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Conserved domains on  [gi|546232005|ref|NP_001271227|]
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1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 isoform 3 [Homo sapiens]

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: 561.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08624     1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08624    81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtaYEEMSSLV 550
Cdd:cd08624   155 ------------------------------------------------------------------------YEEMSSLV 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08624   163 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVAL 242

                         330
                  ....*....|....*....
gi 546232005  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 3.37e-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: 319.13  E-value: 3.37e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  149 DKILVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSY 228
Cdd:cd16209     1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546232005  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 ...
 963-1138 5.84e-91

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: 289.66  E-value: 5.84e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   963 GRVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLERIQG 1042
Cdd:pfam08703    1 KQVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1043 MTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAE 1122
Cdd:pfam08703   81 AKKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAE 160

                          170
                   ....*....|....*.
gi 546232005  1123 VKESVRACLRTCFPSE 1138
Cdd:pfam08703  161 VRESVKSCLKEGFPDE 176
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-141 6.82e-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: 226.49  E-value: 6.82e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005    12 KVKAYLSQGERFIKWDDETTVASP-VILRVDPKGYYLYWTYQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVFNMDFP 90
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 546232005    91 DNSFLLKTLTVVSGPDMVDLTFHNFVSYKENVGKAWAEDVLALVKHPLTAN 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 8.85e-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: 8.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  681 ATTLSITVISGQFLS------ERSVRTYVEVELFGLPGDPKRRYRTKLSPStNSINPVWkEEPFVFEKIlMPELASLRVA 754
Cdd:cd00275     1 PLTLTIKIISGQQLPkpkgdkGSIVDPYVEVEIHGLPADDSAKFKTKVVKN-NGFNPVW-NETFEFDVT-VPELAFLRFV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 546232005  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: 561.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08624     1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08624    81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtaYEEMSSLV 550
Cdd:cd08624   155 ------------------------------------------------------------------------YEEMSSLV 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08624   163 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVAL 242

                         330
                  ....*....|....*....
gi 546232005  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 3.37e-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: 319.13  E-value: 3.37e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  149 DKILVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSY 228
Cdd:cd16209     1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546232005  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 ...
 963-1138 5.84e-91

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: 289.66  E-value: 5.84e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   963 GRVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLERIQG 1042
Cdd:pfam08703    1 KQVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1043 MTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAE 1122
Cdd:pfam08703   81 AKKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAE 160

                          170
                   ....*....|....*.
gi 546232005  1123 VKESVRACLRTCFPSE 1138
Cdd:pfam08703  161 VRESVKSCLKEGFPDE 176
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 314-462 1.69e-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: 1.69e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   314 MTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIAE 393
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546232005   394 SAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKN 462
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLD----DDLTELPSPEDLKGKILIKG 142
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-141 6.82e-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: 226.49  E-value: 6.82e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005    12 KVKAYLSQGERFIKWDDETTVASP-VILRVDPKGYYLYWTYQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVFNMDFP 90
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 546232005    91 DNSFLLKTLTVVSGPDMVDLTFHNFVSYKENVGKAWAEDVLALVKHPLTAN 141
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 314-463 1.24e-64

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: 215.22  E-value: 1.24e-64
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005    314 MTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIAE 393
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDG--PDGEPVIYHGHTFTLPIKLSEVLEAIKD 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005    394 SAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKpgvpLPSPEDLRGKILIKNK 463
Cdd:smart00148   79 FAFVTSPYPVILSLENHC-SPDQQAKMAQMFKEIFGDMLYTPPLTSSLEV----LPSPEQLRGKILLKVR 143
PLN02228 PLN02228
Phosphoinositide phospholipase C
 217-786 1.11e-57

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 209.89  E-value: 1.11e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  217 PRPEIDEIFTSYHAKAKpyMTKEHLTKFINQKQRDSRlnsllfppARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLC 296
Cdd:PLN02228   22 PPVSIKRLFEAYSRNGK--MSFDELLRFVSEVQGERH--------AGLDYVQDIFHSVKHHNVFHHHGLVHLNAFYRYLF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  297 GPENSVLAQDKLLlHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKgKPPDEEPIITHGF 376
Cdd:PLN02228   92 SDTNSPLPMSGQV-HHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWP-NPSGNAAEVRHGR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  377 TMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLL---TEPLEKFplkpgvplPSPED 453
Cdd:PLN02228  170 TLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHL-PPNLQAQVAKMLTKTFRGMLFrctSESTKHF--------PSPEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  454 LRGKILIKNKKNQFSGPTSSSKDTggeaegssppSAPAGEGTVWAGEEGTeleeeeveeeeeeesgnldEEEIKKMQSDE 533
Cdd:PLN02228  241 LKNKILISTKPPKEYLESKTVQTT----------RTPTVKETSWKRVADA-------------------ENKILEEYKDE 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  534 GTAGLEvtaYEEMSSL--VNYIQPTKFVsfeFSAQKNRSYVIsSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMD 611
Cdd:PLN02228  292 ESEAVG---YRDLIAIhaANCKDPLKDC---LSDDPEKPIRV-SMDEQWLETMVRTRGTDLVRFTQRNLVRIYPKGTRVD 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  612 SSNYMPQMFWNAGCQMVALNFQT--MDLPMQQNMavFEFNGQSGYLLKHEFMRRPDKQFNPFSvdriDVVVATTLSITVI 689
Cdd:PLN02228  365 SSNYDPHVGWTHGAQMVAFNMQGhgKQLWIMQGM--FRANGGCGYVKKPRILLDEHTLFDPCK----RLPIKTTLKVKIY 438

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  690 SGQ----------FLSERSVRTYVEVELFGLPGDPKrRYRTKLspSTNSINPVWKEEPFVFEkILMPELASLRVAVME-- 757
Cdd:PLN02228  439 TGEgwdldfhlthFDQYSPPDFFVKIGIAGVPRDTV-SYRTET--AVDQWFPIWGNDEFLFQ-LRVPELALLWFKVQDyd 514

                         570       580       590
                  ....*....|....*....|....*....|.
gi 546232005  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 1.35e-55

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: 188.55  E-value: 1.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   17 LSQGERFIKWDDETTVASPVILRVDPKGYYLYWTYQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVfNMDFPDNSFLL 96
Cdd:cd13361     1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 546232005   97 KTLTVVSGPDMVDLTFHNFVSYKENVGKAWAEDVLALVKHPLTANASR 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 8.85e-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: 8.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  681 ATTLSITVISGQFLS------ERSVRTYVEVELFGLPGDPKRRYRTKLSPStNSINPVWkEEPFVFEKIlMPELASLRVA 754
Cdd:cd00275     1 PLTLTIKIISGQQLPkpkgdkGSIVDPYVEVEIHGLPADDSAKFKTKVVKN-NGFNPVW-NETFEFDVT-VPELAFLRFV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 546232005  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 6.98e-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: 6.98e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005    683 TLSITVISGQFLSER----SVRTYVEVELFGlpgDPKRRYRTKLSPSTNsiNPVWKEEpFVFEkILMPELASLRVAVMEE 758
Cdd:smart00239    1 TLTVKIISARNLPPKdkggKSDPYVKVSLDG---DPKEKKKTKVVKNTL--NPVWNET-FEFE-VPPPELAELEIEVYDK 73

                            90       100
                    ....*....|....*....|....*
gi 546232005    759 ----GNKFLGHRIIPINALNSGYHH 779
Cdd:smart00239   74 drfgRDDFIGQVTIPLSDLLLGGRH 98
C2 pfam00168
C2 domain;
683-776 3.70e-10

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 58.10  E-value: 3.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   683 TLSITVISGQFL----SERSVRTYVEVELfglpGDPKRRYRTKLSPstNSINPVWKEEpFVFEkILMPELASLRVAVMEE 758
Cdd:pfam00168    2 RLTVTVIEAKNLppkdGNGTSDPYVKVYL----LDGKQKKKTKVVK--NTLNPVWNET-FTFS-VPDPENAVLEIEVYDY 73

                           90       100
                   ....*....|....*....|..
gi 546232005   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 9.11e-09

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: 53.40  E-value: 9.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   215 LCPRPEIDEIFTSYhAKAKPYMTKEHLTKFINQKQRDSRlnsllfppARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWF 294
Cdd:pfam09279    5 LTQREEIDEIFQEY-SGDGQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAMTKDGFLMY 75


                   ....*....
gi 546232005   295 LCGPENSVL 303
Cdd:pfam09279   76 LCSPDGSIF 84
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
875-1125 4.21e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.30  E-value: 4.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  875 EELRELKGVVKLQRRHEKELRELERRgARRWEELlqrgAAQLAELGPPgvggvgacklgpgKGSRKKRSLPREESAGAAP 954
Cdd:PRK03918  204 EVLREINEISSELPELREELEKLEKE-VKELEEL----KEEIEELEKE-------------LESLEGSKRKLEEKIRELE 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  955 gEGPEGVDGRVRELKDRL-ELELLRQGEEQYECVLKRKEQHVAE--QISKMMELAREKQAAELKALKETS--ENDTKEMK 1029
Cdd:PRK03918  266 -ERIEELKKEIEELEEKVkELKELKEKAEEYIKLSEFYEEYLDElrEIEKRLSRLEEEINGIEERIKELEekEERLEELK 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1030 KKLET--KRLERIQGMTKVTTD---KMAQ-ERLKREINNSHIQEvvqvIKQMTENLERHQEKLEEKQAACLEQIREMEK- 1102
Cdd:PRK03918  345 KKLKEleKRLEELEERHELYEEakaKKEElERLKKRLTGLTPEK----LEKELEELEKAKEEIEEEISKITARIGELKKe 420

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 546232005 1103 ---------------------------QFQKEALAEYEARMKGLEAEVKE 1125
Cdd:PRK03918  421 ikelkkaieelkkakgkcpvcgrelteEHRKELLEEYTAELKRIEKELKE 470
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 964-1129 1.47e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  964 RVRELKDRLE----------LELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEMKKKLE 1033
Cdd:COG1196   214 RYRELKEELKeleaellllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1034 TKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAAcLEQIREMEKQfQKEALAEYE 1113
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE-LEEAEAELAE-AEEALLEAE 371

                         170
                  ....*....|....*.
gi 546232005 1114 ARMKGLEAEVKESVRA 1129
Cdd:COG1196   372 AELAEAEEELEELAEE 387
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 865-1170 2.19e-06

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: 52.37  E-value: 2.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   865 GSPEPRTASLEELRELKGVVKLQRRHEKELRELERRgARRWEELLQRGAAQLAELGPPGVGGVGacklgpgKGSRKKRSL 944
Cdd:TIGR02168  664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKA-LAELRKELEELEEELEQLRKELEELSR-------QISALRKDL 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   945 PREESAGAAPGEGPEGVDGRVRELKDRLELELLRQGEEQYEcvLKRKEQHVAEQISKMMELAREKQA---------AELK 1015
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE--LAEAEAEIEELEAQIEQLKEELKAlrealdelrAELT 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1016 ALKETSENDTKEMK-----KKLETKRLERIQGMTKVTTDKMA-----QERLKREINNSHIQ--EVVQVIKQMTENLERHQ 1083
Cdd:TIGR02168  814 LLNEEAANLRERLEslerrIAATERRLEDLEEQIEELSEDIEslaaeIEELEELIEELESEleALLNERASLEEALALLR 893

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1084 EKLEEKQaaclEQIREMEKQFQK---------EALAEYEARMKGLEAEVKEsvracLRTCFPSEAKDKPERACECPPELc 1154
Cdd:TIGR02168  894 SELEELS----EELRELESKRSElrreleelrEKLAQLELRLEGLEVRIDN-----LQERLSEEYSLTLEEAEALENKI- 963

                          330
                   ....*....|....*.
gi 546232005  1155 eqDPLIAKADAQESRL 1170
Cdd:TIGR02168  964 --EDDEEEARRRLKRL 977
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 979-1108 6.12e-04

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: 43.33  E-value: 6.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  979 QGEEQYECVLKRKEqHVAEQIskmmelarekqaaeLKALKETSENDTKEMKKKLETKRLERIQGMTKVttDKMAQERLKR 1058
Cdd:cd16269   167 KAEEVLQEFLQSKE-AEAEAI--------------LQADQALTEKEKEIEAERAKAEAAEQERKLLEE--QQRELEQKLE 229

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 546232005 1059 EINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACL-EQIREMEKQFQKEA 1108
Cdd:cd16269   230 DQERSYEEHLRQLKEKMEEERENLLKEQERALESKLkEQEALLEEGFKEQA 280
 
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: 561.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08624     1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08624    81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtaYEEMSSLV 550
Cdd:cd08624   155 ------------------------------------------------------------------------YEEMSSLV 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08624   163 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVAL 242

                         330
                  ....*....|....*....
gi 546232005  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: 545.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08591     1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVDSPrQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08591    81 IAETAFKTSEYPVILSFENHCSSK-QQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSLV 550
Cdd:cd08591   154 ---------------------------------------------------------------------------LSSLV 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08591   159 NYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQLSRIYPKGTRVDSSNYMPQIFWNAGCQMVAL 238

