NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2509832820|ref|XP_056210009|]
View 

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 isoform X1 [Falco biarmicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 311-647 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: 565.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08624      1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKdqsmsg 470
Cdd:cd08624     81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  471 krqnslkkgrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtaYEEMSSLVNY 550
Cdd:cd08624    155 ----------------------------------------------------------------------YEEMSSLVNY 164

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  551 IQPIKFDSFEVSAEKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08624    165 IQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 244

                          330
                   ....*....|....*..
gi 2509832820  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08624    245 QTMDLPMQQNMALFEFN 261
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 149-299 9.12e-100

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: 312.97  E-value: 9.12e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  149 EKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSH 228
Cdd:cd16209      1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2509832820  229 HLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 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 ...
 981-1155 5.51e-79

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: 256.92  E-value: 5.51e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  981 RILELRERLEMDLIHLGEEHHDGIRRKKEQHATEQVTKIIELAREKQTAELKALKEASESNIKDIKKKLEAKRVERIQTM 1060
Cdd:pfam08703    2 QVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1061 MRNTSDKAAQERLKKEINNSHIQEVVQTIKLMTEKTARCQQKLEEKQADNLRRIKEKESQLQQDALAEYEEKLKSLAVEV 1140
Cdd:pfam08703   82 KKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAEV 161

                          170
                   ....*....|....*
gi 2509832820 1141 QSMMKNYAKAGFSGE 1155
Cdd:pfam08703  162 RESVKSCLKEGFPDE 176
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-141 1.27e-60

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: 203.38  E-value: 1.27e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820   12 EVKEYLSKGERFIKWDDETAGASP-VILRVDPKGFYLYWTYQNKEMEILDITSIRDTRVGRFAKIPKCQKLREVFNLDYP 90
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2509832820   91 HSTFLLKTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVRNPLTYN 141
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 681-800 6.32e-37

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: 135.36  E-value: 6.32e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  681 TLSVTILSGQFLSD------RSVKTYVEVELFGLPRDTKRKYRTKlTSTANSINPVWkEEAFVFEkIMMPELASLKIVAW 754
Cdd:cd00275      3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAKFKTK-VVKNNGFNPVW-NETFEFD-VTVPELAFLRFVVY 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2509832820  755 EEGG---KFIGHRIIPVIAMHSGYHHVCLRSESNMPLTMPSLFVYLEIK 800
Cdd:cd00275     80 DEDSgddDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
 
Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 311-647 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: 565.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08624      1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKdqsmsg 470
Cdd:cd08624     81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  471 krqnslkkgrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtaYEEMSSLVNY 550
Cdd:cd08624    155 ----------------------------------------------------------------------YEEMSSLVNY 164

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  551 IQPIKFDSFEVSAEKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08624    165 IQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 244

                          330
                   ....*....|....*..
gi 2509832820  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08624    245 QTMDLPMQQNMALFEFN 261
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 149-299 9.12e-100

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: 312.97  E-value: 9.12e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  149 EKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSH 228
Cdd:cd16209      1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2509832820  229 HLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 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 ...
 981-1155 5.51e-79

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: 256.92  E-value: 5.51e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  981 RILELRERLEMDLIHLGEEHHDGIRRKKEQHATEQVTKIIELAREKQTAELKALKEASESNIKDIKKKLEAKRVERIQTM 1060
Cdd:pfam08703    2 QVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1061 MRNTSDKAAQERLKKEINNSHIQEVVQTIKLMTEKTARCQQKLEEKQADNLRRIKEKESQLQQDALAEYEEKLKSLAVEV 1140
Cdd:pfam08703   82 KKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAEV 161

                          170
                   ....*....|....*
gi 2509832820 1141 QSMMKNYAKAGFSGE 1155
Cdd:pfam08703  162 RESVKSCLKEGFPDE 176
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 314-462 5.30e-77

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: 250.11  E-value: 5.30e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  314 MTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAIAE 393
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2509832820  394 SAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEkyplKPGVPLPSPKDLLGKILIKN 462
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLD----DDLTELPSPEDLKGKILIKG 142
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 545-659 7.28e-67

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: 220.19  E-value: 7.28e-67
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820   545 SSLVNYIQPIKFDSFEVSAEKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQ 624
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 2509832820   625 MVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFM 659
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
PLN02222 PLN02222
phosphoinositide phospholipase C 2
 219-798 8.11e-62

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 222.21  E-value: 8.11e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  219 PEIDEIFTSHhlKAKPYMTKEHLAKFINKKQRDSRlndilfppAKPEQVQSLIEKyepSGINIQRGQLSPEGMVWFLCGP 298
Cdd:PLN02222    25 REIKTIFEKY--SENGVMTVDHLHRFLIDVQKQDK--------ATREDAQSIINS---ASSLLHRNGLHLDAFFKYLFGD 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  299 ENNVIALDKLvlHQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIItHGFTM 378
Cdd:PLN02222    92 NNPPLALHEV--HHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSDKDDIDVL-HGMTL 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  379 TTEILFKDAIEAIAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKyPLKPgvpLPSPKDLLGKI 458
Cdd:PLN02222   169 TTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHL-TPDLQSKVAEMVTEIFGEILFTPPVGE-SLKE---FPSPNSLKKRI 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  459 LIKNKKDQSM-SGKRQNSLKKGRNVepeiieqpaptdAEDTVWAGDVAEEEPEEEDEHLGNLDEEEikKMQSDEGTAGLE 537
Cdd:PLN02222   244 IISTKPPKEYkEGKDDEVVQKGKDL------------GDEEVWGREVPSFIQRNKSVDKNDSNGDD--DDDDDDGEDKSK 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  538 VTAYEEMSSLVNyIQPIK-----FDSFEVSAEKNRSYVISSFTELKAYDlltKFPVQFVEYNKRQMSRIYPKGTRMDSSN 612
Cdd:PLN02222   310 KNAPPQYKHLIA-IHAGKpkggiTECLKVDPDKVRRLSLSEEQLEKAAE---KYAKQIVRFTQHNLLRIYPKGTRVTSSN 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  613 YMPQMFWNVGCQMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRRPDKQFDPFSvDRIDVVVASTLSVTILSGQ-- 690
Cdd:PLN02222   386 YNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKKPDLLLKSGSDSDIFD-PKATLPVKTTLRVTIYMGEgw 464

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  691 --------FLSDRSVKTYVEVELFGLPRDTKRKyRTKlTSTANSInPVWKEeafVFE-KIMMPELASLKIVAWE----EG 757
Cdd:PLN02222   465 yfdfrhthFDQYSPPDFYTRVGIAGVPGDTVMK-KTK-TLEDNWI-PAWDE---VFEfPLTVPELALLRLEVHEydmsEK 538

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 2509832820  758 GKFIGHRIIPVIAMHSGYHHVCLRSESNMPLTMPSLFVYLE 798
Cdd:PLN02222   539 DDFGGQTCLPVWELSQGIRAFPLHSRKGEKYKSVKLLVKVE 579
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-141 1.27e-60

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: 203.38  E-value: 1.27e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820   12 EVKEYLSKGERFIKWDDETAGASP-VILRVDPKGFYLYWTYQNKEMEILDITSIRDTRVGRFAKIPKCQKLREVFNLDYP 90
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2509832820   91 HSTFLLKTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVRNPLTYN 141
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-144 2.23e-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: 188.16  E-value: 2.23e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820   17 LSKGERFIKWDDETAGASPVILRVDPKGFYLYWTYQNKEMEILDITSIRDTRVGRFAKIPKCQKLREVfNLDYPHSTFLL 96
Cdd:cd13361      1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2509832820   97 KTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVRNPLTYNASR 144
Cdd:cd13361     80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 681-800 6.32e-37

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: 135.36  E-value: 6.32e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  681 TLSVTILSGQFLSD------RSVKTYVEVELFGLPRDTKRKYRTKlTSTANSINPVWkEEAFVFEkIMMPELASLKIVAW 754
Cdd:cd00275      3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAKFKTK-VVKNNGFNPVW-NETFEFD-VTVPELAFLRFVVY 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2509832820  755 EEGG---KFIGHRIIPVIAMHSGYHHVCLRSESNMPLTMPSLFVYLEIK 800
Cdd:cd00275     80 DEDSgddDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 681-780 1.71e-12

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: 64.82  E-value: 1.71e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820   681 TLSVTILSGQFLSDR----SVKTYVEVELFGlprDTKRKYRTKltSTANSINPVWKEEaFVFEkIMMPELASLKIVAWEE 756
Cdd:smart00239    1 TLTVKIISARNLPPKdkggKSDPYVKVSLDG---DPKEKKKTK--VVKNTLNPVWNET-FEFE-VPPPELAELEIEVYDK 73

                            90       100
                    ....*....|....*....|....*...
gi 2509832820   757 GG----KFIGHRIIPVIAMHSGYHHVCL 780
Cdd:smart00239   74 DRfgrdDFIGQVTIPLSDLLLGGRHEKL 101
C2 pfam00168
C2 domain;
681-768 8.10e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 51.55  E-value: 8.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  681 TLSVTILSGQFL----SDRSVKTYVEVELfglpRDTKRKYRTKLTStaNSINPVWKEEaFVFEkIMMPELASLKIVAWEE 756
Cdd:pfam00168    2 RLTVTVIEAKNLppkdGNGTSDPYVKVYL----LDGKQKKKTKVVK--NTLNPVWNET-FTFS-VPDPENAVLEIEVYDY 73

                           90
                   ....*....|....*.
gi 2509832820  757 GG----KFIGHRIIPV 768
Cdd:pfam00168   74 DRfgrdDFIGEVRIPL 89
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 215-302 1.33e-07

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: 50.32  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  215 LCPRPEIDEIFTSHHlKAKPYMTKEHLAKFINKKQRDSRlndilfppAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWF 294
Cdd:pfam09279    5 LTQREEIDEIFQEYS-GDGQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAMTKDGFLMY 75


                   ....*...
gi 2509832820  295 LCGPENNV 302
Cdd:pfam09279   76 LCSPDGSI 83
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 978-1143 3.80e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.54  E-value: 3.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  978 IDSRILELRERLE---MDLIHLgEEHHDGIRRKKEQHATEqvtkIIELAREKQTAELKAlkEASESNIKDIKKKLEAKRV 1054
Cdd:COG1579     15 LDSELDRLEHRLKelpAELAEL-EDELAALEARLEAAKTE----LEDLEKEIKRLELEI--EEVEARIKKYEEQLGNVRN 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1055 ERIQTMMrnTSDKAAQERLKKEINNsHIQEVVQTIKLMTEKTARCQQKLEEKQADnlrrIKEKESQLQQdALAEYEEKLK 1134
Cdd:COG1579     88 NKEYEAL--QKEIESLKRRISDLED-EILELMERIEELEEELAELEAELAELEAE----LEEKKAELDE-ELAELEAELE 159


