKETSENDTKEMKKKLE-----TKRLERIQGmtkvttDKMAQERLKREINNshiqevvqvIKQ 1146
Cdd:PRK03918  243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEeleekVKELKELKE------KAEEYIKLSEFYEE---------YLD 307

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 694958715 1147 MTENLERHQEKLEEKQAACLEQIREMEKqfQKEALAEYEARMKGLE---AEVKESVRA 1201
Cdd:PRK03918  308 ELREIEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEkrlEELEERHEL 363
PH_PLC_ELMO1 cd01248
Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain; The ...
 17-134 5.42e-03

Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain; The C-terminal region of ELMO1, the PH domain and Pro-rich sequences, binds the SH3-containing region of DOCK2 forming a intermolecular five-helix bundle allowing for DOCK mediated Rac1 activation. ELMO1, a mammalian homolog of C. elegans CED-12, contains an N-terminal RhoG-binding region, a ELMO domain, a PH domain, and a C-terminal sequence with three PxxP motifs. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). All PLCs, except for PLCzeta, have a PH domain which is for most part N-terminally located, though lipid binding specificity is not conserved between them. In addition PLC gamma contains a split PH domain within its catalytic domain that is separated by 2 SH2 domains and a single SH3 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: 269952  Cd Length: 108  Bit Score: 37.69  E-value: 5.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715   17 LSQGERFIKWDdETTVASPVILRVDPKGYYLYWTYQSKEME--FLDITSIRDTRFGKFAKMPKSQKLRdvfNMDFPDNSF 94
Cdd:cd01248     1 LQQGTLLLKYR-EGSKPKERTFYLDPDGTRITWESSKKKSEkkSIDISDIKEIRPGKDTDGFKRKKKS---NKPKEERCF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 694958715   95 llkTLTVVSGPDMVDLtfhnfVSYKENVGKVWAEDVLALV 134
Cdd:cd01248    77 ---SIIYGSNNKTLDL-----VAPSEDEANLWVEGLRALL 108
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1062-1184 5.61e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1062 RQGLSQEEQISKMMELAREKQA--AELKALKETSENDTKEMKKKLETKRLERIQgmTKVTTDKMAQERLKREINNshIQE 1139
Cdd:COG4717   378 EAGVEDEEELRAALEQAEEYQElkEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEE--LRE 453

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 694958715 1140 VVQVIKQMTENLERHQE--KLEEKQAACLEQIREMEKQFQKEALAEY 1184
Cdd:COG4717   454 ELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALE 500
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1057-1194 5.95e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1057 LQARSRQGLSQEEQISKMMELAREKQAAELKALKE-TSENDTKEMKKKLETKRLERIQgmtkvttDKMAQERLKREINNS 1135
Cdd:COG1196   286 AQAEEYELLAELARLEQDIARLEERRRELEERLEElEEELAELEEELEELEEELEELE-------EELEEAEEELEEAEA 358

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 694958715 1136 HIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQfqKEALAEYEARMKGLEAE 1194
Cdd:COG1196   359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--AAQLEELEEAEEALLER 415
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1068-1197 6.64e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 6.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715 1068 EEQISKmmeLAREKQAAEL-KALKEtsenDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQ 1146
Cdd:COG1196   199 ERQLEP---LERQAEKAERyRELKE----ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 694958715 1147 MTENLERHQEKLEEKQAACLEQIREMEK-----QFQKEALAEYEARMKGLEAEVKE 1197
Cdd:COG1196   272 LRLELEELELELEEAQAEEYELLAELARleqdiARLEERRRELEERLEELEEELAE 327
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1061-1197 7.04e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.32  E-value: 7.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1061 SRQGLSQEEQISKMMELAREKQA-AELKALKETSENDTKEMKKKLETKRLERIQGMtKVTTDKMAQERLKREIN--NSHI 1137
Cdd:pfam15709  334 SRDRLRAERAEMRRLEVERKRREqEEQRRLQQEQLERAEKMREELELEQQRRFEEI-RLRKQRLEEERQRQEEEerKQRL 412

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694958715  1138 QEvvqvikQMTenlerhQEKLEEKQAACLEQIREMEKQFQKEALAEYEA---RMKGLEAEVKE 1197
Cdd:pfam15709  413 QL------QAA------QERARQQQEEFRRKLQELQRKKQQEEAERAEAekqRQKELEMQLAE 463
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1084-1194 7.61e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 7.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1084 AELKALKETSEND-TKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREIN------------NSHIQEVVQVIKQMTEN 1150
Cdd:TIGR04523  295 SEISDLNNQKEQDwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISqlkkeltnseseNSEKQRELEEKQNEIEK 374

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 694958715  1151 LER-HQEKLEEKQAacLE-QIREMEKQF--QKEALAEYEARMKGLEAE 1194
Cdd:TIGR04523  375 LKKeNQSYKQEIKN--LEsQINDLESKIqnQEKLNQQKDEQIKKLQQE 420
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 1060-1195 7.73e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 38.52  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1060 RSRQGLSQEEQISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNshiqe 1139
Cdd:pfam11600    5 KSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDE----- 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 694958715  1140 vvqviKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAEV 1195
Cdd:pfam11600   80 -----KEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEI 130
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1098-1189 7.92e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 7.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1098 KEMKKKLETKRLERIQGMTKVT--TDKMAQERLKREINNSHIQEVVQVIKQMTEN----LERHQEKLEEKqaaclEQIRE 1171
Cdd:pfam13868   31 KKRIKAEEKEEERRLDEMMEEEreRALEEEEEKEEERKEERKRYRQELEEQIEEReqkrQEEYEEKLQER-----EQMDE 105

                           90
                   ....*....|....*...
gi 694958715  1172 MEKQFQKEALAEYEARMK 1189
Cdd:pfam13868  106 IVERIQEEDQAEAEEKLE 123
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1068-1198 8.94e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 8.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694958715  1068 EEQISKMMElaREKQaaeLKALKETSENDTKEMKKKLETKRleriQGMTKvttdkmaqERLKREINNSHiQEVVQvIKQM 1147
Cdd:TIGR04523  516 TKKISSLKE--KIEK---LESEKKEKESKISDLEDELNKDD----FELKK--------ENLEKEIDEKN-KEIEE-LKQT 576

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 694958715  1148 TENLERHQEKLEEKqaacleqIREMEKQFQ--KEALAEYEARMKGLEAEVKES 1198
Cdd:TIGR04523  577 QKSLKKKQEEKQEL-------IDQKEKEKKdlIKEIEEKEKKISSLEKELEKA 622
 
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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