                         330
                  ....*....|....*....
gi 546232005  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 2.63e-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: 445.27  E-value: 2.63e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  313 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEAIA 392
Cdd:cd08625     3 DMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEAIA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  393 ESAFKTSPYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgpts 472
Cdd:cd08625    83 ESAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK-------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  473 sskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSLVNY 552
Cdd:cd08625   155 -------------------------------------------------------------------------MSTLVNY 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  553 IQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVALNF 632
Cdd:cd08625   162 IEPVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPMEFVEYNKKQLSRIYPKGTRVDSSNYMPQLFWNVGCQMVALNF 241

                         330
                  ....*....|....*..
gi 546232005  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 5.90e-136

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: 411.46  E-value: 5.90e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08558     1 YQDMTQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGHTLTSKILFKDVIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEKFPlkpgVPLPSPEDLRGKILIKNKKNQfsgp 470
Cdd:cd08558    79 IKEYAFVTSPYPVILSLENHC-SLEQQKKMAQILKEIFGDKLLTPPLDENP----VQLPSPEQLKGKILIKGKKYH---- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeemsslv 550
Cdd:cd08558       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  551 nyiqptkfvsfefsaqknrsyvISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08558   150 ----------------------MSSFSETKALKLLKESPEEFVKYNKRQLSRVYPKGTRVDSSNYNPQPFWNAGCQMVAL 207

                         330
                  ....*....|....*....
gi 546232005  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 5.36e-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: 402.54  E-value: 5.36e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  313 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEAIA 392
Cdd:cd08623     3 DMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  393 ESAFKTSPYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgpts 472
Cdd:cd08623    83 ECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKK-------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  473 sskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSLVNY 552
Cdd:cd08623   155 -------------------------------------------------------------------------MSNLVNY 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  553 IQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVALNF 632
Cdd:cd08623   162 IQPVKFESFEASKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNF 241

                         330
                  ....*....|....*..
gi 546232005  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 2.51e-131

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: 400.68  E-value: 2.51e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08626     1 YQDMDQPLAHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCIELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVDSPrQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08626    81 IKDTAFVTSDYPVILSFENHCSKP-QQYKLAKYCEEIFGDLLLTKPLESHPLEPGVPLPSPNKLKRKILIKNKR------ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSLV 550
Cdd:cd08626   154 ---------------------------------------------------------------------------LSSLV 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08626   159 NYAQPVKFQGFDVAEERNIHFNMSSFNESVGLGYLKTSAIEFVNYNKRQMSRIYPKGTRVDSSNYMPQIFWNAGCQMVSL 238

                         330
                  ....*....|....*....
gi 546232005  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 1.76e-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: 1.76e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08593     1 YQDMTQPLSHYFIASSHNTYLLEDQLKGPSSTEAYIRALKKGCRCVELDCWDG--PDGEPIIYHGHTLTSKILFKDVIQA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKNKKNQFSgp 470
Cdd:cd08593    79 IREYAFKVSPYPVILSLENHC-SVEQQKVMAQHLKSILGDKLLTQPLD----GVLTALPSPEELKGKILVKGKKLKLA-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSLV 550
Cdd:cd08593   152 -------------------------------------------------------------------------KELSDLV 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08593   159 IYCKSVHFKSFEHSKENYHFYEMSSFSESKALKLAQESGNEFVRHNKRQLSRIYPAGLRTDSSNYDPQEMWNVGCQIVAL 238

                         330
                  ....*....|....*....
gi 546232005  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08593   239 NFQTPGEEMDLNDGLFRQN 257
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 311-649 4.76e-111

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: 4.76e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFS-----GLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTtDIFFK 385
Cdd:cd00137     1 HHPDTQPLAHYSIPGTHDTYLTAGQFTikqvwGLTQTEMYRQQLLSGCRCVDIRCWDG--KPEEPIIYHGPTFL-DIFLK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  386 EAIEAIAESAFKTSPYPIILSFENHVDS-PRQQAKMAEYCRTIFGDMLLTeplekFPLKPGVPLPSPEDLRGKILIKNKK 464
Cdd:cd00137    78 EVIEAIAQFLKKNPPETIIMSLKNEVDSmDSFQAKMAEYCRTIFGDMLLT-----PPLKPTVPLPSLEDLRGKILLLNKK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  465 NQFSGPTSSSKDTGgeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtaye 544
Cdd:cd00137   153 NGFSGPTGSSNDTG------------------------------------------------------------------ 166

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  545 emsslvnyiqptkFVSFEFSAQKNRSYVISSFTELKAYD----LLSKASVQFVDYNKRQMSRIYPKGTR---------MD 611
Cdd:cd00137   167 -------------FVSFEFSTQKNRSYNISSQDEYKAYDdekvKLIKATVQFVDYNKNQLSRNYPSGTSggtawyyyaMD 233

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 546232005  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 3.37e-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: 319.13  E-value: 3.37e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  149 DKILVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSY 228
Cdd:cd16209     1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546232005  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 6.77e-92

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: 6.77e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08597     1 CQDMTQPLSHYFIASSHNTYLIEDQLRGPSSVEGYVRALQRGCRCVELDCWDG--PNGEPVIYHGHTLTSKISFRSVIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPlekfPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08597    79 INEYAFVASEYPLILCIENHC-SEKQQLVMAQYLKEIFGDKLYTEP----PNEGESYLPSPHDLKGKIIIKGKK------ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeIKKMQsdegtaglevtAYEEMSSLV 550
Cdd:cd08597   148 -------------------------------------------------------LKRRK-----------LCKELSDLV 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08597   162 SLCKSVRFQDFPTSAQNQKYWEVCSFSENLARRLANEFPEDFVNYNKKFLSRVYPSPMRVDSSNYNPQDFWNCGCQIVAM 241

                         330
                  ....*....|....*....
gi 546232005  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08597   242 NYQTPGLMMDLNTGKFLEN 260
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 963-1138 5.84e-91

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: 289.66  E-value: 5.84e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   963 GRVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLERIQG 1042
Cdd:pfam08703    1 KQVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1043 MTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAE 1122
Cdd:pfam08703   81 AKKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAE 160

                          170
                   ....*....|....*.
gi 546232005  1123 VKESVRACLRTCFPSE 1138
Cdd:pfam08703  161 VRESVKSCLKEGFPDE 176
PI-PLC1c_yeast cd08598
Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This ...
 312-646 2.96e-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: 2.96e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  312 HDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAI 391
Cdd:cd08598     2 EDLSRPLNEYFISSSHNTYLLGRQLAGDSSVEGYIRALQRGCRCVEIDVWDG--DDGEPVVTHGYTLTSSVPFRDVCRAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  392 AESAFKTSPYPIILSFENHVDsPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKpgvpLPSPEDLRGKILIKNKKNqfsgpt 471
Cdd:cd08598    80 KKYAFVTSPYPLILSLEVHCD-AEQQERMVEIMKETFGDLLVTEPLDGLEDE----LPSPEELRGKILIKVKKE------ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  472 ssskdtggeaegSSPPSApagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeemsslvn 551
Cdd:cd08598   149 ------------SKTPNH-------------------------------------------------------------- 154

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  552 yiqptkfvsfefsaqknrsyvISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVALN 631
Cdd:cd08598   155 ---------------------IFSLSERSLLKLLKDKRAALDKHNRRHLMRVYPSGTRISSSNFNPLPFWRAGVQMVALN 213

                         330
                  ....*....|....*
gi 546232005  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 7.28e-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: 283.16  E-value: 7.28e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  312 HDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAI 391
Cdd:cd08592     2 QDMNNPLSHYWIASSHNTYLTGDQLSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPIIYHGHTLTSKIKFMDVLKTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  392 AESAFKTSPYPIILSFENHVDSPrQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKNKKnqfsgpt 471
Cdd:cd08592    80 KEHAFVTSEYPVILSIENHCSLP-QQRNMAQAFKEVFGDMLLTQPVD----RNADQLPSPNQLKRKIIIKHKK------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  472 ssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMsslvn 551
Cdd:cd08592   148 ----------------------------------------------------------------------LFYEM----- 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  552 yiqptkfvsfefsaqknrsyviSSFTELKAYDLLSKA-SVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08592   153 ----------------------SSFPETKAEKYLNRQkGKIFLKYNRRQLSRVYPKGQRVDSSNYDPVPMWNCGSQMVAL 210

                         330
                  ....*....|....*....
gi 546232005  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 1.63e-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: 280.75  E-value: 1.63e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08630     1 FQDMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEG--PGGEPVIYHGHTLTSKILFRDVIQA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKpgvPLPSPEDLRGKILIKNKKNQFSgp 470
Cdd:cd08630    79 VRQHAFTASPYPVILSLENHC-GLEQQAAMARHLQTILGDMLVTQPLDSLNPE---ELPSPEELKGRVLVKGKKLQIS-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSLV 550
Cdd:cd08630   153 -------------------------------------------------------------------------PELSALA 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08630   160 VYCQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQEMWNSGCQLVAL 239

                         330
                  ....*....|....*....
gi 546232005  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 2.65e-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: 2.65e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKppDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08595     1 YQDMDHPLSDYFISSSHNTYLVSDQLVGPSDLDGYVSALRKGCRCLEIDCWDGA--DNEPVVYHGYTLTSKILFKEVITT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKpgvPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08595    79 VEKYAFEKSDYPVVLSLENHC-STEQQEIMAHYLVSILGEKLLRAPIDDPATG---ELPSPEALKFKILVKNKK------ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeEIKKMQSDegtaglevtayeemssLV 550
Cdd:cd08595   149 ------------------------------------------------------KIAKALSD----------------LV 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  551 NYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08595   159 IYTKSEKFCSFTHSRDNQHSYENNSIGENKARKLLKSSGADFVGHTQRFITRIYPKGTRASSSNYNPQEFWNVGCQMVAL 238

                         330
                  ....*....|....*....
gi 546232005  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 1.46e-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: 1.46e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08629     1 YQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDG--PNQEPIIYHGYTFTSKILFCDVLRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKNKKNQFSgp 470
Cdd:cd08629    79 IRDYAFKASPYPVILSLENHC-SLEQQRVMARHLRAILGPILLDQPLD----GVTTSLPSPEQLKGKILLKGKKLKLV-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSLV 550
Cdd:cd08629   152 -------------------------------------------------------------------------PELSDMI 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  551 NYIQPTKFVSFEFSAQKNRS-YVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVA 629
Cdd:cd08629   159 IYCKSVHFGGFSSPGTSGQAfYEMASFSESRALRLLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVA 238

                         330       340
                  ....*....|....*....|
gi 546232005  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 2.13e-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: 2.13e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08631     1 YQDMTQPLCHYFICSSHNTYLMEDQLRGQSSVEGYIRALKRGCRCVEVDVWDG--PNGEPIVYHGHTFTSKILFKDVVAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLE-KFPlkpgVPLPSPEDLRGKILIKNKKNQFSg 469
Cdd:cd08631    79 VAQYAFQVSDYPVILSLENHC-GVEQQQTMAQHLTEILGEKLLSTTLDgVLP----TQLPSPEELRGKILLKGKKIRLS- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  470 ptssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSL 549
Cdd:cd08631   153 --------------------------------------------------------------------------PELSDC 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  550 VNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVA 629
Cdd:cd08631   159 VIYCKSVSFRSFTHSREHYHFYEISSFTETKARKLIREAGNEFVQHNTWQLSRVYPSGLRTDSSNYNPQEMWNAGCQMVA 238

                         330       340
                  ....*....|....*....|
gi 546232005  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 2.32e-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: 263.63  E-value: 2.32e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  313 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKppDEEPIITHGFTMTTDIFFKEAIEAIA 392
Cdd:cd08596     3 DLQYPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLTGCRCVELDCWDGD--DGMPIIYHGHTLTTKIPFKDVVEAIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  393 ESAFKTSPYPIILSFENHVDSPrQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgpts 472
Cdd:cd08596    81 RSAFITSDYPVILSIENHCSLQ-QQRKMAEIFKTVFGEKLVTKFLFESDFSDDPSLPSPLQLKNKILLKNKK-------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  473 sskdtggeaegssppsAPagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeEMSSLVNY 552
Cdd:cd08596   152 ----------------AP------------------------------------------------------ELSDLVIY 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  553 IQPTKFVSFEFSaqknRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVALNF 632
Cdd:cd08596   162 CQAVKFPGLSTP----KCYHISSLNENAAKRLCRRYPQKLVQHTRCQLLRTYPAATRIDSSNPNPLIFWLHGLQLVALNY 237

                         330
                  ....*....|....*..
gi 546232005  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 1.69e-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: 1.69e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   314 MTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIAE 393
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546232005   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 8.08e-78