                   ....*....
gi 2509832820 1135 SLAVEVQSM 1143
Cdd:COG1579    160 ELEAEREEL 168
PTZ00121 PTZ00121
MAEBL; Provisional
 1005-1187 1.02e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1005 RRKKEQHATEQVTKIIEL--AREKQTAElKALKEASESNIKDIKKKLEAKRVERIQTMMRNTSDKAAQERLKKEINNSHI 1082
Cdd:PTZ00121  1176 KKAEAARKAEEVRKAEELrkAEDARKAE-AARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEI 1254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1083 QEVVQTIKLMTEKTARCQQKLEEKQADNLRRIKEKEsqlQQDALAEYEEKLKslAVEVQSMMKNYAKAgfsgepETQKQA 1162
Cdd:PTZ00121  1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK---KADEAKKAEEKKK--ADEAKKKAEEAKKA------DEAKKK 1323

                          170       180
                   ....*....|....*....|....*
gi 2509832820 1163 VQSIPEGGQGSKEQLEEKIPVAEVS 1187
Cdd:PTZ00121  1324 AEEAKKKADAAKKKAEEAKKAAEAA 1348
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 922-1181 1.99e-04

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: 45.83  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  922 SKRREELLqKYSVLFSEPVCYGGKKRMIHTRKTQKKRSLTTGDVgtcADPVEMAEGIDSRILELRERLEMDLIHLgEEHH 1001
Cdd:TIGR02169  204 RREREKAE-RYQALLKEKREYEGYELLKEKEALERQKEAIERQL---ASLEEELEKLTEEISELEKRLEEIEQLL-EELN 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1002 DGIRRKKEQHATEQVTKI------IELAR-------------EKQTAELKALKEASESNIKDIKKKLEAKRVERIQTMMR 1062
Cdd:TIGR02169  279 KKIKDLGEEEQLRVKEKIgeleaeIASLErsiaekereledaEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE 358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1063 NTSDKAAQERLKKEInnshiQEVVQTIKLMTEKTARCQQKLEE-------------KQADNLRRIKEKESQLQQDaLAEY 1129
Cdd:TIGR02169  359 YAELKEELEDLRAEL-----EEVDKEFAETRDELKDYREKLEKlkreinelkreldRLQEELQRLSEELADLNAA-IAGI 432

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2509832820 1130 EEKLKSLAVEVQSMMKNYAKAgfsgepETQKQAVQSIPEGGQGSKEQLEEKI 1181
Cdd:TIGR02169  433 EAKINELEEEKEDKALEIKKQ------EWKLEQLAADLSKYEQELYDLKEEY 478
 
Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 311-647 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: 565.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08624      1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKdqsmsg 470
Cdd:cd08624     81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  471 krqnslkkgrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtaYEEMSSLVNY 550
Cdd:cd08624    155 ----------------------------------------------------------------------YEEMSSLVNY 164

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  551 IQPIKFDSFEVSAEKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08624    165 IQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 244

                          330
                   ....*....|....*..
gi 2509832820  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08624    245 QTMDLPMQQNMALFEFN 261
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
 311-647 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: 551.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08591      1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVDSpKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKdqsmsg 470
Cdd:cd08591     81 IAETAFKTSEYPVILSFENHCSS-KQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------ 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  471 krqnslkkgrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNY 550
Cdd:cd08591    154 -------------------------------------------------------------------------LSSLVNY 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  551 IQPIKFDSFEVSAEKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08591    161 IQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQLSRIYPKGTRVDSSNYMPQIFWNAGCQMVALNF 240

                          330
                   ....*....|....*..
gi 2509832820  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08591    241 QTPDLPMQLNQGKFEYN 257
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
 313-647 8.26e-153

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: 457.98  E-value: 8.26e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  313 DMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEAIA 392
Cdd:cd08625      3 DMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEAIA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  393 ESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKdqsmsgkr 472
Cdd:cd08625     83 ESAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK-------- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  473 qnslkkgrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNYIQ 552
Cdd:cd08625    155 -----------------------------------------------------------------------MSTLVNYIE 163

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  553 PIKFDSFEVSAEKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQT 632
Cdd:cd08625    164 PVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPMEFVEYNKKQLSRIYPKGTRVDSSNYMPQLFWNVGCQMVALNFQT 243

                          330
                   ....*....|....*
gi 2509832820  633 MDVPMQQNMALFEFN 647
Cdd:cd08625    244 LDLAMQLNMGVFEYN 258
PI-PLCc_eukaryota cd08558
Catalytic domain of eukaryotic phosphoinositide-specific phospholipase C and similar proteins; ...
 311-647 1.12e-135

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


Pssm-ID: 176501 [Multi-domain]  Cd Length: 226  Bit Score: 411.84  E-value: 1.12e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08558      1 YQDMTQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGHTLTSKILFKDVIEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPlkpgVPLPSPKDLLGKILIKNKKdqsmsg 470
Cdd:cd08558     79 IKEYAFVTSPYPVILSLENHC-SLEQQKKMAQILKEIFGDKLLTPPLDENP----VQLPSPEQLKGKILIKGKK------ 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  471 krqnslkkgrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeemsslvny 550
Cdd:cd08558        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  551 iqpikfdsfevsaeknrsYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08558    148 ------------------YHMSSFSETKALKLLKESPEEFVKYNKRQLSRVYPKGTRVDSSNYNPQPFWNAGCQMVALNY 209

                          330
                   ....*....|....*..
gi 2509832820  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08558    210 QTPDLPMQLNQGKFEQN 226
PI-PLCc_beta1 cd08623
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1; This subfamily ...
 312-647 2.14e-134

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: 409.86  E-value: 2.14e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  312 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEAI 391
Cdd:cd08623      2 EDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  392 AESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKdqsmsgk 471
Cdd:cd08623     82 AECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKK------- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  472 rqnslkkgrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNYI 551
Cdd:cd08623    155 ------------------------------------------------------------------------MSNLVNYI 162

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  552 QPIKFDSFEVSAEKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQ 631
Cdd:cd08623    163 QPVKFESFEASKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQ 242

                          330
                   ....*....|....*.
gi 2509832820  632 TMDVPMQQNMALFEFN 647
Cdd:cd08623    243 TVDLSMQINMGMYEYN 258
PI-PLCc_beta4 cd08626
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4; This subfamily ...
 311-647 5.60e-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: 5.60e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08626      1 YQDMDQPLAHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCIELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKdqsmsg 470
Cdd:cd08626     81 IKDTAFVTSDYPVILSFENHC-SKPQQYKLAKYCEEIFGDLLLTKPLESHPLEPGVPLPSPNKLKRKILIKNKR------ 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  471 krqnslkkgrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNY 550
Cdd:cd08626    154 -------------------------------------------------------------------------LSSLVNY 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  551 IQPIKFDSFEVSAEKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08626    161 AQPVKFQGFDVAEERNIHFNMSSFNESVGLGYLKTSAIEFVNYNKRQMSRIYPKGTRVDSSNYMPQIFWNAGCQMVSLNF 240

                          330
                   ....*....|....*..
gi 2509832820  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08626    241 QTPDLGMQLNQGKFEYN 257
PI-PLCc_delta cd08593
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta; This subfamily ...
 311-647 8.94e-113

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: 352.41  E-value: 8.94e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08593      1 YQDMTQPLSHYFIASSHNTYLLEDQLKGPSSTEAYIRALKKGCRCVELDCWDG--PDGEPIIYHGHTLTSKILFKDVIQA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEkyplKPGVPLPSPKDLLGKILIKNKKdqsmsg 470
Cdd:cd08593     79 IREYAFKVSPYPVILSLENHC-SVEQQKVMAQHLKSILGDKLLTQPLD----GVLTALPSPEELKGKILVKGKK------ 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  471 krqnsLKkgrnvepeiieqpaptdaedtvwagdVAeeepeeedehlgnldeeeikkmqsdegtaglevtayEEMSSLVNY 550
Cdd:cd08593    148 -----LK--------------------------LA------------------------------------KELSDLVIY 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  551 IQPIKFDSFEVSAEKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08593    161 CKSVHFKSFEHSKENYHFYEMSSFSESKALKLAQESGNEFVRHNKRQLSRIYPAGLRTDSSNYDPQEMWNVGCQIVALNF 240

                          330
                   ....*....|....*..
gi 2509832820  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08593    241 QTPGEEMDLNDGLFRQN 257
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 149-299 9.12e-100

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: 312.97  E-value: 9.12e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  149 EKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSH 228
Cdd:cd16209      1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2509832820  229 HLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16209     81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PI-PLCc_PRIP_metazoa cd08597
Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein; This ...
 311-647 2.02e-94

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: 302.80  E-value: 2.02e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08597      1 CQDMTQPLSHYFIASSHNTYLIEDQLRGPSSVEGYVRALQRGCRCVELDCWDG--PNGEPVIYHGHTLTSKISFRSVIEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPlekyPLKPGVPLPSPKDLLGKILIKNKKdqsmsg 470
Cdd:cd08597     79 INEYAFVASEYPLILCIENHC-SEKQQLVMAQYLKEIFGDKLYTEP----PNEGESYLPSPHDLKGKIIIKGKK------ 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  471 krqnsLKKgrnvePEIIeqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayEEMSSLVNY 550
Cdd:cd08597    148 -----LKR-----RKLC------------------------------------------------------KELSDLVSL 163

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  551 IQPIKFDSFEVSAEKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08597    164 CKSVRFQDFPTSAQNQKYWEVCSFSENLARRLANEFPEDFVNYNKKFLSRVYPSPMRVDSSNYNPQDFWNCGCQIVAMNY 243

                          330
                   ....*....|....*..
gi 2509832820  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08597    244 QTPGLMMDLNTGKFLEN 260
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 311-647 4.16e-92

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: 297.25  E-value: 4.16e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFS-----GISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTtEILFK 385
Cdd:cd00137      1 HHPDTQPLAHYSIPGTHDTYLTAGQFTikqvwGLTQTEMYRQQLLSGCRCVDIRCWDG--KPEEPIIYHGPTFL-DIFLK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  386 DAIEAIAESAFKTSLYPVILSFENHVDS-PKQQAKMAEYCRTIFGDMLLTeplekYPLKPGVPLPSPKDLLGKILIKNKK 464
Cdd:cd00137     78 EVIEAIAQFLKKNPPETIIMSLKNEVDSmDSFQAKMAEYCRTIFGDMLLT-----PPLKPTVPLPSLEDLRGKILLLNKK 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  465 DQSMsgkrqnslkkgrnvepeiieqpAPTDAEDTVWagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeem 544
Cdd:cd00137    153 NGFS----------------------GPTGSSNDTG-------------------------------------------- 166

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  545 sslvnyiqpikFDSFEVSAEKNRSYVISSFTELKAYD----LLTKFPVQFVEYNKRQMSRIYPKGTR---------MDSS 611
Cdd:cd00137    167 -----------FVSFEFSTQKNRSYNISSQDEYKAYDdekvKLIKATVQFVDYNKNQLSRNYPSGTSggtawyyyaMDSN 235

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2509832820  612 NYMPQMFWN---VGCQMVALNFQTMDVPMQQNMALFEFN 647
Cdd:cd00137    236 NYMPQMFWNanpAGCGIVILDFQTMDLPMQQYMAVIEFN 274
PI-PLCc_gamma cd08592
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma; This family ...
 312-647 2.89e-90

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: 290.10  E-value: 2.89e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  312 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAI 391
Cdd:cd08592      2 QDMNNPLSHYWIASSHNTYLTGDQLSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPIIYHGHTLTSKIKFMDVLKTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  392 AESAFKTSLYPVILSFENHVDSPkQQAKMAEYCRTIFGDMLLTEPLEkyplKPGVPLPSPKDLLGKILIKNKKdqsmsgk 471
Cdd:cd08592     80 KEHAFVTSEYPVILSIENHCSLP-QQRNMAQAFKEVFGDMLLTQPVD----RNADQLPSPNQLKRKIIIKHKK------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  472 rqnslkkgrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtAYEEMsslvnyi 551
Cdd:cd08592    148 --------------------------------------------------------------------LFYEM------- 152

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  552 qpikfdsfevsaeknrsyviSSFTELKAYDLLTKF-PVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08592    153 --------------------SSFPETKAEKYLNRQkGKIFLKYNRRQLSRVYPKGQRVDSSNYDPVPMWNCGSQMVALNF 212

                          330
                   ....*....|....*..
gi 2509832820  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08592    213 QTPDKPMQLNQALFMLN 229
PI-PLCc_delta3 cd08630
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily ...
 311-647 4.33e-84

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: 274.59  E-value: 4.33e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08630      1 FQDMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEG--PGGEPVIYHGHTLTSKILFRDVIQA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvPLPSPKDLLGKILIKNKKDQsmsg 470
Cdd:cd08630     79 VRQHAFTASPYPVILSLENHC-GLEQQAAMARHLQTILGDMLVTQPLDSLNPE---ELPSPEELKGRVLVKGKKLQ---- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  471 krqnslkkgrnVEPeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeEMSSLVNY 550
Cdd:cd08630    151 -----------ISP----------------------------------------------------------ELSALAVY 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  551 IQPIKFDSFEVSAEKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08630    162 CQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQEMWNSGCQLVALNF 241

                          330
                   ....*....|....*..
gi 2509832820  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08630    242 QTPGYEMDLNAGRFLVN 258
PI-PLC1c_yeast cd08598
Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This ...
 312-644 4.33e-84

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: 273.35  E-value: 4.33e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  312 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAI 391
Cdd:cd08598      2 EDLSRPLNEYFISSSHNTYLLGRQLAGDSSVEGYIRALQRGCRCVEIDVWDG--DDGEPVVTHGYTLTSSVPFRDVCRAI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  392 AESAFKTSLYPVILSFENHVDsPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvpLPSPKDLLGKILIKNKKDQSMsgk 471
Cdd:cd08598     80 KKYAFVTSPYPLILSLEVHCD-AEQQERMVEIMKETFGDLLVTEPLDGLEDE----LPSPEELRGKILIKVKKESKT--- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  472 rqnslkkgrnvepeiieqpaptdaedtvwagdvaeeepeeeDEHLGNLDEEEIKKMQSDegtaglevtayeemsslvnyi 551
Cdd:cd08598    152 -----------------------------------------PNHIFSLSERSLLKLLKD--------------------- 169

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  552 qpikfdsfevsaeknrsyvissftelKAYDLltkfpvqfVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQ 631
Cdd:cd08598    170 --------------------------KRAAL--------DKHNRRHLMRVYPSGTRISSSNFNPLPFWRAGVQMVALNWQ 215

                          330
                   ....*....|...
gi 2509832820  632 TMDVPMQQNMALF 644
Cdd:cd08598    216 TYDLGMQLNEAMF 228
PI-PLCc_delta1 cd08629
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily ...
 311-647 9.27e-83

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: 270.75  E-value: 9.27e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08629      1 YQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDG--PNQEPIIYHGYTFTSKILFCDVLRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvpLPSPKDLLGKILIKNKKdqsmsg 470
Cdd:cd08629     79 IRDYAFKASPYPVILSLENHC-SLEQQRVMARHLRAILGPILLDQPLDGVTTS----LPSPEQLKGKILLKGKK------ 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  471 krqnsLKKGRnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeEMSSLVNY 550
Cdd:cd08629    148 -----LKLVP--------------------------------------------------------------ELSDMIIY 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  551 IQPIKFDSFEVSAEKNRS-YVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALN 629
Cdd:cd08629    161 CKSVHFGGFSSPGTSGQAfYEMASFSESRALRLLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALN 240

                          330
                   ....*....|....*...
gi 2509832820  630 FQTMDVPMQQNMALFEFN 647
Cdd:cd08629    241 FQTPGPEMDVYLGCFQDN 258
PI-PLCc_zeta cd08595
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta; This family ...
 311-647 7.39e-81

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: 265.65  E-value: 7.39e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08595      1 YQDMDHPLSDYFISSSHNTYLVSDQLVGPSDLDGYVSALRKGCRCLEIDCWDG--ADNEPVVYHGYTLTSKILFKEVITT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvPLPSPKDLLGKILIKNKKDQSMSg 470
Cdd:cd08595     79 VEKYAFEKSDYPVVLSLENHC-STEQQEIMAHYLVSILGEKLLRAPIDDPATG---ELPSPEALKFKILVKNKKKIAKA- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  471 krqnslkkgrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNY 550
Cdd:cd08595    154 -------------------------------------------------------------------------LSDLVIY 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  551 IQPIKFDSFEVSAEKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08595    161 TKSEKFCSFTHSRDNQHSYENNSIGENKARKLLKSSGADFVGHTQRFITRIYPKGTRASSSNYNPQEFWNVGCQMVALNF 240

                          330
                   ....*....|....*..
gi 2509832820  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08595    241 QTLGAPMDLQNGKFLDN 257
PI-PLCc_delta4 cd08631
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4; This subfamily ...
 311-647 9.35e-81

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: 265.27  E-value: 9.35e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08631      1 YQDMTQPLCHYFICSSHNTYLMEDQLRGQSSVEGYIRALKRGCRCVEVDVWDG--PNGEPIVYHGHTFTSKILFKDVVAA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLE-KYPlkpgVPLPSPKDLLGKILIKNKKdqsms 469
Cdd:cd08631     79 VAQYAFQVSDYPVILSLENHC-GVEQQQTMAQHLTEILGEKLLSTTLDgVLP----TQLPSPEELRGKILLKGKK----- 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  470 gkrqnslkkgrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtagleVTAYEEMSSLVN 549
Cdd:cd08631    149 --------------------------------------------------------------------IRLSPELSDCVI 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  550 YIQPIKFDSFEVSAEKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALN 629
Cdd:cd08631    161 YCKSVSFRSFTHSREHYHFYEISSFTETKARKLIREAGNEFVQHNTWQLSRVYPSGLRTDSSNYNPQEMWNAGCQMVALN 240

                          330
                   ....*....|....*...
gi 2509832820  630 FQTMDVPMQQNMALFEFN 647
Cdd:cd08631    241 FQTAGLEMDLNDGLFRQN 258
PI-PLCc_epsilon cd08596
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon; This family ...
 312-647 7.93e-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: 262.48  E-value: 7.93e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  312 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRppDEEPIITHGFTMTTEILFKDAIEAI 391
Cdd:cd08596      2 EDLQYPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLTGCRCVELDCWDGD--DGMPIIYHGHTLTTKIPFKDVVEAI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  392 AESAFKTSLYPVILSFENHVDSPkQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKdqsmsgk 471
Cdd:cd08596     80 NRSAFITSDYPVILSIENHCSLQ-QQRKMAEIFKTVFGEKLVTKFLFESDFSDDPSLPSPLQLKNKILLKNKK------- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  472 rqnslkkgrnvepeiieqpAPtdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeEMSSLVNYI 551
Cdd:cd08596    152 -------------------AP--------------------------------------------------ELSDLVIYC 162

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  552 QPIKFDSFEVSaeknRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQ 631
Cdd:cd08596    163 QAVKFPGLSTP----KCYHISSLNENAAKRLCRRYPQKLVQHTRCQLLRTYPAATRIDSSNPNPLIFWLHGLQLVALNYQ 238

                          330
                   ....*....|....*.
gi 2509832820  632 TMDVPMQQNMALFEFN 647
Cdd:cd08596    239 TDDLPMHLNAAMFEAN 254
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 981-1155 5.51e-79

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: 256.92  E-value: 5.51e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  981 RILELRERLEMDLIHLGEEHHDGIRRKKEQHATEQVTKIIELAREKQTAELKALKEASESNIKDIKKKLEAKRVERIQTM 1060
Cdd:pfam08703    2 QVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1061 MRNTSDKAAQERLKKEINNSHIQEVVQTIKLMTEKTARCQQKLEEKQADNLRRIKEKESQLQQDALAEYEEKLKSLAVEV 1140
Cdd:pfam08703   82 KKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAEV 161

                          170
                   ....*....|....*
gi 2509832820 1141 QSMMKNYAKAGFSGE 1155
Cdd:pfam08703  162 RESVKSCLKEGFPDE 176
PI-PLCc_eta2 cd08633
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily ...
 311-647 5.85e-78

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: 257.28  E-value: 5.85e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08633      1 NQDMTQPLSHYFITSSHNTYLSGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDG--PDGEPIVHHGYTLTSKILFKDVIET 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVDSPkQQAKMAEYCRTIFGDMLltePLEKYPLKPGVPLPSPKDLLGKILIKNKKdqsmsg 470
Cdd:cd08633     79 INKYAFIKNEYPVILSIENHCSVP-QQKKMAQYLTEILGDKL---DLSSVISNDCTRLPSPEILKGKILVKGKK------ 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  471 krqnsLKKGrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNY 550
Cdd:cd08633    149 -----LSRA----------------------------------------------------------------LSDLVKY 159

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  551 IQPIKFDSFEVSAekNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08633    160 TKSVRVHDIETEA--TSSWQVSSFSETKAHQILQQKPAQYLRFNQRQLSRIYPSSYRVDSSNYNPQPFWNAGCQMVALNY 237

                          330
                   ....*....|....*..
gi 2509832820  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08633    238 QSEGRMLQLNRAKFSAN 254
PI-PLCc_eta cd08594
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta; This family ...
 311-647 2.63e-77