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: 8.08e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08594     1 NQDMTQPLSHYFIASSHNTYLTGDQLLSQSRVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKILFRDVIET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLtepLEKFPLKPGVPLPSPEDLRGKILIKNKKNQfsgp 470
Cdd:cd08594    79 INKYAFIKNEYPVILSIENHC-SVQQQKKMAQYLKEILGDKLD---LSSVISGDSKQLPSPQSLKGKILIKGKKWQ---- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeemsslv 550
Cdd:cd08594       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  551 nyiqptkfvsfefsaqknrsyvISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08594   151 ----------------------VSSFSETRAHQIVQQKAAQFLRFNQRQLSRIYPSAYRIDSSNFNPQPYWNAGCQLVAL 208

                         330
                  ....*....|....*....
gi 546232005  631 NFQTMDLPMQQNMAVFEFN 649
Cdd:cd08594   209 NYQTEGRMLQLNRAKFRAN 227
PI-PLCc_eta2 cd08633
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily ...
 311-649 4.70e-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: 4.70e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08633     1 NQDMTQPLSHYFITSSHNTYLSGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDG--PDGEPIVHHGYTLTSKILFKDVIET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVDSPrQQAKMAEYCRTIFGDMLltePLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08633    79 INKYAFIKNEYPVILSIENHCSVP-QQKKMAQYLTEILGDKL---DLSSVISNDCTRLPSPEILKGKILVKGKK------ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMSSLV 550
Cdd:cd08633   149 -----------------------------------------------------------------------LSRALSDLV 157

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  551 NYiqpTKFVSF-EFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVA 629
Cdd:cd08633   158 KY---TKSVRVhDIETEATSSWQVSSFSETKAHQILQQKPAQYLRFNQRQLSRIYPSSYRVDSSNYNPQPFWNAGCQMVA 234

                         330       340
                  ....*....|....*....|
gi 546232005  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 2.93e-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: 243.81  E-value: 2.93e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  313 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIA 392
Cdd:cd08628     3 DMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRMGCRCIELDCWDG--PDGKPIIYHGWTRTTKIKFDDVVQAIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  393 ESAFKTSPYPIILSFENHVDSpRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKNKKnqfsgpts 472
Cdd:cd08628    81 DHAFVTSEYPVILSIEEHCSV-EQQRHMAKVFKEVFGDKLLMKPLE----ASADQLPSPTQLKEKIIIKHKK-------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  473 sskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevTAYEEMSSLVNY 552
Cdd:cd08628   148 --------------------------------------------------------------------LIAIELSDLVVY 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  553 IQPTkfvSFEFSAQKNRSYV-ISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVALN 631
Cdd:cd08628   160 CKPT---SKTKDNLENPDFKeIRSFVETKAPSIIRQKPVQLLKYNRKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALN 236

                         330
                  ....*....|....*...
gi 546232005  632 FQTMDLPMQQNMAVFEFN 649
Cdd:cd08628   237 FQTADKYMQLNHALFSLN 254
PI-PLCc_eta1 cd08632
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily ...
 311-649 3.46e-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: 3.46e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08632     1 NQDMDQPLCNYFIASSHNTYLTGDQLLSQSKVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKITFRDVIET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDML-LTEPLEKFPLKpgvpLPSPEDLRGKILIKNKKnqfsg 469
Cdd:cd08632    79 INKYAFVKNEFPVILSIENHC-SIQQQKKIAQYLKEIFGDKLdLSSVLTGDPKQ----LPSPQLLKGKILVKGKK----- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  470 ptssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMSSL 549
Cdd:cd08632   149 ------------------------------------------------------------------------LCRDLSDL 156

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  550 VNYiqpTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVA 629
Cdd:cd08632   157 VVY---TNSVAAQDIVDDGSTGNVLSFSETRAHQLVQQKAEQFMTYNQKQLTRIYPSAYRIDSSNFNPLPYWNVGCQLVA 233

                         330       340
                  ....*....|....*....|
gi 546232005  630 LNFQTMDLPMQQNMAVFEFN 649
Cdd:cd08632   234 LNYQSEGRMMQLNRAKFMVN 253
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-141 6.82e-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: 226.49  E-value: 6.82e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005    12 KVKAYLSQGERFIKWDDETTVASP-VILRVDPKGYYLYWTYQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVFNMDFP 90
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 546232005    91 DNSFLLKTLTVVSGPDMVDLTFHNFVSYKENVGKAWAEDVLALVKHPLTAN 141
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
PI-PLCc_gamma1 cd08627
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily ...
 313-649 2.76e-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: 2.76e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  313 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIA 392
Cdd:cd08627     3 EMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPVIYHGHTLTTKIKFSDVLHTIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  393 ESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKNKKnqfsgpts 472
Cdd:cd08627    81 EHAFVTSEYPIILSIEDHC-SIVQQRNMAQHFKKVFGDMLLTKPVD----INADGLPSPNQLKRKILIKHKK-------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  473 sskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMsslvny 552
Cdd:cd08627   148 ---------------------------------------------------------------------LYRDM------ 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  553 iqptkfvsfefsaqknrsyviSSFTELKAYDLLSKAS-VQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVALN 631
Cdd:cd08627   153 ---------------------SSFPETKAEKYVNRSKgKKFLQYNRRQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALN 211

                         330
                  ....*....|....*...
gi 546232005  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 5.62e-65

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: 216.34  E-value: 5.62e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  149 DKILVKLKMQLNSEGKIPVKNFFQMFPAD--RKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFT 226
Cdd:cd16200     1 KKLYTKLKLSVNITGKIPVKNIIKCFSSDkkRKRVLKALKALGLPDGKNDEIDPEDFTFEKFFKLYNKLCPRPDIDEIFK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546232005  227 SYHAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16200    81 ELGGKRKPYLTLEQLVDFLNEEQRDPRLNEILFPFHTKEQAKKLIDKYEPNEKNKKKGQLTLEGFLRYLMSDE 153
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 314-463 1.24e-64

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: 215.22  E-value: 1.24e-64
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005    314 MTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIAE 393
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDG--PDGEPVIYHGHTFTLPIKLSEVLEAIKD 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005    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 2.66e-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: 210.17  E-value: 2.66e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005    547 SSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQ 626
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 546232005    627 MVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFM 661
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
PI-PLCc_plant cd08599
Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family ...
 311-649 7.04e-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: 204.91  E-value: 7.04e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDeePIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08599     1 HHDMTAPLSHYFIFSSHNSYLTGNQLSSRSSTAPIIEALLRGCRVIELDLWPGGRGD--ICVLHGGTLTKPVKFEDCIKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPlekfPLKPGVPLPSPEDLRGKILIKNKknqfsgp 470
Cdd:cd08599    79 IKENAFTASEYPVIITLENHL-SPELQAKAAQILRETLGDKLFYPD----SEDLPEEFPSPEELKGKILISDK------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  471 tssskdtggeaegssPPsapagegtvwageegteleeeeveeeeeEESGNLDEEEIKKMQSDEGTAGLevtayeemsslv 550
Cdd:cd08599   147 ---------------PP----------------------------VIRNSLSETQLKKVIEGEHPTDL------------ 171

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  551 nyiqptkfvsfefsaqknrsyvissftelkaydllskasvqfVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVAL 630
Cdd:cd08599   172 ------------------------------------------IEFTQKNLLRVYPAGLRITSSNYDPMLAWMHGAQMVAL 209

                         330
                  ....*....|....*....
gi 546232005  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 7.00e-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: 198.95  E-value: 7.00e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  149 DKILVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSY 228
Cdd:cd16208     1 EKAYTKLKLQVNPEGRIPVKNIYRLFSADRKRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDHIFSEF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546232005  229 HAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16208    81 GAKSKPYLSVDQMTEFINSKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSTLAKKGQISVDGFMRYLSGEE 151
PLN02228 PLN02228
Phosphoinositide phospholipase C
 217-786 1.11e-57

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 209.89  E-value: 1.11e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  217 PRPEIDEIFTSYHAKAKpyMTKEHLTKFINQKQRDSRlnsllfppARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLC 296
Cdd:PLN02228   22 PPVSIKRLFEAYSRNGK--MSFDELLRFVSEVQGERH--------AGLDYVQDIFHSVKHHNVFHHHGLVHLNAFYRYLF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  297 GPENSVLAQDKLLlHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKgKPPDEEPIITHGF 376
Cdd:PLN02228   92 SDTNSPLPMSGQV-HHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWP-NPSGNAAEVRHGR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  377 TMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLL---TEPLEKFplkpgvplPSPED 453
Cdd:PLN02228  170 TLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHL-PPNLQAQVAKMLTKTFRGMLFrctSESTKHF--------PSPEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  454 LRGKILIKNKKNQFSGPTSSSKDTggeaegssppSAPAGEGTVWAGEEGTeleeeeveeeeeeesgnldEEEIKKMQSDE 533
Cdd:PLN02228  241 LKNKILISTKPPKEYLESKTVQTT----------RTPTVKETSWKRVADA-------------------ENKILEEYKDE 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  534 GTAGLEvtaYEEMSSL--VNYIQPTKFVsfeFSAQKNRSYVIsSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMD 611
Cdd:PLN02228  292 ESEAVG---YRDLIAIhaANCKDPLKDC---LSDDPEKPIRV-SMDEQWLETMVRTRGTDLVRFTQRNLVRIYPKGTRVD 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  612 SSNYMPQMFWNAGCQMVALNFQT--MDLPMQQNMavFEFNGQSGYLLKHEFMRRPDKQFNPFSvdriDVVVATTLSITVI 689
Cdd:PLN02228  365 SSNYDPHVGWTHGAQMVAFNMQGhgKQLWIMQGM--FRANGGCGYVKKPRILLDEHTLFDPCK----RLPIKTTLKVKIY 438

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  690 SGQ----------FLSERSVRTYVEVELFGLPGDPKrRYRTKLspSTNSINPVWKEEPFVFEkILMPELASLRVAVME-- 757
Cdd:PLN02228  439 TGEgwdldfhlthFDQYSPPDFFVKIGIAGVPRDTV-SYRTET--AVDQWFPIWGNDEFLFQ-LRVPELALLWFKVQDyd 514

                         570       580       590
                  ....*....|....*....|....*....|.
gi 546232005  758 --EGNKFLGHRIIPINALNSGYHHLCLHSES 786
Cdd:PLN02228  515 ndTQNDFAGQTCLPLPELKSGVRAVRLHDRA 545
PLN02952 PLN02952
phosphoinositide phospholipase C
 310-783 1.41e-57

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 210.24  E-value: 1.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  310 LHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDeEPIITHGFTMTTDIFFKEAIE 389
Cdd:PLN02952  121 VHHDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGSTKD-EILVLHGRTLTTPVPLIKCLK 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  390 AIAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLteplekFPLKPG-VPLPSPEDLRGKILIKNKKnqfs 468
Cdd:PLN02952  200 SIRDYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLY------YPESDSlVQFPSPESLKHRIIISTKP---- 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  469 gPTSSSKDTGGEAEGSSPPSAPAGEGTvwageegteLEEEEVEEEEEEESGNLD-EEEIKKMQSDEGTAGLEVTAYEEMS 547
Cdd:PLN02952  269 -PKEYLESSGPIVIKKKNNVSPSGRNS---------SEETEEAQTLESMLFEQEaDSRSDSDQDDNKSGELQKPAYKRLI 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  548 SlVNYIQPTKFV--SFEFSAQKNRSYvisSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGC 625
Cdd:PLN02952  339 T-IHAGKPKGTLkdAMKVAVDKVRRL---SLSEQELEKAATTNGQDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGA 414

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  626 QMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFM--RRPDKQ-FNPfsvdRIDVVVATTLSITVISG----------Q 692
Cdd:PLN02952  415 QMIAFNMQGYGKSLWLMHGMFRANGGCGYLKKPDFLmkKGFHDEvFDP----KKKLPVKKTLKVKVYLGdgwrldfshtH 490

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  693 FLSERSVRTYVEVELFGLPGDPKRRyRTKLspSTNSINPVWKEEpFVFeKILMPELASLRVAV----MEEGNKFLGHRII 768
Cdd:PLN02952  491 FDSYSPPDFYTKMYIVGVPADNAKK-KTKI--IEDNWYPAWNEE-FSF-PLTVPELALLRIEVreydMSEKDDFGGQTCL 565

                         490
                  ....*....|....*
gi 546232005  769 PINALNSGYHHLCLH 783
Cdd:PLN02952  566 PVSELRPGIRSVPLH 580
PLN02222 PLN02222
phosphoinositide phospholipase C 2
 219-800 2.61e-57