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


Pssm-ID: 176536 [Multi-domain]  Cd Length: 227  Bit Score: 254.34  E-value: 2.63e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08594      1 NQDMTQPLSHYFIASSHNTYLTGDQLLSQSRVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKILFRDVIET 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLtepLEKYPLKPGVPLPSPKDLLGKILIKNKKDQsmsg 470
Cdd:cd08594     79 INKYAFIKNEYPVILSIENHC-SVQQQKKMAQYLKEILGDKLD---LSSVISGDSKQLPSPQSLKGKILIKGKKWQ---- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  471 krqnslkkgrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeemsslvny 550
Cdd:cd08594        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  551 iqpikfdsfevsaeknrsyvISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08594    151 --------------------VSSFSETRAHQIVQQKAAQFLRFNQRQLSRIYPSAYRIDSSNFNPQPYWNAGCQLVALNY 210

                          330
                   ....*....|....*..
gi 2509832820  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08594    211 QTEGRMLQLNRAKFRAN 227
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 314-462 5.30e-77

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: 250.11  E-value: 5.30e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  314 MTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAIAE 393
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2509832820  394 SAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEkyplKPGVPLPSPKDLLGKILIKN 462
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLD----DDLTELPSPEDLKGKILIKG 142
PI-PLCc_gamma2 cd08628
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2; This subfamily ...
 312-647 7.19e-77

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: 254.21  E-value: 7.19e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  312 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAI 391
Cdd:cd08628      2 QDMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRMGCRCIELDCWDG--PDGKPIIYHGWTRTTKIKFDDVVQAI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  392 AESAFKTSLYPVILSFENHVDSpKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvpLPSPKDLLGKILIKNKKDQSMsgk 471
Cdd:cd08628     80 KDHAFVTSEYPVILSIEEHCSV-EQQRHMAKVFKEVFGDKLLMKPLEASADQ----LPSPTQLKEKIIIKHKKLIAI--- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  472 rqnslkkgrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeEMSSLVNYI 551
Cdd:cd08628    152 -----------------------------------------------------------------------ELSDLVVYC 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  552 QPI--KFDSFEVSAEKNrsyvISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALN 629
Cdd:cd08628    161 KPTskTKDNLENPDFKE----IRSFVETKAPSIIRQKPVQLLKYNRKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALN 236

                          330
                   ....*....|....*...
gi 2509832820  630 FQTMDVPMQQNMALFEFN 647
Cdd:cd08628    237 FQTADKYMQLNHALFSLN 254
PI-PLCc_eta1 cd08632
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily ...
 311-647 3.17e-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: 3.17e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08632      1 NQDMDQPLCNYFIASSHNTYLTGDQLLSQSKVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKITFRDVIET 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDML-LTEPLEKYPLKpgvpLPSPKDLLGKILIKNKKdqsms 469
Cdd:cd08632     79 INKYAFVKNEFPVILSIENHC-SIQQQKKIAQYLKEIFGDKLdLSSVLTGDPKQ----LPSPQLLKGKILVKGKK----- 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  470 gkrqnslkkgrnvepeiieqpAPTDAED-TVWAGDVAEeepeeedehlgnldeEEIkkmqSDEGTAGlevtayeemsslv 548
Cdd:cd08632    149 ---------------------LCRDLSDlVVYTNSVAA---------------QDI----VDDGSTG------------- 175

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  549 nyiqpikfdsfevsaeknrsyVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVAL 628
Cdd:cd08632    176 ---------------------NVLSFSETRAHQLVQQKAEQFMTYNQKQLTRIYPSAYRIDSSNFNPLPYWNVGCQLVAL 234

                          330
                   ....*....|....*....
gi 2509832820  629 NFQTMDVPMQQNMALFEFN 647
Cdd:cd08632    235 NYQSEGRMMQLNRAKFMVN 253
PI-PLCc_gamma1 cd08627
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily ...
 312-647 3.89e-69

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: 231.46  E-value: 3.89e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  312 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAI 391
Cdd:cd08627      2 EEMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPVIYHGHTLTTKIKFSDVLHTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  392 AESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEkyplKPGVPLPSPKDLLGKILIKNKKdqsmsgk 471
Cdd:cd08627     80 KEHAFVTSEYPIILSIEDHC-SIVQQRNMAQHFKKVFGDMLLTKPVD----INADGLPSPNQLKRKILIKHKK------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  472 rqnslkkgrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtAYEEMSSLvnyi 551
Cdd:cd08627    148 --------------------------------------------------------------------LYRDMSSF---- 155

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  552 qPikfdsfEVSAEKnrsYVissfTELKAYdlltkfpvQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQ 631
Cdd:cd08627    156 -P------ETKAEK---YV----NRSKGK--------KFLQYNRRQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQ 213

                          330
                   ....*....|....*.
gi 2509832820  632 TMDVPMQQNMALFEFN 647
Cdd:cd08627    214 TPDKPMQMNQALFMLG 229
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 545-659 7.28e-67

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: 220.19  E-value: 7.28e-67
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820   545 SSLVNYIQPIKFDSFEVSAEKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQ 624
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 2509832820   625 MVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFM 659
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
EFh_PI-PLCbeta cd16200
EF-hand motif found in metazoan phosphoinositide-specific phospholipase C (PI-PLC)-beta ...
 149-299 1.17e-63

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: 212.88  E-value: 1.17e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  149 EKILVKLKMQLNAEGKIPVRNIFQMFPAD--RKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFT 226
Cdd:cd16200      1 KKLYTKLKLSVNITGKIPVKNIIKCFSSDkkRKRVLKALKALGLPDGKNDEIDPEDFTFEKFFKLYNKLCPRPDIDEIFK 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2509832820  227 SHHLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16200     81 ELGGKRKPYLTLEQLVDFLNEEQRDPRLNEILFPFHTKEQAKKLIDKYEPNEKNKKKGQLTLEGFLRYLMSDE 153
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 314-463 6.54e-62

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: 207.52  E-value: 6.54e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820   314 MTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAIAE 393
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDG--PDGEPVIYHGHTFTLPIKLSEVLEAIKD 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820   394 SAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvpLPSPKDLLGKILIKNK 463
Cdd:smart00148   79 FAFVTSPYPVILSLENHC-SPDQQAKMAQMFKEIFGDMLYTPPLTSSLEV----LPSPEQLRGKILLKVR 143
PLN02222 PLN02222
phosphoinositide phospholipase C 2
 219-798 8.11e-62

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 222.21  E-value: 8.11e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  219 PEIDEIFTSHhlKAKPYMTKEHLAKFINKKQRDSRlndilfppAKPEQVQSLIEKyepSGINIQRGQLSPEGMVWFLCGP 298
Cdd:PLN02222    25 REIKTIFEKY--SENGVMTVDHLHRFLIDVQKQDK--------ATREDAQSIINS---ASSLLHRNGLHLDAFFKYLFGD 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  299 ENNVIALDKLvlHQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIItHGFTM 378
Cdd:PLN02222    92 NNPPLALHEV--HHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSDKDDIDVL-HGMTL 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  379 TTEILFKDAIEAIAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKyPLKPgvpLPSPKDLLGKI 458
Cdd:PLN02222   169 TTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHL-TPDLQSKVAEMVTEIFGEILFTPPVGE-SLKE---FPSPNSLKKRI 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  459 LIKNKKDQSM-SGKRQNSLKKGRNVepeiieqpaptdAEDTVWAGDVAEEEPEEEDEHLGNLDEEEikKMQSDEGTAGLE 537
Cdd:PLN02222   244 IISTKPPKEYkEGKDDEVVQKGKDL------------GDEEVWGREVPSFIQRNKSVDKNDSNGDD--DDDDDDGEDKSK 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  538 VTAYEEMSSLVNyIQPIK-----FDSFEVSAEKNRSYVISSFTELKAYDlltKFPVQFVEYNKRQMSRIYPKGTRMDSSN 612
Cdd:PLN02222   310 KNAPPQYKHLIA-IHAGKpkggiTECLKVDPDKVRRLSLSEEQLEKAAE---KYAKQIVRFTQHNLLRIYPKGTRVTSSN 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  613 YMPQMFWNVGCQMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRRPDKQFDPFSvDRIDVVVASTLSVTILSGQ-- 690
Cdd:PLN02222   386 YNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKKPDLLLKSGSDSDIFD-PKATLPVKTTLRVTIYMGEgw 464

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  691 --------FLSDRSVKTYVEVELFGLPRDTKRKyRTKlTSTANSInPVWKEeafVFE-KIMMPELASLKIVAWE----EG 757
Cdd:PLN02222   465 yfdfrhthFDQYSPPDFYTRVGIAGVPGDTVMK-KTK-TLEDNWI-PAWDE---VFEfPLTVPELALLRLEVHEydmsEK 538

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 2509832820  758 GKFIGHRIIPVIAMHSGYHHVCLRSESNMPLTMPSLFVYLE 798
Cdd:PLN02222   539 DDFGGQTCLPVWELSQGIRAFPLHSRKGEKYKSVKLLVKVE 579
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-141 1.27e-60

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: 203.38  E-value: 1.27e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820   12 EVKEYLSKGERFIKWDDETAGASP-VILRVDPKGFYLYWTYQNKEMEILDITSIRDTRVGRFAKIPKCQKLREVFNLDYP 90
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2509832820   91 HSTFLLKTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVRNPLTYN 141
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
EFh_PI-PLCbeta1 cd16208
EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1); PI-PLC-beta1, ...
 149-299 1.34e-60

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: 203.96  E-value: 1.34e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  149 EKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSH 228
Cdd:cd16208      1 EKAYTKLKLQVNPEGRIPVKNIYRLFSADRKRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDHIFSEF 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2509832820  229 HLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16208     81 GAKSKPYLSVDQMTEFINSKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSTLAKKGQISVDGFMRYLSGEE 151
PLN02952 PLN02952
phosphoinositide phospholipase C
 310-795 3.90e-59

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 214.86  E-value: 3.90e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  310 LHQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDeEPIITHGFTMTTEILFKDAIE 389
Cdd:PLN02952   121 VHHDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGSTKD-EILVLHGRTLTTPVPLIKCLK 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  390 AIAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLteplekYPLKPG-VPLPSPKDLLGKILIKNKKDQS- 467
Cdd:PLN02952   200 SIRDYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLY------YPESDSlVQFPSPESLKHRIIISTKPPKEy 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  468 MSGKRQNSLKKGRNVEPEIIEQPAPTDAEDTVwagdvaeeepeeeDEHLGNLD-EEEIKKMQSDEGTAGLEVTAYEEMSS 546
Cdd:PLN02952   273 LESSGPIVIKKKNNVSPSGRNSSEETEEAQTL-------------ESMLFEQEaDSRSDSDQDDNKSGELQKPAYKRLIT 339

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  547 lVNYIQP---IKfDSFEVSAEKNRSYvisSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGC 623
Cdd:PLN02952   340 -IHAGKPkgtLK-DAMKVAVDKVRRL---SLSEQELEKAATTNGQDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGA 414

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  624 QMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFM--RRPDKQ-FDPfsvdRIDVVVASTLSVTILSG----------Q 690
Cdd:PLN02952   415 QMIAFNMQGYGKSLWLMHGMFRANGGCGYLKKPDFLmkKGFHDEvFDP----KKKLPVKKTLKVKVYLGdgwrldfshtH 490

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  691 FLSDRSVKTYVEVELFGLPRDTKRKyRTKLTStaNSINPVWKEEaFVFeKIMMPELASLKIVAWE----EGGKFIGHRII 766
Cdd:PLN02952   491 FDSYSPPDFYTKMYIVGVPADNAKK-KTKIIE--DNWYPAWNEE-FSF-PLTVPELALLRIEVREydmsEKDDFGGQTCL 565

                          490       500       510
                   ....*....|....*....|....*....|....
gi 2509832820  767 PVIAMHSGYHHVCLRSE-----SNMPLTMPSLFV 795
Cdd:PLN02952   566 PVSELRPGIRSVPLHDKkgeklKNVRLLMRFIFV 599
PI-PLC-Y pfam00387
Phosphatidylinositol-specific phospholipase C, Y domain; This associates with pfam00388 to ...
 544-658 6.25e-59

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


Pssm-ID: 459794  Cd Length: 114  Bit Score: 197.68  E-value: 6.25e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  544 MSSLVNYIQPIKFDSFEvSAEKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGC 623
Cdd:pfam00387    1 LSDLVVYTQSVKFKSFS-TPESKTPNHIFSFSESKALKLIKSSSAAFVKHNRRHLMRVYPKGTRVDSSNFNPQPFWNCGV 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2509832820  624 QMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEF 658
Cdd:pfam00387   80 QMVALNWQTPDEGMQLNEGMFADNGGCGYVLKPEF 114
PI-PLCc_plant cd08599
Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family ...
 311-647 1.60e-58

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: 201.06  E-value: 1.60e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  311 HQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDeePIITHGFTMTTEILFKDAIEA 390
Cdd:cd08599      1 HHDMTAPLSHYFIFSSHNSYLTGNQLSSRSSTAPIIEALLRGCRVIELDLWPGGRGD--ICVLHGGTLTKPVKFEDCIKA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPlekyPLKPGVPLPSPKDLLGKILIKNKkdqsmsg 470
Cdd:cd08599     79 IKENAFTASEYPVIITLENHL-SPELQAKAAQILRETLGDKLFYPD----SEDLPEEFPSPEELKGKILISDK------- 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  471 krqnslkkgrnvePEIIEqpaptdaedtvwagdvaeeepeeedehlGNLDEEEIKKMQSDEgtaglevtayeemsslvny 550
Cdd:cd08599    147 -------------PPVIR----------------------------NSLSETQLKKVIEGE------------------- 166

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  551 iqpikfdsfevsaeknrsyvissftelkaydlltkFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08599    167 -----------------------------------HPTDLIEFTQKNLLRVYPAGLRITSSNYDPMLAWMHGAQMVALNM 211

                          330
                   ....*....|....*..
gi 2509832820  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08599    212 QGYDRPLWLNRGKFRAN 228
PLN02228 PLN02228
Phosphoinositide phospholipase C
 217-780 1.77e-55

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 203.34  E-value: 1.77e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  217 PRPEIDEIFTSHHLKAKpyMTKEHLAKFINKKQRDSRlndilfppAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLC 296
Cdd:PLN02228    22 PPVSIKRLFEAYSRNGK--MSFDELLRFVSEVQGERH--------AGLDYVQDIFHSVKHHNVFHHHGLVHLNAFYRYLF 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  297 GPENNVIALDKLVlHQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrPPDEEPIITHGF 376
Cdd:PLN02228    92 SDTNSPLPMSGQV-HHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWPN-PSGNAAEVRHGR 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  377 TMTTEILFKDAIEAIAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLkpgvpLPSPKDLLG 456
Cdd:PLN02228   170 TLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHL-PPNLQAQVAKMLTKTFRGMLFRCTSESTKH-----FPSPEELKN 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  457 KILIKNKKDQSMsgkrqnslkkgrnVEPEIIEQPAPTDAEDTVWAgDVAEEepeeedehlgnldEEEIKKMQSDEGTAGL 536
Cdd:PLN02228   244 KILISTKPPKEY-------------LESKTVQTTRTPTVKETSWK-RVADA-------------ENKILEEYKDEESEAV 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  537 EvtaYEEMSSL--VNYIQPIKfDSFEVSAEKNRSYvisSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYM 614
Cdd:PLN02228   297 G---YRDLIAIhaANCKDPLK-DCLSDDPEKPIRV---SMDEQWLETMVRTRGTDLVRFTQRNLVRIYPKGTRVDSSNYD 369

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  615 PQMFWNVGCQMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRRPDKQFDPFSvdriDVVVASTLSVTILSGQ---- 690
Cdd:PLN02228   370 PHVGWTHGAQMVAFNMQGHGKQLWIMQGMFRANGGCGYVKKPRILLDEHTLFDPCK----RLPIKTTLKVKIYTGEgwdl 445

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  691 ------FLSDRSVKTYVEVELFGLPRDTKrKYRTKLtsTANSINPVWKEEAFVFEkIMMPELASL--KIVAWEEGGK--F 760
Cdd:PLN02228   446 dfhlthFDQYSPPDFFVKIGIAGVPRDTV-SYRTET--AVDQWFPIWGNDEFLFQ-LRVPELALLwfKVQDYDNDTQndF 521

                          570       580
                   ....*....|....*....|
gi 2509832820  761 IGHRIIPVIAMHSGYHHVCL 780
Cdd:PLN02228   522 AGQTCLPLPELKSGVRAVRL 541
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-144 2.23e-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: 188.16  E-value: 2.23e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820   17 LSKGERFIKWDDETAGASPVILRVDPKGFYLYWTYQNKEMEILDITSIRDTRVGRFAKIPKCQKLREVfNLDYPHSTFLL 96
Cdd:cd13361      1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2509832820   97 KTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVRNPLTYNASR 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, ...
 149-299 2.61e-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: 171.64  E-value: 2.61e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  149 EKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSH 228
Cdd:cd16210      1 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILLEI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2509832820  229 HLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16210     81 GAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQVRQLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 151
EFh_PI-PLC21 cd16213
EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family ...
 149-295 1.60e-48

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


Pssm-ID: 320043  Cd Length: 154  Bit Score: 169.79  E-value: 1.60e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  149 EKILVKLKMQLNAEGKIPVRNIFQMFPA---DRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIF 225
Cdd:cd16213      1 EKAYTKLTLQTDKEGKIPVKNIVKMFAQhkdDRKRVEKALEAIGLPSGKNDAIDPKKFTFEDFFNFYRRLTGRQEVEKIF 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  226 TSHHLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFL 295
Cdd:cd16213     81 DELGAKKKPYLTTEQFVDFLNKTQRDPRLNEILYPYANPKRARDLINQYEPNKSFAKKGHLSVEGFLRYL 150
PLN02230 PLN02230
phosphoinositide phospholipase C 4
 310-798 2.93e-47

phosphoinositide phospholipase C 4


Pssm-ID: 177875 [Multi-domain]  Cd Length: 598  Bit Score: 179.52  E-value: 2.93e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  310 LHQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKgRPPDEePIITHGFTMTTEILFKDAIE 389
Cdd:PLN02230   113 VHQNMDAPLSHYFIFTGHNSYLTGNQLSSNCSELPIADALRRGVRVVELDLWP-RGTDD-VCVKHGRTLTKEVKLGKCLD 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  390 AIAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPlkpgvPLPSPKDLLGKILIKNKKD---- 465
Cdd:PLN02230   191 SIKANAFAISKYPVIITLEDHL-TPKLQFKVAKMITQTFGDMLYYHDSEGCQ-----EFPSPEELKEKILISTKPPkeyl 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  466 QSMSGKRQNSLKKGRNVEPEIIEQpAPTDAEDTvwAGDVAEEEPEEEDEhlgNLDEEEIKKMQSDEgTAGLEVTAYEEMS 545
Cdd:PLN02230   265 EANDAKEKDNGEKGKDSDEDVWGK-EPEDLIST--QSDLDKVTSSVNDL---NQDDEERGSCESDT-SCQLQAPEYKRLI 337

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  546 SlVNYIQPIKFDSFEVSAEKNRSYVISsFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQM 625
Cdd:PLN02230   338 A-IHAGKPKGGLRMALKVDPNKIRRLS-LSEQLLEKAVASYGADVIRFTQKNFLRIYPKGTRFNSSNYKPQIGWMSGAQM 415

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  626 VALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRRPDKQFDPFsVDRIDVVVASTLSVTILSG----------QFLSDR 695
Cdd:PLN02230   416 IAFNMQGYGRALWLMEGMFRANGGCGYVKKPDFLMDAGPNGQDF-YPKDNSCPKKTLKVKVCMGdgwlldfkktHFDSYS 494

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  696 SVKTYVEVELFGLPRDTKRKyRTKLTStaNSINPVWKEEaFVFeKIMMPELASLKIVAWE----EGGKFIGHRIIPVIAM 771
Cdd:PLN02230   495 PPDFFVRVGIAGAPVDEVME-KTKIEY--DTWTPIWNKE-FIF-PLAVPELALLRVEVHEhdinEKDDFGGQTCLPVSEI 569

                          490       500
                   ....*....|....*....|....*..
gi 2509832820  772 HSGYHHVCLRSESNMPLTMPSLFVYLE 798
Cdd:PLN02230   570 RQGIHAVPLFNRKGVKYSSTRLLMRFE 596
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 681-800 6.32e-37

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: 135.36  E-value: 6.32e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  681 TLSVTILSGQFLSD------RSVKTYVEVELFGLPRDTKRKYRTKlTSTANSINPVWkEEAFVFEkIMMPELASLKIVAW 754
Cdd:cd00275      3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAKFKTK-VVKNNGFNPVW-NETFEFD-VTVPELAFLRFVVY 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2509832820  755 EEGG---KFIGHRIIPVIAMHSGYHHVCLRSESNMPLTMPSLFVYLEIK 800
Cdd:cd00275     80 DEDSgddDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
 154-295 2.67e-31