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 209.12  E-value: 2.61e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  219 PEIDEIFTSYHAKAkpYMTKEHLTKFINQKQRDSRlnsllfppARPDQVQGLIDKyepSGINAQRGQLSPEGMVWFLCGP 298
Cdd:PLN02222   25 REIKTIFEKYSENG--VMTVDHLHRFLIDVQKQDK--------ATREDAQSIINS---ASSLLHRNGLHLDAFFKYLFGD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  299 ENSVLAQDKLllHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIItHGFTM 378
Cdd:PLN02222   92 NNPPLALHEV--HHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSDKDDIDVL-HGMTL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  379 TTDIFFKEAIEAIAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEP----LEKFPlkpgvplpSPEDL 454
Cdd:PLN02222  169 TTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHL-TPDLQSKVAEMVTEIFGEILFTPPvgesLKEFP--------SPNSL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  455 RGKILIKNKKNQfsgPTSSSKDTGGEAEGSSppsapAGEGTVWaGEEGTELEEEEVEEEEEEESGNLDEEEikkmqsDEG 534
Cdd:PLN02222  240 KKRIIISTKPPK---EYKEGKDDEVVQKGKD-----LGDEEVW-GREVPSFIQRNKSVDKNDSNGDDDDDD------DDG 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  535 TAGLEVTAYEEMSSLV--NYIQPTKFVS--FEFSAQKNRSYVISSFTELKAYDLLSKasvQFVDYNKRQMSRIYPKGTRM 610
Cdd:PLN02222  305 EDKSKKNAPPQYKHLIaiHAGKPKGGITecLKVDPDKVRRLSLSEEQLEKAAEKYAK---QIVRFTQHNLLRIYPKGTRV 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  611 DSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFMRRPDKQFNPFSvDRIDVVVATTLSITVIS 690
Cdd:PLN02222  382 TSSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKKPDLLLKSGSDSDIFD-PKATLPVKTTLRVTIYM 460

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  691 GQ----------FLSERSVRTYVEVELFGLPGDPKRRyRTKlSPSTNSInPVWKEepfVFE-KILMPELASLRVAV---- 755
Cdd:PLN02222  461 GEgwyfdfrhthFDQYSPPDFYTRVGIAGVPGDTVMK-KTK-TLEDNWI-PAWDE---VFEfPLTVPELALLRLEVheyd 534

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 546232005  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 1.01e-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: 191.52  E-value: 1.01e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   546 MSSLVNYIQPTKFVSFEfSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGC 625
Cdd:pfam00387    1 LSDLVVYTQSVKFKSFS-TPESKTPNHIFSFSESKALKLIKSSSAAFVKHNRRHLMRVYPKGTRVDSSNFNPQPFWNCGV 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 546232005   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 1.35e-55

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: 188.55  E-value: 1.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   17 LSQGERFIKWDDETTVASPVILRVDPKGYYLYWTYQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVfNMDFPDNSFLL 96
Cdd:cd13361     1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 546232005   97 KTLTVVSGPDMVDLTFHNFVSYKENVGKAWAEDVLALVKHPLTANASR 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 1.16e-49

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: 172.80  E-value: 1.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  150 KILVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSYH 229
Cdd:cd16210     2 KAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILLEIG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  230 AKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16210    82 AKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQVRQLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 151
PLN02230 PLN02230
phosphoinositide phospholipase C 4
 217-800 1.94e-48

phosphoinositide phospholipase C 4


Pssm-ID: 177875 [Multi-domain]  Cd Length: 598  Bit Score: 182.98  E-value: 1.94e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  217 PRPEIDEIFTSYhAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQV---QGLIDKYepsginaQRGQLSPEGMVW 293
Cdd:PLN02230   27 PVADVRDLFEKY-ADGDAHMSPEQLQKLMAEEGGGEGETSLEEAERIVDEVlrrKHHIAKF-------TRRNLTLDDFNY 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  294 FLCGPENSVLAQDKLllHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDeePIIT 373
Cdd:PLN02230   99 YLFSTDLNPPIADQV--HQNMDAPLSHYFIFTGHNSYLTGNQLSSNCSELPIADALRRGVRVVELDLWPRGTDD--VCVK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  374 HGFTMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLL---TEPLEKFPlkpgvplpS 450
Cdd:PLN02230  175 HGRTLTKEVKLGKCLDSIKANAFAISKYPVIITLEDHL-TPKLQFKVAKMITQTFGDMLYyhdSEGCQEFP--------S 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  451 PEDLRGKILIKNK--KNQFSGPTSSSKDTGGEAEGSsppsapagEGTVWAGEEGTELEEEEVEEEEEEESGNL--DEEEI 526
Cdd:PLN02230  246 PEELKEKILISTKppKEYLEANDAKEKDNGEKGKDS--------DEDVWGKEPEDLISTQSDLDKVTSSVNDLnqDDEER 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  527 KKMQSDEgTAGLEVTAYEEMSSlVNYIQPTKFVSFEFSAQKNRSYVISSftelkAYDLLSKASVQF----VDYNKRQMSR 602
Cdd:PLN02230  318 GSCESDT-SCQLQAPEYKRLIA-IHAGKPKGGLRMALKVDPNKIRRLSL-----SEQLLEKAVASYgadvIRFTQKNFLR 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  603 IYPKGTRMDSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFMRR---------PDKQFNPFSV 673
Cdd:PLN02230  391 IYPKGTRFNSSNYKPQIGWMSGAQMIAFNMQGYGRALWLMEGMFRANGGCGYVKKPDFLMDagpngqdfyPKDNSCPKKT 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  674 DRIDVVVATTLSITVISGQFLSERSVRTYVEVelfGLPGDPKRRYRTKLSPSTNSINPVWKEEpFVFeKILMPELASLRV 753
Cdd:PLN02230  471 LKVKVCMGDGWLLDFKKTHFDSYSPPDFFVRV---GIAGAPVDEVMEKTKIEYDTWTPIWNKE-FIF-PLAVPELALLRV 545

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 546232005  754 AVME----EGNKFLGHRIIPINALNSGYHHLCLHSESNMPLTMPALFIFLE 800
Cdd:PLN02230  546 EVHEhdinEKDDFGGQTCLPVSEIRQGIHAVPLFNRKGVKYSSTRLLMRFE 596
EFh_PI-PLC21 cd16213
EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family ...
 150-295 3.62e-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: 168.63  E-value: 3.62e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  150 KILVKLKMQLNSEGKIPVKNFFQMFPA---DRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFT 226
Cdd:cd16213     2 KAYTKLTLQTDKEGKIPVKNIVKMFAQhkdDRKRVEKALEAIGLPSGKNDAIDPKKFTFEDFFNFYRRLTGRQEVEKIFD 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546232005  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 8.85e-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: 8.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  681 ATTLSITVISGQFLS------ERSVRTYVEVELFGLPGDPKRRYRTKLSPStNSINPVWkEEPFVFEKIlMPELASLRVA 754
Cdd:cd00275     1 PLTLTIKIISGQQLPkpkgdkGSIVDPYVEVEIHGLPADDSAKFKTKVVKN-NGFNPVW-NETFEFDVT-VPELAFLRFV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 546232005  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 2.93e-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: 111.36  E-value: 2.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  154 KLKMQLNSEGKIPVKNFFQMFPADR--KRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSYHAK 231
Cdd:cd16211     6 RLCFLVNPNGKIPVRSITRTFASGKteKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFKKINGD 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 546232005  232 AKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFL 295
Cdd:cd16211    86 KKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYL 149
PLN02223 PLN02223
phosphoinositide phospholipase C
 311-791 1.06e-26

phosphoinositide phospholipase C


Pssm-ID: 165867 [Multi-domain]  Cd Length: 537  Bit Score: 116.28  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  311 HHDMTQPLNHYFINSSHNTYLTAGQ-FSGLSSAEMYRQVLLSGCRCVELDCWkgkPPDEEPI-ITHGFTMTTDIFFKEAI 388
Cdd:PLN02223  105 HHDMHAPLSHYFIHTSLKSYFTGNNvFGKLYSIEPIIDALEQGVRVVELDLL---PDGKDGIcVRPKWNFEKPLELQECL 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  389 EAIAESAF-KTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTE----PLEKFplkpgvplPSPEDLRGKILIKNK 463
Cdd:PLN02223  182 DAIKEHAFtKCRSYPLIITFKDGL-KPDLQSKATQMIDQTFGDMVYHEdpqhSLEEF--------PSPAELQNKILISRR 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  464 knqfsgptssskdtggeaegssPPS----APAGEGTVwageegteleeeeveeeeeeesGNLDEEEIKKMQSDEGtagle 539
Cdd:PLN02223  253 ----------------------PPKellyAKADDGGV----------------------GVRNELEIQEGPADKN----- 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  540 vtaYEEMSSLvNYIQPTKFVSFEFSAQKNRSYVISSFTElkayDLLSKASVQFVDYN-KRQMSRIYPKgtrmdssnYMPQ 618
Cdd:PLN02223  284 ---YQSLVGF-HAVEPRGMLQKALTGKADDIQQPGWYER----DIISFTQKKFLRTRpKKKNLLINAP--------YKPQ 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  619 MFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFMRR--PDKQFNPfsvdRIDVVVATTLSITVISGQF--- 693
Cdd:PLN02223  348 RAWMHGAQLIALSRKDDKEKLWLMQGMFRANGGCGYVKKPDFLLNagPSGVFYP----TENPVVVKILKVKIYMGDGwiv 423

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  694 -LSERSVR-----TYVEVELFGLPGDPKrryRTKLSPSTNSINPVWKEEpFVFeKILMPELASLRVAV----MEEGNKFL 763
Cdd:PLN02223  424 dFKKRIGRlskpdLYVRISIAGVPHDEK---IMKTTVKNNEWKPTWGEE-FTF-PLTYPDLALISFEVydyeVSTADAFC 498

                         490       500       510
                  ....*....|....*....|....*....|....
gi 546232005  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 2.00e-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: 2.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  324 NSSHNTYLTAGQfsgLSSAEMYRQVLLSGCRCVELDCWKGKppDEEPIITHGFTMT------TDIFFKEAIEAIAESAFk 397
Cdd:cd08555     1 VLSHRGYSQNGQ---ENTLEAFYRALDAGARGLELDVRLTK--DGELVVYHGPTLDrttagiLPPTLEEVLELIADYLK- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  398 TSPYPIILSFENHVDS---PRQQAKMAEYCRTIFGDmllteplekfplkpgvplpspeDLRGKILIKnkknqfsgptsss 474
Cdd:cd08555    75 NPDYTIILSLEIKQDSpeyDEFLAKVLKELRVYFDY----------------------DLRGKVVLS------------- 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  475 kdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeemsslvnyiq 554
Cdd:cd08555       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546232005  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 2.67e-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: 97.23  E-value: 2.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  153 VKLKMQLNSEGKIPVKNFFQMFPADR--KRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSYHA 230
Cdd:cd16212     5 MRLGFMVDSGGKIPVKHIARTFASGKteKLVYQCLAEMGLPSGKGDSIEKEDFTFEKFYALYHKICPRNDIEELFTSITK 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546232005  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 6.98e-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: 6.98e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005    683 TLSITVISGQFLSER----SVRTYVEVELFGlpgDPKRRYRTKLSPSTNsiNPVWKEEpFVFEkILMPELASLRVAVMEE 758
Cdd:smart00239    1 TLTVKIISARNLPPKdkggKSDPYVKVSLDG---DPKEKKKTKVVKNTL--NPVWNET-FEFE-VPPPELAELEIEVYDK 73

                            90       100
                    ....*....|....*....|....*
gi 546232005    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 1.06e-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: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  195 NDAINPEDFPEpvyksFLMSLCPRPEIDEIFTSYhAKAKPYMTKEHLTKFINQKQRdsrlnsllFPPARPDQVQGLIDKY 274
Cdd:cd16202    50 EDVLDEEEFVQ-----FYNRLTKRPEIEELFKKY-SGDDEALTVEELRRFLQEEQK--------VKDVTLEWAEQLIETY 115

                          90       100
                  ....*....|....*....|....*
gi 546232005  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 2.52e-11

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: 62.30  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  155 LKMQLNSEGKIPVKNFFQM-----FPADRKRVEAALSACHlpKGKNDAINPEDFpepvyKSFLMSLCPRPEIDEIFTSYH 229
Cdd:cd15898     7 IKADKDGDGKLSLKEIKKLlkrlnIRVSEKELKKLFKEVD--TNGDGTLTFDEF-----EELYKSLTERPELEPIFKKYA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  230 AKAKPYMTKEHLTKFINQKQRDSRlnsllfppaRPDQVQGLIDKYEPSGinaQRGQLSPEGMVWFLCGPE 299
Cdd:cd15898    80 GTNRDYMTLEEFIRFLREEQGENV---------SEEECEELIEKYEPER---ENRQLSFEGFTNFLLSPE 137
C2 pfam00168
C2 domain;
683-776 3.70e-10

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 58.10  E-value: 3.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   683 TLSITVISGQFL----SERSVRTYVEVELfglpGDPKRRYRTKLSPstNSINPVWKEEpFVFEkILMPELASLRVAVMEE 758
Cdd:pfam00168    2 RLTVTVIEAKNLppkdGNGTSDPYVKVYL----LDGKQKKKTKVVK--NTLNPVWNET-FTFS-VPDPENAVLEIEVYDY 73

                           90       100
                   ....*....|....*....|..
gi 546232005   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 9.11e-09

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: 53.40  E-value: 9.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   215 LCPRPEIDEIFTSYhAKAKPYMTKEHLTKFINQKQRDSRlnsllfppARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWF 294
Cdd:pfam09279    5 LTQREEIDEIFQEY-SGDGQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAMTKDGFLMY 75


                   ....*....
gi 546232005   295 LCGPENSVL 303
Cdd:pfam09279   76 LCSPDGSIF 84
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
875-1125 4.21e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.30  E-value: 4.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  875 EELRELKGVVKLQRRHEKELRELERRgARRWEELlqrgAAQLAELGPPgvggvgacklgpgKGSRKKRSLPREESAGAAP 954
Cdd:PRK03918  204 EVLREINEISSELPELREELEKLEKE-VKELEEL----KEEIEELEKE-------------LESLEGSKRKLEEKIRELE 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  955 gEGPEGVDGRVRELKDRL-ELELLRQGEEQYECVLKRKEQHVAE--QISKMMELAREKQAAELKALKETS--ENDTKEMK 1029
Cdd:PRK03918  266 -ERIEELKKEIEELEEKVkELKELKEKAEEYIKLSEFYEEYLDElrEIEKRLSRLEEEINGIEERIKELEekEERLEELK 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1030 KKLET--KRLERIQGMTKVTTD---KMAQ-ERLKREINNSHIQEvvqvIKQMTENLERHQEKLEEKQAACLEQIREMEK- 1102
Cdd:PRK03918  345 KKLKEleKRLEELEERHELYEEakaKKEElERLKKRLTGLTPEK----LEKELEELEKAKEEIEEEISKITARIGELKKe 420

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 546232005 1103 ---------------------------QFQKEALAEYEARMKGLEAEVKE 1125
Cdd:PRK03918  421 ikelkkaieelkkakgkcpvcgrelteEHRKELLEEYTAELKRIEKELKE 470
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 868-1114 6.95e-07

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: 53.59  E-value: 6.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   868 EPRTASLEELRELKGVVKLQRrhekeLRELERrgarrweelLQRGAAQLAELGPPGVGGVGACKLGPGKGSRKKRSLPRE 947
Cdd:pfam17380  356 EERKRELERIRQEEIAMEISR-----MRELER---------LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   948 ESAGAAPGEGPEGVDGRVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQ----AAELKAL---KET 1020
Cdd:pfam17380  422 MEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRdrkrAEEQRRKileKEL 501

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1021 SENDTK----EMKKKLETKRLE-RIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTEnlERHQEKLEEKQAACLE 1095
Cdd:pfam17380  502 EERKQAmieeERKRKLLEKEMEeRQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE--ERSRLEAMEREREMMR 579

                          250
                   ....*....|....*....
gi 546232005  1096 QIREMEKQFQkealaEYEA 1114
Cdd:pfam17380  580 QIVESEKARA-----EYEA 593
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 684-773 7.30e-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: 7.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  684 LSITVISGQFL----SERSVRTYVEVELfglpgDPKRRYRTKLSPstNSINPVWKEEpFVFEkILMPELASLRVAVMEE- 758
Cdd:cd00030     1 LRVTVIEARNLpakdLNGKSDPYVKVSL-----GGKQKFKTKVVK--NTLNPVWNET-FEFP-VLDPESDTLTVEVWDKd 71

                          90
                  ....*....|....*...
gi 546232005  759 ---GNKFLGHRIIPINAL 773
Cdd:cd00030    72 rfsKDDFLGEVEIPLSEL 89
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 973-1131 1.05e-06

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: 53.20  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   973 ELELLRQGEEQYECVLKRKEQhVAEQISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLERIQgmtkvtTDKMA 1052
Cdd:pfam17380  349 ELERIRQEERKRELERIRQEE-IAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQ------QQKVE 421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1053 QERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAAcLEQIR-----------EMEKQFQKEALAEyEARMKGLEA 1121
Cdd:pfam17380  422 MEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQ-VERLRqqeeerkrkklELEKEKRDRKRAE-EQRRKILEK 499

                          170
                   ....*....|
gi 546232005  1122 EVKESVRACL 1131
Cdd:pfam17380  500 ELEERKQAMI 509
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 964-1129 1.47e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  964 RVRELKDRLE----------LELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEMKKKLE 1033
Cdd:COG1196   214 RYRELKEELKeleaellllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1034 TKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAAcLEQIREMEKQfQKEALAEYE 1113
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE-LEEAEAELAE-AEEALLEAE 371

                         170
                  ....*....|....*.
gi 546232005 1114 ARMKGLEAEVKESVRA 1129
Cdd:COG1196   372 AELAEAEEELEELAEE 387
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 865-1170 2.19e-06

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: 52.37  E-value: 2.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   865 GSPEPRTASLEELRELKGVVKLQRRHEKELRELERRgARRWEELLQRGAAQLAELGPPGVGGVGacklgpgKGSRKKRSL 944
Cdd:TIGR02168  664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKA-LAELRKELEELEEELEQLRKELEELSR-------QISALRKDL 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   945 PREESAGAAPGEGPEGVDGRVRELKDRLELELLRQGEEQYEcvLKRKEQHVAEQISKMMELAREKQA---------AELK 1015
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE--LAEAEAEIEELEAQIEQLKEELKAlrealdelrAELT 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1016 ALKETSENDTKEMK-----KKLETKRLERIQGMTKVTTDKMA-----QERLKREINNSHIQ--EVVQVIKQMTENLERHQ 1083
Cdd:TIGR02168  814 LLNEEAANLRERLEslerrIAATERRLEDLEEQIEELSEDIEslaaeIEELEELIEELESEleALLNERASLEEALALLR 893

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1084 EKLEEKQaaclEQIREMEKQFQK---------EALAEYEARMKGLEAEVKEsvracLRTCFPSEAKDKPERACECPPELc 1154
Cdd:TIGR02168  894 SELEELS----EELRELESKRSElrreleelrEKLAQLELRLEGLEVRIDN-----LQERLSEEYSLTLEEAEALENKI- 963

                          330
                   ....*....|....*.
gi 546232005  1155 eqDPLIAKADAQESRL 1170
Cdd:TIGR02168  964 --EDDEEEARRRLKRL 977
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
 209-299 2.52e-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: 48.20  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  209 KSFLMSLCPRPEIDEIFTSYhAKAKPYMTKEHLTKFINQKQRDsrlnsllfpPARPDQVQGLIDKYEPSGINAQRGQLSP 288
Cdd:cd16217    59 EEFYKLLTKREEIDVIFGEY-AKSDGTMSRNNLLNFLQEEQRE---------EVAPAYALSLIEKYEPDETAKAQRQMTK 128

                          90
                  ....*....|.
gi 546232005  289 EGMVWFLCGPE 299
Cdd:cd16217   129 DGFLMYLLSPE 139
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 965-1126 3.00e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 51.90  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   965 VRELKDRLELELLRQGEEQYECVL--KRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLERIQG 1042
Cdd:pfam02463  203 KEQAKKALEYYQLKEKLELEEEYLlyLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1043 MTKVTTDKMA-------QERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEAR 1115
Cdd:pfam02463  283 LQEEELKLLAkeeeelkSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE 362

                          170
                   ....*....|.
gi 546232005  1116 MKGLEAEVKES 1126
Cdd:pfam02463  363 KLQEKLEQLEE 373
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 967-1166 5.24e-06

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: 50.53  E-value: 5.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   967 ELKDRLELELLRQGEEQYEcvlkrKEQHVAEQISKMMELAREKQAAELKA-LKETSENDTKEMKKKLETKrLERiqgmtk 1045
Cdd:pfam09731  305 ELKKREEKHIERALEKQKE-----ELDKLAEELSARLEEVRAADEAQLRLeFEREREEIRESYEEKLRTE-LER------ 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1046 vtTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEAR-MKGLEAEVk 1124
Cdd:pfam09731  373 --QAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNELLANLKGLEKATSSHSEVEDENRkAQQLWLAV- 449

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 546232005  1125 ESVRACLRTCFPSEAKDKPERACECPPELCEQDPLIAKADAQ 1166
Cdd:pfam09731  450 EALRSTLEDGSADSRPRPLVRELKALKELASDDEVVKAALAS 491
PTZ00121 PTZ00121
MAEBL; Provisional
 875-1145 8.81e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 8.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  875 EELRELKGVVKLQ--RRHEKELRELERR--GARRWEELLQRGAAQLAELGppgvggvgacKLGPGKGSRKKRSLPREESA 950
Cdd:PTZ00121 1549 DELKKAEELKKAEekKKAEEAKKAEEDKnmALRKAEEAKKAEEARIEEVM----------KLYEEEKKMKAEEAKKAEEA 1618

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  951 gaapgegpegvdgrvrelkdRLELELLRQGEEQYECVLKRKEQHvAEQISKMMELAREKQAAELKAlKETSENDTKEMKK 1030
Cdd:PTZ00121 1619 --------------------KIKAEELKKAEEEKKKVEQLKKKE-AEEKKKAEELKKAEEENKIKA-AEEAKKAEEDKKK 1676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1031 KLETKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEALA 1110
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 546232005 1111 EYEARMKGLEAEVKESVRACLRTCFPSEAKDKPER 1145
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEK 1791
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
868-1125 2.61e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  868 EPRTASLEELRELK----GVVKLQRRHEKELRELERRGARrWEELLQRGAAQLAELGPPGVggvgacKLGPGKGSRK--K 941
Cdd:PRK03918  279 EEKVKELKELKEKAeeyiKLSEFYEEYLDELREIEKRLSR-LEEEINGIEERIKELEEKEE------RLEELKKKLKelE 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  942 RSLPR-EESAGAApgEGPEGVDGRVRELKDRLELELLRQGEEQYECVLKRKEQhVAEQISKMMEL---------AREKQA 1011
Cdd:PRK03918  352 KRLEElEERHELY--EEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE-IEEEISKITARigelkkeikELKKAI 428

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1012 AELKALK--------ETSENDTKEMKKKLeTKRLERIQGMTKVTTDKMAQ-ERLKREINNS-HIQEVVQVIKQMTENLER 1081
Cdd:PRK03918  429 EELKKAKgkcpvcgrELTEEHRKELLEEY-TAELKRIEKELKEIEEKERKlRKELRELEKVlKKESELIKLKELAEQLKE 507

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 546232005 1082 HQEKLEEKQaacLEQIREMEKQFQ--KEALAEYEARMKGLEAEVKE 1125
Cdd:PRK03918  508 LEEKLKKYN---LEELEKKAEEYEklKEKLIKLKGEIKSLKKELEK 550
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 993-1127 3.28e-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: 3.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   993 QHVAEQISKMMELAREKQAAELKALKETSENDTKEMKKKLEtKRLERIQGMTKVTTDKMaQERLKREInnSHIQEVV-QV 1071
Cdd:pfam01442   25 QELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLG-QNVEELRQRLEPYTEEL-RKRLNADA--EELQEKLaPY 100

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546232005  1072 IKQMTENLERHQEKLEEKQAACLEQIRE-MEKQFQ------KEALAEYEARMKGLEAEVKESV 1127
Cdd:pfam01442  101 GEELRERLEQNVDALRARLAPYAEELRQkLAERLEelkeslAPYAEEVQAQLSQRLQELREKL 163
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 973-1121 3.90e-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: 46.19  E-value: 3.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   973 ELELLRQGEEQYECVlkrkEQHVAEQISKMMELAREKQAAELKALKETSENDTK---------EMKKKLEtkrlERIQGM 1043
Cdd:pfam15665   48 ELDLKRRIQTLEESL----EQHERMKRQALTEFEQYKRRVEERELKAEAEHRQRvvelsreveEAKRAFE----EKLESF 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1044 TKVTTdKMAQERLK-----REINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREME---KQFQKEALAEYEAR 1115
Cdd:pfam15665  120 EQLQA-QFEQEKRKaleelRAKHRQEIQELLTTQRAQSASSLAEQEKLEELHKAELESLRKEVedlRKEKKKLAEEYEQK 198


                   ....*.
gi 546232005  1116 MKGLEA 1121
Cdd:pfam15665  199 LSKAQA 204
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
872-1122 4.06e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  872 ASLEELRE------LKGVVKL-QRRHEKELReleRRGARRW------EELLQRGAAQLAELGPPGVGGVGACKlgpgKGS 938
Cdd:COG4913   565 DSPEELRRhpraitRAGQVKGnGTRHEKDDR---RRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLE----ALE 637

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  939 RKKRSLPREESAGAAPGEGPE------GVDGRVRELKDRLE--------LELLRQGEEQYECVLKRKEQHVAEQISKMME 1004
Cdd:COG4913   638 AELDALQERREALQRLAEYSWdeidvaSAEREIAELEAELErldassddLAALEEQLEELEAELEELEEELDELKGEIGR 717

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1005 LAREKQAA--ELKALKEtsendtkemkkkletkRLERIQGMTKVTTDKMAQERLKREINNshiqevvQVIKQMTENLERH 1082
Cdd:COG4913   718 LEKELEQAeeELDELQD----------------RLEAAEDLARLELRALLEERFAAALGD-------AVERELRENLEER 774

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 546232005 1083 QEKLEEKQAACLEQIREMEKQFQK-------------EALAEYEARMKGLEAE 1122
Cdd:COG4913   775 IDALRARLNRAEEELERAMRAFNRewpaetadldadlESLPEYLALLDRLEED 827
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 875-1114 4.34e-05