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: 120.22  E-value: 2.67e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  154 KLKMQLNAEGKIPVRNIFQMFPADR--KRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSHHLK 231
Cdd:cd16211      6 RLCFLVNPNGKIPVRSITRTFASGKteKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFKKINGD 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2509832820  232 AKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFL 295
Cdd:cd16211     86 KKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYL 149
PLN02223 PLN02223
phosphoinositide phospholipase C
 309-789 7.93e-28

phosphoinositide phospholipase C


Pssm-ID: 165867 [Multi-domain]  Cd Length: 537  Bit Score: 119.74  E-value: 7.93e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  309 VLHQDMTQPLSHYFINSSHNTYLTAGQ-FSGISSPEMYRQTLLAGCRCVELDCWkgrPPDEEPI-ITHGFTMTTEILFKD 386
Cdd:PLN02223   103 VRHHDMHAPLSHYFIHTSLKSYFTGNNvFGKLYSIEPIIDALEQGVRVVELDLL---PDGKDGIcVRPKWNFEKPLELQE 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  387 AIEAIAESAF-KTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPlekyPLKPGVPLPSPKDLLGKILIKNKKD 465
Cdd:PLN02223   180 CLDAIKEHAFtKCRSYPLIITFKDGL-KPDLQSKATQMIDQTFGDMVYHED----PQHSLEEFPSPAELQNKILISRRPP 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  466 QSMSGKRQNSLKKGRNVEPEIIEQPAPTDAEDTVwagdvaeeepeeedehlgnldeeeikkmqsdegtaGLEVTayeEMS 545
Cdd:PLN02223   255 KELLYAKADDGGVGVRNELEIQEGPADKNYQSLV-----------------------------------GFHAV---EPR 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  546 SLVNYIQPIKFDSFEVSAEKNRSyvISSFTELKaydLLTKFPvqfveynKRQMSRIYPKgtrmdssnYMPQMFWNVGCQM 625
Cdd:PLN02223   297 GMLQKALTGKADDIQQPGWYERD--IISFTQKK---FLRTRP-------KKKNLLINAP--------YKPQRAWMHGAQL 356

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  626 VALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRR--PDKQFDPfsvdRIDVVVASTLSVTILSGQ-FLSDRSVKT--- 699
Cdd:PLN02223   357 IALSRKDDKEKLWLMQGMFRANGGCGYVKKPDFLLNagPSGVFYP----TENPVVVKILKVKIYMGDgWIVDFKKRIgrl 432

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  700 -----YVEVELFGLPRDTKrkyRTKLTSTANSINPVWKEEaFVFeKIMMPELA--SLKIVAWE--EGGKFIGHRIIPVIA 770
Cdd:PLN02223   433 skpdlYVRISIAGVPHDEK---IMKTTVKNNEWKPTWGEE-FTF-PLTYPDLAliSFEVYDYEvsTADAFCGQTCLPVSE 507

                          490       500
                   ....*....|....*....|....*
gi 2509832820  771 MHSGYHHVCLRSE------SNMPLT 789
Cdd:PLN02223   508 LIEGIRAVPLYDErgkacsSTMLLT 532
EFh_NorpA_like cd16212
EF-hand motif found in Drosophila melanogaster No receptor potential A protein (NorpA) and ...
 153-299 5.77e-25

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: 102.24  E-value: 5.77e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  153 VKLKMQLNAEGKIPVRNIFQMFPADR--KRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSHHL 230
Cdd:cd16212      5 MRLGFMVDSGGKIPVKHIARTFASGKteKLVYQCLAEMGLPSGKGDSIEKEDFTFEKFYALYHKICPRNDIEELFTSITK 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2509832820  231 KAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16212     85 GKGEHISLAQLINFMNDKQRDPRLNEILYPLYDEKRCTEIIKAYEQNEENIKNKRMSKDGFIRYLMSDE 153
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 324-630 1.49e-23

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: 99.05  E-value: 1.49e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  324 NSSHNTYLTAGQfsgISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMT------TEILFKDAIEAIAESAFK 397
Cdd:cd08555      1 VLSHRGYSQNGQ---ENTLEAFYRALDAGARGLELDVRLT--KDGELVVYHGPTLDrttagiLPPTLEEVLELIADYLKN 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  398 TSlYPVILSFENHVDS---PKQQAKMAEYCRTIFGDmllteplekyplkpgvplpspkDLLGKILIKnkkdqsmsgkrqn 474
Cdd:cd08555     76 PD-YTIILSLEIKQDSpeyDEFLAKVLKELRVYFDY----------------------DLRGKVVLS------------- 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  475 slkkgrnvepeiieqpaptdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeemsslvnyiqpi 554
Cdd:cd08555        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2509832820  555 kfdsfevsaeknrSYVISSFTELKAYDLLTKFPVQFVEYNK-RQMSRIYPKGTrmdsSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08555    120 -------------SFNALGVDYYNFSSKLIKDTELIASANKlGLLSRIWTVND----NNEIINKFLNLGVDGLITDF 179
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 195-299 1.36e-13

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: 69.18  E-value: 1.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  195 NDAINPEDFpetvyKTFLMNLCPRPEIDEIFTSHHlKAKPYMTKEHLAKFINKKQRdsrlndilFPPAKPEQVQSLIEKY 274
Cdd:cd16202     50 EDVLDEEEF-----VQFYNRLTKRPEIEELFKKYS-GDDEALTVEELRRFLQEEQK--------VKDVTLEWAEQLIETY 115

                           90       100
                   ....*....|....*....|....*
gi 2509832820  275 EPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16202    116 EPSEDLKAQGLMSLDGFTLFLLSPD 140
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 681-780 1.71e-12

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: 64.82  E-value: 1.71e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820   681 TLSVTILSGQFLSDR----SVKTYVEVELFGlprDTKRKYRTKltSTANSINPVWKEEaFVFEkIMMPELASLKIVAWEE 756
Cdd:smart00239    1 TLTVKIISARNLPPKdkggKSDPYVKVSLDG---DPKEKKKTK--VVKNTLNPVWNET-FEFE-VPPPELAELEIEVYDK 73

                            90       100
                    ....*....|....*....|....*...
gi 2509832820   757 GG----KFIGHRIIPVIAMHSGYHHVCL 780
Cdd:smart00239   74 DRfgrdDFIGQVTIPLSDLLLGGRHEKL 101
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 155-299 1.21e-10

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: 60.37  E-value: 1.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  155 LKMQLNAEGKIPVRNIFQM-----FPADRKRVEAALSACHlpKGKNDAINPEDFpetvyKTFLMNLCPRPEIDEIFTSHH 229
Cdd:cd15898      7 IKADKDGDGKLSLKEIKKLlkrlnIRVSEKELKKLFKEVD--TNGDGTLTFDEF-----EELYKSLTERPELEPIFKKYA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  230 LKAKPYMTKEHLAKFINKKQRDSRlndilfppaKPEQVQSLIEKYEPSGiniQRGQLSPEGMVWFLCGPE 299
Cdd:cd15898     80 GTNRDYMTLEEFIRFLREEQGENV---------SEEECEELIEKYEPER---ENRQLSFEGFTNFLLSPE 137
C2 pfam00168
C2 domain;
681-768 8.10e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 51.55  E-value: 8.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  681 TLSVTILSGQFL----SDRSVKTYVEVELfglpRDTKRKYRTKLTStaNSINPVWKEEaFVFEkIMMPELASLKIVAWEE 756
Cdd:pfam00168    2 RLTVTVIEAKNLppkdGNGTSDPYVKVYL----LDGKQKKKTKVVK--NTLNPVWNET-FTFS-VPDPENAVLEIEVYDY 73

                           90
                   ....*....|....*.
gi 2509832820  757 GG----KFIGHRIIPV 768
Cdd:pfam00168   74 DRfgrdDFIGEVRIPL 89
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 215-302 1.33e-07

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: 50.32  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  215 LCPRPEIDEIFTSHHlKAKPYMTKEHLAKFINKKQRDSRlndilfppAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWF 294
Cdd:pfam09279    5 LTQREEIDEIFQEYS-GDGQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAMTKDGFLMY 75


                   ....*...
gi 2509832820  295 LCGPENNV 302
Cdd:pfam09279   76 LCSPDGSI 83
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 992-1144 4.67e-07

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 53.85  E-value: 4.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  992 DLIHLGEEHHDGIRRKKEQHATEQVTKIIELAREKQTAELKalKEASESNIKDIKKKL-EAKRVERIQTMMRNTSDKAAQ 1070
Cdd:pfam05262  199 DMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFA--QDNADKQRDEVRQKQqEAKNLPKPADTSSPKEDKQVA 276

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2509832820 1071 ERLKKEINNSHIQevvqtiklmTEKTARCQQKLEEKQADNLRRIKEKESQLQQDALAEYEEKLKSLAVEVQSMM 1144
Cdd:pfam05262  277 ENQKREIEKAQIE---------IKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTK 341
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
 209-299 2.16e-06

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


Pssm-ID: 320047 [Multi-domain]  Cd Length: 139  Bit Score: 48.58  E-value: 2.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  209 KTFLMNLCPRPEIDEIFTSHHlKAKPYMTKEHLAKFINKKQRDsrlndilfpPAKPEQVQSLIEKYEPSGINIQRGQLSP 288
Cdd:cd16217     59 EEFYKLLTKREEIDVIFGEYA-KSDGTMSRNNLLNFLQEEQRE---------EVAPAYALSLIEKYEPDETAKAQRQMTK 128

                           90
                   ....*....|.
gi 2509832820  289 EGMVWFLCGPE 299
Cdd:cd16217    129 DGFLMYLLSPE 139
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 978-1143 3.80e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.54  E-value: 3.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  978 IDSRILELRERLE---MDLIHLgEEHHDGIRRKKEQHATEqvtkIIELAREKQTAELKAlkEASESNIKDIKKKLEAKRV 1054
Cdd:COG1579     15 LDSELDRLEHRLKelpAELAEL-EDELAALEARLEAAKTE----LEDLEKEIKRLELEI--EEVEARIKKYEEQLGNVRN 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1055 ERIQTMMrnTSDKAAQERLKKEINNsHIQEVVQTIKLMTEKTARCQQKLEEKQADnlrrIKEKESQLQQdALAEYEEKLK 1134
Cdd:COG1579     88 NKEYEAL--QKEIESLKRRISDLED-EILELMERIEELEEELAELEAELAELEAE----LEEKKAELDE-ELAELEAELE 159


                   ....*....
gi 2509832820 1135 SLAVEVQSM 1143
Cdd:COG1579    160 ELEAEREEL 168
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 1004-1135 2.54e-05

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 47.01  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1004 IRRKKEQHATEQVTKIIELAREKQTAELKalKEASESNIKD-IKKKLEAKRVERIQTMMRNTSDKAAQERLKKEINNSH- 1081
Cdd:pfam13904   61 LAAKQRQRQKELQAQKEEREKEEQEAELR--KRLAKEKYQEwLQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQe 138

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2509832820 1082 -IQEVVQtiKLMTEKTARCQQKLEEKQADNLRRiKEKESQLQQDALAEYEEKLKS 1135
Cdd:pfam13904  139 eAKEVLQ--EWERKKLEQQQRKREEEQREQLKK-EEEEQERKQLAEKAWQKWMKN 190
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 682-763 9.92e-05

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: 42.82  E-value: 9.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  682 LSVTILSGQFLSDR----SVKTYVEVELfglprDTKRKYRTKLTStaNSINPVWKEEaFVFEkIMMPELASLKIVAWEEG 757
Cdd:cd00030      1 LRVTVIEARNLPAKdlngKSDPYVKVSL-----GGKQKFKTKVVK--NTLNPVWNET-FEFP-VLDPESDTLTVEVWDKD 71

                           90
                   ....*....|
gi 2509832820  758 G----KFIGH 763
Cdd:cd00030     72 RfskdDFLGE 81
PTZ00121 PTZ00121
MAEBL; Provisional
 1005-1187 1.02e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1005 RRKKEQHATEQVTKIIEL--AREKQTAElKALKEASESNIKDIKKKLEAKRVERIQTMMRNTSDKAAQERLKKEINNSHI 1082
Cdd:PTZ00121  1176 KKAEAARKAEEVRKAEELrkAEDARKAE-AARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEI 1254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1083 QEVVQTIKLMTEKTARCQQKLEEKQADNLRRIKEKEsqlQQDALAEYEEKLKslAVEVQSMMKNYAKAgfsgepETQKQA 1162
Cdd:PTZ00121  1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK---KADEAKKAEEKKK--ADEAKKKAEEAKKA------DEAKKK 1323

                          170       180
                   ....*....|....*....|....*
gi 2509832820 1163 VQSIPEGGQGSKEQLEEKIPVAEVS 1187
Cdd:PTZ00121  1324 AEEAKKKADAAKKKAEEAKKAAEAA 1348
DUF874 pfam05917
Helicobacter pylori protein of unknown function (DUF874); This family consists of several ...
 1012-1176 1.95e-04

Helicobacter pylori protein of unknown function (DUF874); This family consists of several hypothetical proteins specific to Helicobacter pylori. The function of this family is unknown.