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: 47.76  E-value: 4.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   875 EELRELKGVVklqRRHEKELRELERRGARR------WEELLQRGAAQLAELGPPGVGGVGACKLGPGKGSRKKRSLPREE 948
Cdd:TIGR02169  798 AELSKLEEEV---SRIEARLREIEQKLNRLtlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   949 SAGAAPGEGPEGVDGRVRELKDrlELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQA--AELKALKETSENDTK 1026
Cdd:TIGR02169  875 AALRDLESRLGDLKKERDELEA--QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEieDPKGEDEEIPEEELS 952

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1027 EMKKKLETKRLERiqgmtkvttDKMAQErlkrEINNSHIQEVVQVIKQMTEnLERHQEKLEEKQAACLEQIREMEKQFQK 1106
Cdd:TIGR02169  953 LEDVQAELQRVEE---------EIRALE----PVNMLAIQEYEEVLKRLDE-LKEKRAKLEEERKAILERIEEYEKKKRE 1018


                   ....*...
gi 546232005  1107 EALAEYEA 1114
Cdd:TIGR02169 1019 VFMEAFEA 1026
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 961-1125 5.38e-05

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: 46.07  E-value: 5.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  961 VDGRVRELKDRLElELLRQgeeqyecvLKRKEQHVAEQISKMMELarEKQAAELKALKETSENDTKEMKKKLetKRLERI 1040
Cdd:COG1579    15 LDSELDRLEHRLK-ELPAE--------LAELEDELAALEARLEAA--KTELEDLEKEIKRLELEIEEVEARI--KKYEEQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1041 QGMtkVTTDKMAQ------ERLKREIN--NSHIQEVVQVIKQMTENLERHQEKLEEKQaaclEQIREMEKQFQkEALAEY 1112
Cdd:COG1579    82 LGN--VRNNKEYEalqkeiESLKRRISdlEDEILELMERIEELEEELAELEAELAELE----AELEEKKAELD-EELAEL 154

                         170
                  ....*....|...
gi 546232005 1113 EARMKGLEAEVKE 1125
Cdd:COG1579   155 EAELEELEAEREE 167
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 966-1120 9.18e-05

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: 46.07  E-value: 9.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   966 RELKDRLELELLRQ--GEEQYECVLKRKEQHVAEQISKMMEL---AREKQAAELKALKETSENDTKEMKKKL--ETKRLE 1038
Cdd:pfam13868  195 KAQDEKAERDELRAklYQEEQERKERQKEREEAEKKARQRQElqqAREEQIELKERRLAEEAEREEEEFERMlrKQAEDE 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1039 RIqgmtkvttDKMAQERlKREINNSHIQEVVQVIKqmtenlERHQEKLEEKQAACLEQIREMEKQFQKEALAEyEARMKG 1118
Cdd:pfam13868  275 EI--------EQEEAEK-RRMKRLEHRRELEKQIE------EREEQRAAEREEELEEGERLREEEAERRERIE-EERQKK 338


                   ..
gi 546232005  1119 LE 1120
Cdd:pfam13868  339 LK 340
PRK12704 PRK12704
phosphodiesterase; Provisional
 977-1125 9.23e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 9.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  977 LRQGEEQYECVLK--RKEqhvAEQISKMMEL-AREkqaaELKALKETSENDTKEMKKKLEtKRLERIQgmtkvttdkMAQ 1053
Cdd:PRK12704   33 IKEAEEEAKRILEeaKKE---AEAIKKEALLeAKE----EIHKLRNEFEKELRERRNELQ-KLEKRLL---------QKE 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546232005 1054 ERLKREINNshIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEA-LAEYEAR---MKGLEAEVKE 1125
Cdd:PRK12704   96 ENLDRKLEL--LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgLTAEEAKeilLEKVEEEARH 169
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
864-1125 9.96e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 9.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  864 NGSPEPRTASLEELreLKGVVKLQRRHEKELRELERRgARRWEELlqRGAAQ----LAELGPPGVGGVGACKLGPGKGSR 939
Cdd:PRK03918  247 LESLEGSKRKLEEK--IRELEERIEELKKEIEELEEK-VKELKEL--KEKAEeyikLSEFYEEYLDELREIEKRLSRLEE 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  940 KKRSLPREESAGAAPGEGPEGVDGRVRELKDRLELelLRQGEEQYECVLKRKEQhvAEQISKMME-LAREKQAAELKALK 1018
Cdd:PRK03918  322 EINGIEERIKELEEKEERLEELKKKLKELEKRLEE--LEERHELYEEAKAKKEE--LERLKKRLTgLTPEKLEKELEELE 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1019 ETSENDTKEMKK------KLETKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAA 1092
Cdd:PRK03918  398 KAKEEIEEEISKitarigELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERK 477

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 546232005 1093 CLEQIREMEKQFQKE----ALAEYEARMKGLEAEVKE 1125
Cdd:PRK03918  478 LRKELRELEKVLKKEseliKLKELAEQLKELEEKLKK 514
EFh_PI-PLCdelta4 cd16219
EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, ...
 211-299 1.15e-04

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: 43.29  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  211 FLMSLCPRPEIDEIFTSYHAKAKPyMTKEHLTKFINQKQRDsrlnsllfPPARPDQVQGLIDKYEPSGINAQRGQLSPEG 290
Cdd:cd16219    61 FYKALTQREDVLKIFQDFSADGQK-LTLLEFVDFLQQEQLE--------RENTEELAMELIDRYEPSDTAKKLHALSIDG 131


                  ....*....
gi 546232005  291 MVWFLCGPE 299
Cdd:cd16219   132 FLMYLCSPE 140
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 875-1125 1.38e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  875 EELRELKGVVKLQRRHEKELR-ELERRGARRWEELLQRGAAQLAELGppgvggvgacklgpGKGSRKKRSLPREESAGAA 953
Cdd:COG1196   220 EELKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELE--------------AELEELRLELEELELELEE 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  954 pgegpegVDGRVRELKDRLElellrQGEEQYECVLKRKEQHVAEQISKMMELAREK-QAAELKALKETSENDTKEMKKKL 1032
Cdd:COG1196   286 -------AQAEEYELLAELA-----RLEQDIARLEERRRELEERLEELEEELAELEeELEELEEELEELEEELEEAEEEL 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1033 ETKRLERIQGMTKVTTDKMAQERLKREINN-----SHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKE 1107
Cdd:COG1196   354 EEAEAELAEAEEALLEAEAELAEAEEELEElaeelLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433

                         250
                  ....*....|....*...
gi 546232005 1108 ALAEYEARMKGLEAEVKE 1125
Cdd:COG1196   434 EEEEEEEEEALEEAAEEE 451
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 964-1125 1.65e-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: 45.29  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   964 RVRELKDRLELELLRQgeeqyecvlKRKEQHVAEQISKMMELAREKQAAELKALKETS----------ENDTKEMKKKLE 1033
Cdd:pfam13868   53 RERALEEEEEKEEERK---------EERKRYRQELEEQIEEREQKRQEEYEEKLQEREqmdeiveriqEEDQAEAEEKLE 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1034 TKRLERiQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENL--------------ERHQEKLEEKQAACLEQIRE 1099
Cdd:pfam13868  124 KQRQLR-EEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREeereaereeieeekEREIARLRAQQEKAQDEKAE 202

                          170       180
                   ....*....|....*....|....*.
gi 546232005  1100 MEKQFQKEALAEYEARMKGLEAEVKE 1125
Cdd:pfam13868  203 RDELRAKLYQEEQERKERQKEREEAE 228
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 859-1125 1.65e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 46.12  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   859 LAPTSNGSPEPRTASLE-ELRELKGVVK-LQRRHEKELRELERRGAR-RWEELLQRGAAQLAELGPPGVGGVGAcklgpg 935
Cdd:TIGR00618  209 CTPCMPDTYHERKQVLEkELKHLREALQqTQQSHAYLTQKREAQEEQlKKQQLLKQLRARIEELRAQEAVLEET------ 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   936 kgsRKKRSLPREESAGAAPGEGPEGVDGRVRE----------------------LKDRLELELLRQGEEQY--ECVLKRK 991
Cdd:TIGR00618  283 ---QERINRARKAAPLAAHIKAVTQIEQQAQRihtelqskmrsrakllmkraahVKQQSSIEEQRRLLQTLhsQEIHIRD 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   992 EQHVA----EQISKMME-------LAREKQAAE-----LKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQER 1055
Cdd:TIGR00618  360 AHEVAtsirEISCQQHTltqhihtLQQQKTTLTqklqsLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRY 439

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1056 LkrEINNSHIQEVVQVIKQMTENLERHQEKLEEKQaacleqiremEKQFQKEALAEYEARMKGLEAEVKE 1125
Cdd:TIGR00618  440 A--ELCAAAITCTAQCEKLEKIHLQESAQSLKERE----------QQLQTKEQIHLQETRKKAVVLARLL 497
PTZ00121 PTZ00121
MAEBL; Provisional
 875-1148 1.76e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  875 EELR---ELKGVVKLQRRHEKELRELERRgARRWEELLQRGAAQLAELGPPGVGGVGACKLGPGKGSRKKRSLPREESAG 951
Cdd:PTZ00121 1480 EEAKkadEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  952 AApgEGPEGVDGRVRELKDRLELelLRQGEEqyecvLKRKEQHVAEQISKMMELAREKQAAELKalKETSENDTKEMKKK 1031
Cdd:PTZ00121 1559 KA--EEKKKAEEAKKAEEDKNMA--LRKAEE-----AKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKAEELKK 1627

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1032 LETKRLERIQGMTKVTTDKMAQERLKREINNSHIQEvVQVIKQMTENLERHQE--KLEEKQAACLEQI-REMEKQFQKEA 1108
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA-AEEAKKAEEDKKKAEEakKAEEDEKKAAEALkKEAEEAKKAEE 1706

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 546232005 1109 LAEYEARMKGLEAEVK--ESVRACLRTCFPSEAKDKPERACE 1148
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKkaEEENKIKAEEAKKEAEEDKKKAEE 1748
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 312-460 2.25e-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: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  312 HDMTQPLNHYFINSSHNTY-LTAGQFSGLSSA-----EMY-RQVLLSGCRCVELDCWKgKPPDEEPIITHGFTMTTDIFF 384
Cdd:cd08557     3 LLDDLPLSQLSIPGTHNSYaYTIDGNSPIVSKwsktqDLSiTDQLDAGVRYLDLRVAY-DPDDGDLYVCHGLFLLNGQTL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  385 KEAIEAIAesAF-KTSPY-PIILSFENHV--DSPRQQAKMAEYCRTIFGDMLLTeplekfPLKPGVPLPSPEDLR-GKIL 459
Cdd:cd08557    82 EDVLNEVK--DFlDAHPSeVVILDLEHEYggDNGEDHDELDALLRDVLGDPLYR------PPVRAGGWPTLGELRaGKRV 153


                  .
gi 546232005  460 I 460
Cdd:cd08557   154 L 154
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 964-1092 2.58e-04

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: 41.83  E-value: 2.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   964 RVRELKDRLELEL-LRQGEEQyecvLKRKEQHVAEQISKMMELAREKQAAELkalkETSENDTKEMKKKLETKRLERIQG 1042
Cdd:pfam20492    1 REEAEREKQELEErLKQYEEE----TKKAQEELEESEETAEELEEERRQAEE----EAERLEQKRQEAEEEKERLEESAE 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 546232005  1043 MTKVTTDKMAQERLKREinnSHIQEVVQVIKQMTENLERHQEKLEEKQAA 1092
Cdd:pfam20492   73 MEAEEKEQLEAELAEAQ---EEIARLEEEVERKEEEARRLQEELEEAREE 119
PTZ00121 PTZ00121
MAEBL; Provisional
 875-1169 3.79e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 3.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  875 EELRELKGVVKLQ--RRHEKELRELERRGA---------RRWEELLQRGA-AQLAELGPPGVGGVGACKLGPGKGSRKKR 942
Cdd:PTZ00121 1191 EELRKAEDARKAEaaRKAEEERKAEEARKAedakkaeavKKAEEAKKDAEeAKKAEEERNNEEIRKFEEARMAHFARRQA 1270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  943 SLPREESAGAApgegpegvdgRVRELKDRLELELLRQGEEQYEC-VLKRKeqhvAEQISKMMELarEKQAAELKALKETS 1021
Cdd:PTZ00121 1271 AIKAEEARKAD----------ELKKAEEKKKADEAKKAEEKKKAdEAKKK----AEEAKKADEA--KKKAEEAKKKADAA 1334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1022 ENDTKEMKKKLETKR---------LERIQGMTKVTTDKMAQERLKREINNSHIQEVVQViKQMTENLERHQEKLEE--KQ 1090
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKaeaeaaadeAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADElkKA 1413

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546232005 1091 AACLEQIREMEKQFQKEALAEyEARMKGLEAEVKESVRAclrtcfPSEAKDKPERACECPPELCEQDPliAKADAQESR 1169
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKAD-EAKKKAEEAKKADEAKK------KAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAK 1483
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
959-1127 5.47e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 5.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  959 EGVDGRVRELKD-RLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKAlkETSENDTKEMKKKLETKRL 1037
Cdd:COG4372    31 EQLRKALFELDKlQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL--QAAQAELAQAQEELESLQE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1038 ERIQgmTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMK 1117
Cdd:COG4372   109 EAEE--LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186

                         170
                  ....*....|
gi 546232005 1118 GLEAEVKESV 1127
Cdd:COG4372   187 ELLKEANRNA 196
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 886-1121 5.59e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 5.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  886 LQRRHEKELRELERRGARRWEELLQRGAAQLAELGPPGVggvgacklgpgkgsrKKRSLPREESAGAAPGEGPEGVDGRV 965
Cdd:COG1196   544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI---------------RARAALAAALARGAIGAAVDLVASDL 608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  966 RELK-----------------DRLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEM 1028
Cdd:COG1196   609 READaryyvlgdtllgrtlvaARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1029 KKKLETKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEA 1108
Cdd:COG1196   689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768

                         250
                  ....*....|...
gi 546232005 1109 LAEYEARMKGLEA 1121
Cdd:COG1196   769 LERLEREIEALGP 781
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 979-1108 6.12e-04

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: 43.33  E-value: 6.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  979 QGEEQYECVLKRKEqHVAEQIskmmelarekqaaeLKALKETSENDTKEMKKKLETKRLERIQGMTKVttDKMAQERLKR 1058
Cdd:cd16269   167 KAEEVLQEFLQSKE-AEAEAI--------------LQADQALTEKEKEIEAERAKAEAAEQERKLLEE--QQRELEQKLE 229

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 546232005 1059 EINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACL-EQIREMEKQFQKEA 1108
Cdd:cd16269   230 DQERSYEEHLRQLKEKMEEERENLLKEQERALESKLkEQEALLEEGFKEQA 280
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 684-776 6.78e-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: 40.81  E-value: 6.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  684 LSITVISGQFLSER--SVRTYVEVELfglpGDPKRRYRTklSPSTNSINPVWkEEPFVFEkiLMPELASLRVAVMEEG-- 759
Cdd:cd08678     1 LLVKNIKANGLSEAagSSNPYCVLEM----DEPPQKYQS--STQKNTSNPFW-DEHFLFE--LSPNSKELLFEVYDNGkk 71

                          90
                  ....*....|....*....
gi 546232005  760 --NKFLGHRIIPINALNSG 776
Cdd:cd08678    72 sdSKFLGLAIVPFDELRKN 90
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 939-1119 6.97e-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: 6.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  939 RKKRSLPREESAgaapgegpegVDGRVRELKDRLELELLRQGEEQYEcvLKRKEQHVaEQISKMMELAREKQAA-----E 1013
Cdd:COG1579    24 HRLKELPAELAE----------LEDELAALEARLEAAKTELEDLEKE--IKRLELEI-EEVEARIKKYEEQLGNvrnnkE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1014 LKALKETSENDTKEmKKKLETKRLERiqgMTKVTTDKMAQERLKREInnshiQEVVQVIKQMTENLERHQEKLEEKQAAC 1093
Cdd:COG1579    91 YEALQKEIESLKRR-ISDLEDEILEL---MERIEELEEELAELEAEL-----AELEAELEEKKAELDEELAELEAELEEL 161

                         170       180
                  ....*....|....*....|....*....
gi 546232005 1094 LEQIREMEKQFQKEALAEYE---ARMKGL 1119
Cdd:COG1579   162 EAEREELAAKIPPELLALYErirKRKNGL 190
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
860-1146 7.50e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 7.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  860 APTSNGSPEPRTASL-EELRELKGVVKlqrRHEKELRELERRgARRWEELLQRGaaQLAELGPPGVGGVGACKLGPGKGS 938
Cdd:PRK02224  403 APVDLGNAEDFLEELrEERDELREREA---ELEATLRTARER-VEEAEALLEAG--KCPECGQPVEGSPHVETIEEDRER 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  939 RKKRSLPREESAgaapgEGPEGVDGRVRELKDRLELEL-LRQGEEQYECVLKRKEQH---VAEQISKMMELarEKQAAEL 1014
Cdd:PRK02224  477 VEELEAELEDLE-----EEVEEVEERLERAEDLVEAEDrIERLEERREDLEELIAERretIEEKRERAEEL--RERAAEL 549

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1015 KALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKReinnshIQEVVQVIKQMTENLERHQEKLEEKQaacl 1094
Cdd:PRK02224  550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER------IRTLLAAIADAEDEIERLREKREALA---- 619

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 546232005 1095 eqirEMEKQfQKEALAEYEARMKGLEAEVKESvraclRTcfpSEAKDKPERA 1146
Cdd:PRK02224  620 ----ELNDE-RRERLAEKRERKRELEAEFDEA-----RI---EEAREDKERA 658
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 969-1121 7.86e-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: 43.89  E-value: 7.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   969 KDRLELELLRQgEEQYECVLKRKEQHVAEQISKMMEL-AREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVT 1047
Cdd:TIGR02168  332 LDELAEELAEL-EEKLEELKEELESLEAELEELEAELeELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1048 TDKMAQERLKREIN--------------NSHIQEVVQVIKQMTENLERHQEKLEEKQAAcLEQIREMEKQFQKEaLAEYE 1113
Cdd:TIGR02168  411 RLEDRRERLQQEIEellkkleeaelkelQAELEELEEELEELQEELERLEEALEELREE-LEEAEQALDAAERE-LAQLQ 488


                   ....*...
gi 546232005  1114 ARMKGLEA 1121
Cdd:TIGR02168  489 ARLDSLER 496
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 684-779 7.97e-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: 40.64  E-value: 7.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  684 LSITVISGQFLSERSVR----TYVEVELFGlpgDPKRRYRTKLSPSTNSINPVWKEEpFVFEkilMP----ELASLRVAV 755
Cdd:cd00276    16 LTVVVLKARNLPPSDGKglsdPYVKVSLLQ---GGKKLKKKKTSVKKGTLNPVFNEA-FSFD---VPaeqlEEVSLVITV 88

                          90       100
                  ....*....|....*....|....*...
gi 546232005  756 MEEG----NKFLGHRIIPINALNSGYHH 779
Cdd:cd00276    89 VDKDsvgrNEVIGQVVLGPDSGGEELEH 116
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
 202-295 8.46e-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: 41.08  E-value: 8.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  202 DFPEpvYKSFLMSLCPRPEIDEIFTSYHAKAKPYMTKEHLTKFINQKQRDSRlnsllfppaRPDQVQGLIDKYEPSGINA 281
Cdd:cd16207    56 NFEE--FQEFVKLLKRRKDIKAIFKQLTKPGSDGLTLEEFLKFLRDVQKEDV---------DRETWEKIFEKFARRIDDS 124

                          90
                  ....*....|....
gi 546232005  282 QRGQLSPEGMVWFL 295
Cdd:cd16207   125 DSLTMTLEGFTSFL 138
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 870-1129 8.69e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 8.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  870 RTASLEELRELKGVVKLQRRHEKELRELERRGARRwEELLQRGAAQLAELgppgvggvgacklgpgkgSRKKRSLpREES 949
Cdd:COG1196   273 RLELEELELELEEAQAEEYELLAELARLEQDIARL-EERRRELEERLEEL------------------EEELAEL-EEEL 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  950 AGAApgegpegvdgrvrELKDRLELELLRQGEEQYEcvLKRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEMK 1029
Cdd:COG1196   333 EELE-------------EELEELEEELEEAEEELEE--AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1030 KKLETKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEAL 1109
Cdd:COG1196   398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477

                         250       260
                  ....*....|....*....|
gi 546232005 1110 AEYEARMKGLEAEVKESVRA 1129
Cdd:COG1196   478 ALAELLEELAEAAARLLLLL 497
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
 715-779 8.77e-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: 40.51  E-value: 8.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 546232005  715 KRRYRTklSPSTNSINPVWKEE-PFVFEKILM--PELASLRVAVMEEGN----KFLGHRIIPINALNSGYHH 779
Cdd:cd08682    30 KEKYST--SVKEKTTSPVWKEEcSFELPGLLSgnGNRATLQLTVMHRNLlgldKFLGQVSIPLNDLDEDKGR 99
PRK00106 PRK00106
ribonuclease Y;
964-1125 1.09e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 42.93  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  964 RVRELKDRLELELLRQgeEQYECVLKRKEQHVAEQISKMMElaREKQAAELKALKETSENDTK---EMKKKLETKRLERI 1040
Cdd:PRK00106   25 KMKSAKEAAELTLLNA--EQEAVNLRGKAERDAEHIKKTAK--RESKALKKELLLEAKEEARKyreEIEQEFKSERQELK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1041 QGMTKVTTDKMAQERLKREINNSH--IQEVVQVIKQMTENL-ERHQE--KLEEKQAACLEQIREMEKQFQKEA-LAEYE- 1113
Cdd:PRK00106  101 QIESRLTERATSLDRKDENLSSKEktLESKEQSLTDKSKHIdEREEQveKLEEQKKAELERVAALSQAEAREIiLAETEn 180

                         170
                  ....*....|....*....
gi 546232005 1114 -------ARMKGLEAEVKE 1125
Cdd:PRK00106  181 kltheiaTRIREAEREVKD 199
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 875-1129 1.31e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 42.33  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   875 EELRELKGVVKLqrRHEKELRELERRGARRWE-ELLQRGAAQLAELGPpgvggvgacklgpgKGSRKKRSLPREESAGAA 953
Cdd:pfam15558   35 EELRRRDQKRQE--TLERERRLLLQQSQEQWQaEKEQRKARLGREERR--------------RADRREKQVIEKESRWRE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   954 PGEGPEGvdGRVRELKD-RLELELLRQGEEQYecvLKRKE---QHVAEQISKMMeLAREKQAAELKALKETsendtKEMK 1029
Cdd:pfam15558   99 QAEDQEN--QRQEKLERaRQEAEQRKQCQEQR---LKEKEeelQALREQNSLQL-QERLEEACHKRQLKER-----EEQK 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1030 KKLETKRLERIQ-GMTKVTTDKMAQE-----RLKREINNSHIQEVVQvikQMTEnlERHQEkLEEKqaacleqIREMEKQ 1103
Cdd:pfam15558  168 KVQENNLSELLNhQARKVLVDCQAKAeellrRLSLEQSLQRSQENYE---QLVE--ERHRE-LREK-------AQKEEEQ 234

                          250       260
                   ....*....|....*....|....*....
gi 546232005  1104 FQKEALAEYEA---RMKGLEAEVKESVRA 1129
Cdd:pfam15558  235 FQRAKWRAEEKeeeRQEHKEALAELADRK 263
PRK12704 PRK12704
phosphodiesterase; Provisional
 1005-1125 1.34e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1005 LAREKQA-AELKALKETSENDTKEMKKKLET-KRLERIQGMTKVTTDKMAQERLKREINNsHIQEVVQVIKQMTENLERH 1082
Cdd:PRK12704   23 FVRKKIAeAKIKEAEEEAKRILEEAKKEAEAiKKEALLEAKEEIHKLRNEFEKELRERRN-ELQKLEKRLLQKEENLDRK 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 546232005 1083 QEKLEEKQAACLEQIREMEKqfQKEALAEYEARMKGLEAEVKE 1125
Cdd:PRK12704  102 LELLEKREEELEKKEKELEQ--KQQELEKKEEELEELIEEQLQ 142
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 963-1125 1.46e-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: 43.12  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   963 GRVRELKDRLE-----LELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAA--ELKALKetSENDTKEMKKKLETK 1035
Cdd:TIGR02168  232 LRLEELREELEelqeeLKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELqkELYALA--NEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1036 RLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKqaacleqirEMEKQFQKEALAEYEAR 1115
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL---------EAELEELESRLEELEEQ 380

                          170
                   ....*....|
gi 546232005  1116 MKGLEAEVKE 1125
Cdd:TIGR02168  381 LETLRSKVAQ 390
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 962-1122 1.66e-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: 42.21  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   962 DGRVRE-LKDRLELELLRQGEEQyecVLKRKEQHVAEQISKMMELAREKQAA--ELKALKETSENDTKEMKKKLET--KR 1036
Cdd:pfam13868  154 DERILEyLKEKAEREEEREAERE---EIEEEKEREIARLRAQQEKAQDEKAErdELRAKLYQEEQERKERQKEREEaeKK 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1037 LERIQGMTKVTTDKMAQERLKREI--------NNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEA 1108
Cdd:pfam13868  231 ARQRQELQQAREEQIELKERRLAEeaereeeeFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAER 310

                          170
                   ....*....|....
gi 546232005  1109 LAEYEARMKGLEAE 1122
Cdd:pfam13868  311 EEELEEGERLREEE 324
EFh_PRIP cd16206
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ...
 197-299 1.67e-03