Pssm-ID: 283549 [Multi-domain]  Cd Length: 398  Bit Score: 45.23  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1012 ATEQVTKIIELAREKQTAElkalKEASESNIKDIKKKLEAKRVERIQTMMRNTSDKAAQERLKKEINNSHIQEVVQTIKL 1091
Cdd:pfam05917  119 SAGDTDEQIELEQEKKEAE----NAEDRANKNGIELEQEKQKTNKSGIELANNQIKAEQEQQKTEQEKQKAEKEAIELEQ 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1092 MTEKTARCQQKLEEKQADnlrRIKEKESQLQQDALAEYEEKL---KSLAVEVQSMMKNYAKAGFSGEPETQKQAVQSI-P 1167
Cdd:pfam05917  195 EKQKTIKTQRDLIKEQKD---FIKETEQNCQENHNQFFIEKGgikAGIAIEVEAECKTPKPAKTNQTPIQPKHLPNSKqP 271


                   ....*....
gi 2509832820 1168 EGGQGSKEQ 1176
Cdd:pfam05917  272 HSQRGSKAQ 280
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 922-1181 1.99e-04

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: 45.83  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  922 SKRREELLqKYSVLFSEPVCYGGKKRMIHTRKTQKKRSLTTGDVgtcADPVEMAEGIDSRILELRERLEMDLIHLgEEHH 1001
Cdd:TIGR02169  204 RREREKAE-RYQALLKEKREYEGYELLKEKEALERQKEAIERQL---ASLEEELEKLTEEISELEKRLEEIEQLL-EELN 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1002 DGIRRKKEQHATEQVTKI------IELAR-------------EKQTAELKALKEASESNIKDIKKKLEAKRVERIQTMMR 1062
Cdd:TIGR02169  279 KKIKDLGEEEQLRVKEKIgeleaeIASLErsiaekereledaEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE 358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1063 NTSDKAAQERLKKEInnshiQEVVQTIKLMTEKTARCQQKLEE-------------KQADNLRRIKEKESQLQQDaLAEY 1129
Cdd:TIGR02169  359 YAELKEELEDLRAEL-----EEVDKEFAETRDELKDYREKLEKlkreinelkreldRLQEELQRLSEELADLNAA-IAGI 432

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2509832820 1130 EEKLKSLAVEVQSMMKNYAKAgfsgepETQKQAVQSIPEGGQGSKEQLEEKI 1181
Cdd:TIGR02169  433 EAKINELEEEKEDKALEIKKQ------EWKLEQLAADLSKYEQELYDLKEEY 478
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
 152-299 2.52e-04

EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes represent a class of neuron-specific metazoan PI-PLCs that are most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. They are phosphatidylinositol 4,5-bisphosphate-hydrolyzing enzymes that are more sensitive to Ca2+ than other PI-PLC isozymes. They function as calcium sensors activated by small increases in intracellular calcium concentrations. They are also activated through G-protein-coupled receptor (GPCR) stimulation, and further mediate GPCR signalling pathways. PI-PLC-eta isozymes contain an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, 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. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases. There are two PI-PLC-eta isozymes (1-2). Aside from the PI-PLC-eta isozymes identified in mammals, their eukaryotic homologs are also present in this family.


Pssm-ID: 320035 [Multi-domain]  Cd Length: 141  Bit Score: 42.37  E-value: 2.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  152 LVKLKMQLNAegKIPVRNIFQMF-PADRKRVEAALsachlpkgkndainpeDFPEtvYKTFLMNLCPRPEIDEIFTSHHL 230
Cdd:cd16205     22 ILQLMHKLNV--NLPRRKVRQMFkEADTDDNQGTL----------------DFEE--FCAFYKMMSTRRELYLLLLSYSN 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2509832820  231 KaKPYMTKEHLAKFINKKQRDSRLNDilfppakpEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16205     82 K-KDYLTLEDLARFLEVEQKMTNVTL--------EYCLDIIEKFEPSEENKKNGLLGIDGFTNYMRSPA 141
PTZ00121 PTZ00121
MAEBL; Provisional
 969-1209 2.84e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 2.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  969 ADPVEMAEGIDSRILELR---ERLEMDLIHLGEEHH--DGIRRKKEQHATEQVTKIIEL--AREKQTAElKALKEASESN 1041
Cdd:PTZ00121  1499 ADEAKKAAEAKKKADEAKkaeEAKKADEAKKAEEAKkaDEAKKAEEKKKADELKKAEELkkAEEKKKAE-EAKKAEEDKN 1577

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1042 IK----DIKKKLEAKRVERIQTMMRNTSDKAAQErLKKEINNSHIQEVVQTIKLMTEKTARCQQKLEE--KQADNLRRiK 1115
Cdd:PTZ00121  1578 MAlrkaEEAKKAEEARIEEVMKLYEEEKKMKAEE-AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekKKAEELKK-A 1655

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1116 EKESQLQQDALAEYEEKLKSLAVEVQSMMKNYAKAGFS-GEPETQKQAVQSIPEGGQGSKEQLEEKIPVAEVSGLTTAMP 1194
Cdd:PTZ00121  1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735

                          250
                   ....*....|....*
gi 2509832820 1195 EPPGAETDGEIEESR 1209
Cdd:PTZ00121  1736 KKEAEEDKKKAEEAK 1750
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 1004-1181 3.58e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 44.73  E-value: 3.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1004 IRRKKEQHATEQVTKIIELAReKQTAELKALKEASESNI---KDIKK--KLEAKR-------VERIQTMMRN--TSDKAA 1069
Cdd:pfam05557   14 LQNEKKQMELEHKRARIELEK-KASALKRQLDRESDRNQelqKRIRLleKREAEAeealreqAELNRLKKKYleALNKKL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1070 QER-------------LKKEINNSH--IQEVVQTIKLMTEKTARCQQKLEEKQAdNLRRIKEKESQLQ--QDALAEYEEK 1132
Cdd:pfam05557   93 NEKesqladareviscLKNELSELRrqIQRAELELQSTNSELEELQERLDLLKA-KASEAEQLRQNLEkqQSSLAEAEQR 171

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2509832820 1133 LKSLAVEVQSmmknyaKAGFSGEPETQKQAVQSIPEgGQGSKEQLEEKI 1181
Cdd:pfam05557  172 IKELEFEIQS------QEQDSEIVKNSKSELARIPE-LEKELERLREHN 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1022-1209 3.78e-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: 45.05  E-value: 3.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1022 LAREKQTAELKALKEASESNIKDIKKKLEAKRVEriQTMMRNTSDKAAQERLKKEINNSHIQEVVQTIKLMTEKTARCQQ 1101
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKE--LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1102 KLEEKQADNLRRIKEKESQLQQ--DALAEYEEKLKSLAVEVQSMMK-----NYAKAGFSGEPETQKQAVQSIPEGGQGSK 1174
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEaeEELAEAEAEIEELEAQIEQLKEelkalREALDELRAELTLLNEEAANLRERLESLE 830

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2509832820 1175 EQLEEKIPVAEVSGLTTAMPEPPGAETDGEIEESR 1209
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
PTZ00121 PTZ00121
MAEBL; Provisional
 946-1209 5.25e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 5.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  946 KRMIHTRKTQKKRSLTTGDVGTCADPVEMAEgidsRILELRERLEmdlIHLGEEhhdgIRRKKEQHATEQVTKIIELARE 1025
Cdd:PTZ00121  1152 KRVEIARKAEDARKAEEARKAEDAKKAEAAR----KAEEVRKAEE---LRKAED----ARKAEAARKAEEERKAEEARKA 1220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1026 KQTAELKALKEASESNikdiKKKLEAKRVERIqtmmRNTSdkaaQERLKKEINNSHIQEVVQTIKLMTEKTARCQQKLEE 1105
Cdd:PTZ00121  1221 EDAKKAEAVKKAEEAK----KDAEEAKKAEEE----RNNE----EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1106 -KQADNLRRIKEKESQLQQDALAEYEEKLKSLAVEVQSMMKNYAKAgfSGEPETQKQAVQSIPEGGQGSKEQLEEKIPVA 1184
Cdd:PTZ00121  1289 kKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAA--KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366

                          250       260
                   ....*....|....*....|....*
gi 2509832820 1185 EVSGLTTAMPEPPGAETDGEIEESR 1209
Cdd:PTZ00121  1367 EAAEKKKEEAKKKADAAKKKAEEKK 1391
PTZ00121 PTZ00121
MAEBL; Provisional
 923-1181 9.64e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 9.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  923 KRREELLQKYSVLFSEPVCYGGKKRMIHTRKTQKKRSLTTGDVGTCADPVEMAEGIDSRIL--ELRERLEMDLIHLGEEH 1000
Cdd:PTZ00121  1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEE 1631

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1001 HDGIRRKKEQHAtEQVTKIIELAREKQTAELKALKEASESNiKDIKKKLEAKRVERiqtmmrntSDKAAQERLKKEINNS 1080
Cdd:PTZ00121  1632 KKKVEQLKKKEA-EEKKKAEELKKAEEENKIKAAEEAKKAE-EDKKKAEEAKKAEE--------DEKKAAEALKKEAEEA 1701

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1081 HIQEVVQTIKLMTEKTARCQQKLEEK---QADNLRRIKEKESQLQQDALAEYEEKLKslaveVQSMMKNYAKAGFSGEPE 1157
Cdd:PTZ00121  1702 KKAEELKKKEAEEKKKAEELKKAEEEnkiKAEEAKKEAEEDKKKAEEAKKDEEEKKK-----IAHLKKEEEKKAEEIRKE 1776