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: 39.89  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  197 AINPEDFPEpVYKSflmsLCPRPEIDEIFTSYhAKAKPYMTKEHLTKFINQKQRDSRLNsllfpparPDQVQGLIDKYEP 276
Cdd:cd16206    55 RVSSDEFVE-LFKE----LATRPEIYFLLVRY-ASNKDYLTVDDLMLFLEAEQGMTGVT--------KEKCLEIINKYEP 120

                          90       100
                  ....*....|....*....|...
gi 546232005  277 SGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16206   121 SEEGREKGQLGIDGFTRYLLSEE 143
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 874-1145 1.86e-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: 42.75  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   874 LEELRELKGVVKLQRR--HEKELRELERRGARRWEELLQRgAAQLAELGppgvggvgacklgpgkgsrkKRSLPREESAG 951
Cdd:TIGR02169  217 LKEKREYEGYELLKEKeaLERQKEAIERQLASLEEELEKL-TEEISELE--------------------KRLEEIEQLLE 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   952 AAPGEGPEGVDGRVRELKDRL-----ELELLRQGEEQYEcvlkRKEQHVAEQISKMmELAREKQAAELKALKEtsendtk 1026
Cdd:TIGR02169  276 ELNKKIKDLGEEEQLRVKEKIgeleaEIASLERSIAEKE----RELEDAEERLAKL-EAEIDKLLAEIEELER------- 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1027 emkkKLETKRLERIQGMTKVTTDKMAQERLKREInnshiQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREM-----E 1101
Cdd:TIGR02169  344 ----EIEEERKRRDKLTEEYAELKEELEDLRAEL-----EEVDKEFAETRDELKDYREKLEKLKREINELKRELdrlqeE 414

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 546232005  1102 KQFQKEALAEYEARMKGLEAEVKEsvraclrtcFPSEAKDKPER 1145
Cdd:TIGR02169  415 LQRLSEELADLNAAIAGIEAKINE---------LEEEKEDKALE 449
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 862-1120 2.45e-03

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: 42.08  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   862 TSNGSPEPRTASLEELRELKGVVKLQ-RRHEKELRELERRGARRWEELlqrgAAQLAELGppgvggvgacklgpgkgsRK 940
Cdd:pfam01576  314 TTAAQQELRSKREQEVTELKKALEEEtRSHEAQLQEMRQKHTQALEEL----TEQLEQAK------------------RN 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   941 KRSLPREESAgaapgegpegVDGRVRELKdrLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKET 1020
Cdd:pfam01576  372 KANLEKAKQA----------LESENAELQ--AELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ 439

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1021 SENDT-KEMKKKLETKRLERIQGMTKVT-----TDKMAQERLKREINNSH-----------IQEVVQVIKQMTENLERH- 1082
Cdd:pfam01576  440 SELESvSSLLNEAEGKNIKLSKDVSSLEsqlqdTQELLQEETRQKLNLSTrlrqledernsLQEQLEEEEEAKRNVERQl 519

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 546232005  1083 ----------QEKLEEkQAACLEQIREMEKQFQKEA------LAEYEARMKGLE 1120
Cdd:pfam01576  520 stlqaqlsdmKKKLEE-DAGTLEALEEGKKRLQRELealtqqLEEKAAAYDKLE 572
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
963-1125 2.55e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  963 GRVRELKDRLElELLRQGEEQYECV--LKRKEQHVAEQISKMMELAREKQaaELKALKETSENDTKEMKKKLEtkRLERI 1040
Cdd:COG1340    50 AQVKELREEAQ-ELREKRDELNEKVkeLKEERDELNEKLNELREELDELR--KELAELNKAGGSIDKLRKEIE--RLEWR 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1041 QgMTKVTTdkmaqerLKREInnshiqEVVQVIKQMTENLERHQEKLEEKqaaclEQIREMEKQFQ--KEALAEYEARMKG 1118
Cdd:COG1340   125 Q-QTEVLS-------PEEEK------ELVEKIKELEKELEKAKKALEKN-----EKLKELRAELKelRKEAEEIHKKIKE 185


                  ....*..
gi 546232005 1119 LEAEVKE 1125
Cdd:COG1340   186 LAEEAQE 192
PTZ00121 PTZ00121
MAEBL; Provisional
 940-1128 2.75e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  940 KKRSLPREESAGAAPGEGPEGVDgRVRELKDRLELELLRQGEEQYEC-VLKRKEQHV--AEQISKMMElAREKQAAELKA 1016
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAAD-EAEAAEEKAEAAEKKKEEAKKKAdAAKKKAEEKkkADEAKKKAE-EDKKKADELKK 1412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1017 lKETSENDTKEMKKKLETKRleRIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAAC-LE 1095
Cdd:PTZ00121 1413 -AAAAKKKADEAKKKAEEKK--KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADeAK 1489

                         170       180       190
                  ....*....|....*....|....*....|...
gi 546232005 1096 QIREMEKQFQKEALAEYEARMKGLEAEVKESVR 1128
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
869-1059 2.91e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  869 PRTASLEELRELKGVVKLQRRHEKELRELERRgARRWEELLQRGAAQLAELGPPGVGGVGACKLGP--GKGSRKKRSLpr 946
Cdd:COG4717    65 KPELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAEL-- 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  947 eesagaapgegpEGVDGRVRELKDRLE-----LELLRQGEEQYEcVLKRKEQHVAEQISKMMELAREKQAAELKAL---K 1018
Cdd:COG4717   142 ------------AELPERLEELEERLEelrelEEELEELEAELA-ELQEELEELLEQLSLATEEELQDLAEELEELqqrL 208

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 546232005 1019 ETSENDTKEMKKKLETKRlERIQGMTKVTTDKMAQERLKRE 1059
Cdd:COG4717   209 AELEEELEEAQEELEELE-EELEQLENELEAAALEERLKEA 248
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 976-1130 2.97e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 2.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   976 LLRQGEeqYECVLKRKEQHVAEQISKMMELAREKQ-AAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQE 1054
Cdd:TIGR00618  148 LLPQGE--FAQFLKAKSKEKKELLMNLFPLDQYTQlALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLE 225

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546232005  1055 RLKReinnsHIQEVVQVIKQMTENLERHQEKLEEK---QAACLEQIREMEkqfqkealaEYEARMKGLEAEVKESVRAC 1130
Cdd:TIGR00618  226 KELK-----HLREALQQTQQSHAYLTQKREAQEEQlkkQQLLKQLRARIE---------ELRAQEAVLEETQERINRAR 290
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 947-1134 3.81e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.42  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   947 EESAGAAPGEGPEGVDGRVRELKDRLElellrqgeeqyECvlkRKEQHVAEQISKMMELAREKQAAELKALKETSENDTK 1026
Cdd:pfam07888   11 EESHGEEGGTDMLLVVPRAELLQNRLE-----------EC---LQERAELLQAQEAANRQREKEKERYKRDREQWERQRR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1027 EMKKKLEtkRLERIQGMTKVTTDKMAQERLKREINNSHI-QEVVQVIKQMTENLERHQEkLEEKQAACLEQIREME---- 1101
Cdd:pfam07888   77 ELESRVA--ELKEELRQSREKHEELEEKYKELSASSEELsEEKDALLAQRAAHEARIRE-LEEDIKTLTQRVLEREtele 153

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 546232005  1102 --KQFQKEALA---EYEARMKGLEAEVKESVRACLRTC 1134
Cdd:pfam07888  154 rmKERAKKAGAqrkEEEAERKQLQAKLQQTEEELRSLS 191
APP_E2 pfam12925
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ...
 1014-1156 4.63e-03

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: 39.63  E-value: 4.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1014 LKALKETSENDT-KEMKKKLETKRLERiqgMTKVTTD-KMAQERLKrEINNSHIQEVVQVIKQMTENLERHQEKLEEKQA 1091
Cdd:pfam12925   14 FEHPDPRNEHESfKKAKKRLEEKHRER---MTKVMKEwEEAEERYQ-NLPKADPKAAEKFKKAMTARFQETVEALEEEAA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1092 ACLEQIREMEKQF--------QKEALAEYearMKGLEAEVK--ESVRACLRTCFPSEAKDKP------ERACECPPELCE 1155
Cdd:pfam12925   90 AERQQLVETHQQRveahlndrRRDALECY---LQALQENPPnpHRILKALKKLLRAEQKDRRhtlrhyRHLLASDPEKAE 166


                   .
gi 546232005  1156 Q 1156
Cdd:pfam12925  167 Q 167
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 988-1125 5.66e-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: 40.29  E-value: 5.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   988 LKRKEQHVAEQISKMMELAREKQAAEL----KALKETSENDTKEMKKKLETKRLERIqgmtkvttdkMAQERLKREinns 1063
Cdd:pfam13868   34 IKAEEKEEERRLDEMMEEERERALEEEeekeEERKEERKRYRQELEEQIEEREQKRQ----------EEYEEKLQE---- 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546232005  1064 hIQEVVQVIKQMTENLERHQEKLEEKQAACLEQI----------REMEKQFQKEA---LAEY----EARMKGLEAEVKE 1125
Cdd:pfam13868  100 -REQMDEIVERIQEEDQAEAEEKLEKQRQLREEIdefneeqaewKELEKEEEREEderILEYlkekAEREEEREAEREE 177
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 960-1127 6.17e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.59  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  960 GVDGRVRELKDRLE--LELLRQGEeqyecvLKR---KEQHVAEQISKMMELARekqaAELKAlketsENDTKEMKKKLeT 1034
Cdd:PRK04778  253 DIEKEIQDLKEQIDenLALLEELD------LDEaeeKNEEIQERIDQLYDILE----REVKA-----RKYVEKNSDTL-P 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1035 KRLERIQGMTKVTTDKMaqERLKR--EINNSHIQEVVQV---IKQMTENLERHQEKLEEKQAA----------CLEQIRE 1099
Cdd:PRK04778  317 DFLEHAKEQNKELKEEI--DRVKQsyTLNESELESVRQLekqLESLEKQYDEITERIAEQEIAyselqeeleeILKQLEE 394

                         170       180
                  ....*....|....*....|....*...
gi 546232005 1100 MEKQfQKEaLAEYEARMKGLEAEVKESV 1127
Cdd:PRK04778  395 IEKE-QEK-LSEMLQGLRKDELEAREKL 420
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 684-758 6.30e-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: 38.01  E-value: 6.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  684 LSITVISGQFLSERSVRT----YVEVELfglPGDPKRRYRTKLSPstNSINPVWKEEpfvFEKILMPELAS-LRVAVMEE 758
Cdd:cd04036     2 LTVRVLRATNITKGDLLStpdcYVELWL---PTASDEKKRTKTIK--NSINPVWNET---FEFRIQSQVKNvLELTVMDE 73
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 966-1126 7.74e-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: 7.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   966 RELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKmmelaREKQAAELKALKETSE--NDTKEMKKKLETKRLERI-QG 1042
Cdd:pfam13868   86 EQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEK-----LEKQRQLREEIDEFNEeqAEWKELEKEEEREEDERIlEY 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1043 MTKVTTDKMAQERLKREInnshIQEVVQVIKQMTENLERHQEKLEEKQAACLE-QIREMEKQFQKEALAEYEARMKgLEA 1121
Cdd:pfam13868  161 LKEKAEREEEREAEREEI----EEEKEREIARLRAQQEKAQDEKAERDELRAKlYQEEQERKERQKEREEAEKKAR-QRQ 235


                   ....*
gi 546232005  1122 EVKES 1126
Cdd:pfam13868  236 ELQQA 240
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 964-1125 8.59e-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: 8.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005   964 RVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQ---ISKMMELAREKQAAELKALKETSEndtKEMKKKLETKRLERI 1040
Cdd:pfam13868  116 AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEreeDERILEYLKEKAEREEEREAEREE---IEEEKEREIARLRAQ 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  1041 QGMTKVTTDKMAQERLKREINNshiQEVVQVIKQMTEnLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLE 1120
Cdd:pfam13868  193 QEKAQDEKAERDELRAKLYQEE---QERKERQKEREE-AEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLR 268


                   ....*
gi 546232005  1121 AEVKE 1125
Cdd:pfam13868  269 KQAED 273
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 973-1169 9.84e-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: 39.75  E-value: 9.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005  973 ELELLRQGEEQYECVLKRKEQHVAEQISKMMEL-----AREKQAAELKALKETSENDTKEMKKKLEtKRLERIQGMTKVT 1047
Cdd:COG4942    42 ELAALKKEEKALLKQLAALERRIAALARRIRALeqelaALEAELAELEKEIAELRAELEAQKEELA-ELLRALYRLGRQP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232005 1048 TDKM--AQERLKREINNSH-IQEVVQVIKQMTENLERHQEKLEEKQAAcLEQiremEKQFQKEALAEYEARMKGLEAEVK 1124
Cdd:COG4942   121 PLALllSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAE-LEA----ERAELEALLAELEEERAALEALKA 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 546232005 1125 EsvRACLRTCFPSEAKDKPERACECPPELCEQDPLIAKADAQESR 1169
Cdd:COG4942   196 E--RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
 
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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