                          250       260
                   ....*....|....*....|....
gi 2509832820 1158 TQKQAVQSIPEGGQGSKEQLEEKI 1181
Cdd:PTZ00121  1777 KEAVIEEELDEEDEKRRMEVDKKI 1800
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 998-1133 1.17e-03

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: 41.57  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  998 EEHHDGIRRKKEQHaTEQVTKIIELAREK---------QTAELK----ALKEASESNIKDIKK----------------- 1047
Cdd:pfam15665   10 DEHEAEIQALKEAH-EEEIQQILAETREKilqykskigEELDLKrriqTLEESLEQHERMKRQaltefeqykrrveerel 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1048 KLEAKRVERIQTMMRNTSD--KAAQERLK--------------------KEINNSHIQEVVQTIKLMTEKTARCQQKLEE 1105
Cdd:pfam15665   89 KAEAEHRQRVVELSREVEEakRAFEEKLEsfeqlqaqfeqekrkaleelRAKHRQEIQELLTTQRAQSASSLAEQEKLEE 168

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2509832820 1106 KQADNLRRIKEKESQLQQD---ALAEYEEKL 1133
Cdd:pfam15665  169 LHKAELESLRKEVEDLRKEkkkLAEEYEQKL 199
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 985-1145 1.45e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.79  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  985 LRERLEMDLIHLGEEHHDGIRRKKEQHATEQVTKIIELAREKQTAELKALKEASESNIKDIKKKLEAKRVeriqtmmrnt 1064
Cdd:pfam05483  599 LKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKI---------- 668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1065 sdkaAQERLKKEINNSHIQeVVQTIKLMTEKTARCQQKLEE---------KQADNLrrIKEKESQL---------QQDAL 1126
Cdd:pfam05483  669 ----SEEKLLEEVEKAKAI-ADEAVKLQKEIDKRCQHKIAEmvalmekhkHQYDKI--IEERDSELglyknkeqeQSSAK 741

                          170
                   ....*....|....*....
gi 2509832820 1127 AEYEEKLKSLAVEVQSMMK 1145
Cdd:pfam05483  742 AALEIELSNIKAELLSLKK 760
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 1014-1150 1.45e-03

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: 40.71  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1014 EQVTKIIELAREKQTAELKALKEASESNIKDIKKKLEAKRvERIQTMMRNTSDKAAQeRLK---KEINNSHIQEVVQTIK 1090
Cdd:pfam01442   18 EQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYL-EELQAKLGQNVEELRQ-RLEpytEELRKRLNADAEELQE 95

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2509832820 1091 LMTEKTARCQQKLEEKQ----------ADNLR-RIKEKESQLQQ---DALAEYEEKLKSLAVEVQSMMKNYAKA 1150
Cdd:pfam01442   96 KLAPYGEELRERLEQNVdalrarlapyAEELRqKLAERLEELKEslaPYAEEVQAQLSQRLQELREKLEPQAED 169
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1025-1208 2.22e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1025 EKQTAELKALKEASESNIKDIKKKLEA--KRVERIQTMMR--NTSDKAAQERLKK-EINNSHIQEVVQTIKLMTEKTARC 1099
Cdd:COG4372     51 REELEQAREELEQLEEELEQARSELEQleEELEELNEQLQaaQAELAQAQEELESlQEEAEELQEELEELQKERQDLEQQ 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1100 QQKLEEKQADNLRRIKEKESQLQQ--DALAEYEEKLKSLAVEVQSMMKNYAKAGFSGEPETQKQAVQSIPEGGQGSKEQL 1177
Cdd:COG4372    131 RKQLEAQIAELQSEIAEREEELKEleEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIE 210

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2509832820 1178 EEKIPVAEVSGLTTAMPEPPGAETDGEIEES 1208
Cdd:COG4372    211 SLPRELAEELLEAKDSLEAKLGLALSALLDA 241
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 678-739 2.51e-03

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: 39.49  E-value: 2.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2509832820  678 VASTLSVTILSGQFLSDRSVK----TYVEVELFGlprdTKRKYRTKLTSTA-NSINPVWKeEAFVFE 739
Cdd:cd00276     12 TAERLTVVVLKARNLPPSDGKglsdPYVKVSLLQ----GGKKLKKKKTSVKkGTLNPVFN-EAFSFD 73
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 973-1145 2.72e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 41.94  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  973 EMAEGIDSRILELRE---RLEMDLIHLGEEhhdgIRRKKEQHAT--EQV---TKIIELAR--EKQTAELKALKEASESNI 1042
Cdd:pfam05667  342 EQLEDLESSIQELEKeikKLESSIKQVEEE----LEELKEQNEEleKQYkvkKKTLDLLPdaEENIAKLQALVDASAQRL 417

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1043 KDIKKKLEAKRVERIQTMmrntsdkaaqERLKKEInnshiqevvqtiklmTEKTARCQQKLEEkqadnLRRIKEKESQLQ 1122
Cdd:pfam05667  418 VELAGQWEKHRVPLIEEY----------RALKEAK---------------SNKEDESQRKLEE-----IKELREKIKEVA 467

                          170       180
                   ....*....|....*....|...
gi 2509832820 1123 QDAlAEYEEKLKSLAVEVQSMMK 1145
Cdd:pfam05667  468 EEA-KQKEELYKQLVAEYERLPK 489
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
975-1136 2.81e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  975 AEGIDSRILELRERLEmDLihlgEEHHDGIRRKKEQHatEQVTKIIELAREKQtAELKALKEASESNIKDIKKKLEA--K 1052
Cdd:COG4913    663 VASAEREIAELEAELE-RL----DASSDDLAALEEQL--EELEAELEELEEEL-DELKGEIGRLEKELEQAEEELDElqD 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1053 RVERIQTMMRNTSDKAAQERLKKEINNSHIQEVVQT----IKLMTEKTARCQQKLEEKQADNLRRIKEKES--------- 1119
Cdd:COG4913    735 RLEAAEDLARLELRALLEERFAAALGDAVERELRENleerIDALRARLNRAEEELERAMRAFNREWPAETAdldadlesl 814

                          170       180
                   ....*....|....*....|....*
gi 2509832820 1120 --------QLQQDALAEYEEKLKSL 1136
Cdd:COG4913    815 peylalldRLEEDGLPEYEERFKEL 839
AhaH TIGR02926
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
 972-1053 2.82e-03

ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.


Pssm-ID: 131972 [Multi-domain]  Cd Length: 85  Bit Score: 37.90  E-value: 2.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  972 VEMAEG-IDSRILELRERLEmDLIHLGEEHHDGIRRKKEQHATEQVTKIIELAREKQTAELKALKEASESNIKDIKKKLE 1050
Cdd:TIGR02926    4 IKKAEEdAEELIEEAEEERK-QRIAEAREEARELLEEAEEEASKLGEEIIKEAEEEIEKEAEKIREEGEKEIEAMKSKAK 82


                   ...
gi 2509832820 1051 AKR 1053
Cdd:TIGR02926   83 EKI 85
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 1012-1116 3.47e-03

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


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 38.72  E-value: 3.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1012 ATEQVTKIIELAREKQtAELKALKEASEsNIKDIKKKLEAKRVERIQTMMRntsdkaaQERLKKEINNshiqevvqtikl 1091
Cdd:pfam18595   31 VEKDLRSCIKLLEEIE-AELAKLEEAKK-KLKELRDALEEKEIELRELERR-------EERLQRQLEN------------ 89

                           90       100
                   ....*....|....*....|....*
gi 2509832820 1092 MTEKTARCQQKLEEKQADNLRRIKE 1116
Cdd:pfam18595   90 AQEKLERLREQAEEKREAAQARLEE 114
PRK12704 PRK12704
phosphodiesterase; Provisional
 1004-1147 5.81e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 5.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1004 IRRKKEQHATEQVTKIIELA-REKQTAELKALKEASESnIKDIKKKLEAKRVER---IQTMMRNTSDKaaQERLKKEINN 1079
Cdd:PRK12704    28 IAEAKIKEAEEEAKRILEEAkKEAEAIKKEALLEAKEE-IHKLRNEFEKELRERrneLQKLEKRLLQK--EENLDRKLEL 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1080 ---------SHIQEVVQTIKLMTEKTARCqQKLEEKQADNLRRIkekeSQLQQD-----ALAEYEEKLKslaVEVQSMMK 1145
Cdd:PRK12704   105 lekreeeleKKEKELEQKQQELEKKEEEL-EELIEEQLQELERI----SGLTAEeakeiLLEKVEEEAR---HEAAVLIK 176


                   ..
gi 2509832820 1146 NY 1147
Cdd:PRK12704   177 EI 178
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 970-1117 6.17e-03

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: 39.17  E-value: 6.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  970 DPVEMAEGIDSRILELRERLEmdlihlgeEHHDGIRrkkeqhatEQVTKIIELAREKQTAELKALKEASESNIKDIKKKL 1049
Cdd:pfam01442   34 ETEALRERLQKDLEEVRAKLE--------PYLEELQ--------AKLGQNVEELRQRLEPYTEELRKRLNADAEELQEKL 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2509832820 1050 EAKRVERIQTMMRNTSDKAAQ-----ERLKKEInNSHIQEVVQTIKLMTE----KTARCQQKLEEKQADNLRRIKEK 1117
Cdd:pfam01442   98 APYGEELRERLEQNVDALRARlapyaEELRQKL-AERLEELKESLAPYAEevqaQLSQRLQELREKLEPQAEDLREK 173
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 976-1193 6.65e-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: 40.81  E-value: 6.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820  976 EGIDSRILELRER---LEMDLIHLGEEHHDGIRRKKEQHA--------TEQVTKIIELAREKQtAELKALKEASESNIKD 1044
Cdd:TIGR02168  298 SRLEQQKQILRERlanLERQLEELEAQLEELESKLDELAEelaeleekLEELKEELESLEAEL-EELEAELEELESRLEE 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1045 IKKKLEAKRVERIQ----------TMMRNTSDK----AAQERLKKEINNSHIQEVVQTIKLMTEKTARCQQKLEEKQADN 1110
Cdd:TIGR02168  377 LEEQLETLRSKVAQlelqiaslnnEIERLEARLerleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509832820 1111 LRRIKEKESQLQQ--------DALAEYEEKLKSLAVEVQSMMKNyakagFSGEPETQKQAVQSiPEGGQGSKEQLEEKIP 1182
Cdd:TIGR02168  457 ERLEEALEELREEleeaeqalDAAERELAQLQARLDSLERLQEN-----LEGFSEGVKALLKN-QSGLSGILGVLSELIS 530

                          250
                   ....*....|.
gi 2509832820 1183 VAEvsGLTTAM 1193
Cdd:TIGR02168  531 VDE--GYEAAI 539
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH