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Conserved domains on  [gi|595763333|ref|NP_001277719|]
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1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 isoform b [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 288-627 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: 543.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDILFKEAIEA 367
Cdd:cd08624     1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVDSPRQQAKMAEYCRSMFGETLLTDPLENFPLKPGIPLPSPEDLRGKILIKNKKnqfsgp 447
Cdd:cd08624    81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtaYEEMSSL 527
Cdd:cd08624   155 -------------------------------------------------------------------------YEEMSSL 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 VNYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08624   162 VNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVA 241

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08624   242 LNFQTMDLPMQQNMALFEFN 261
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 126-276 9.18e-98

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: 306.80  E-value: 9.18e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  126 DKILVKLKMQLNPEGKIPVKNFFQMFPADRKRVEAALGACHLAKGKNDAINPEDFPESVYKSFLMSLCPRPEIDEIFTSY 205
Cdd:cd16209     1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 595763333  206 HSKAKPYMTKEHLTKFINQKQRDPRLNSLLFPPARPEQVQVLIDKYEPSGINVQRGQLSPEGMVWFLCGPE 276
Cdd:cd16209    81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 951-1126 4.12e-77

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


:

Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 251.52  E-value: 4.12e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   951 PRVQELKDRLEQELQQQGEEQYRSVLKRKEQHVTEQIAKMMELAREKQAAELKTFKETSETDTKEMKKKLEAKRLERIQA 1030
Cdd:pfam08703    1 KQVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  1031 MTKVTTDKVAQERLKREINNSHIQEVVQAVKQMTETLERHQEKLEERQTACLEQIQAMEKQFQEKALAEYEAKMKGLEAE 1110
Cdd:pfam08703   81 AKKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAE 160

                          170
                   ....*....|....*.
gi 595763333  1111 VKESVRAYFKDCFPTE 1126
Cdd:pfam08703  161 VRESVKSCLKEGFPDE 176
PH_14 super family cl39289
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 13-118 9.88e-45

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


The actual alignment was detected with superfamily member pfam17787:

Pssm-ID: 465506  Cd Length: 131  Bit Score: 157.93  E-value: 9.88e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333    13 VKAYLSQGERFIKWDDETSIASP-VILRVDPKGYYLYWTYQN-----------------------QSQKLREVFNMDFPD 68
Cdd:pfam17787    2 VPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGkegevleitsirdtrlgkfakipKDPKLREVLSMGGSD 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 595763333    69 NHFLLKTLTVVSGPDMVDLTFYNFVSYKENVGKDWAEDVLALAKHPMTVN 118
Cdd:pfam17787   82 NSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 659-780 1.46e-36

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: 134.21  E-value: 1.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  659 ATTLSITIISGQFLS------ERSVRTYVEVELFGLPGDPKRRYRTKLSPtANSINPVWkEEPFIFEKIlMPELASLRIA 732
Cdd:cd00275     1 PLTLTIKIISGQQLPkpkgdkGSIVDPYVEVEIHGLPADDSAKFKTKVVK-NNGFNPVW-NETFEFDVT-VPELAFLRFV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 595763333  733 VMEE---GSKFLGHRIIPINALHSGYHHLCLRSESNMALTMPALFVFLEMK 780
Cdd:cd00275    78 VYDEdsgDDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
 
Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 288-627 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: 543.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDILFKEAIEA 367
Cdd:cd08624     1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVDSPRQQAKMAEYCRSMFGETLLTDPLENFPLKPGIPLPSPEDLRGKILIKNKKnqfsgp 447
Cdd:cd08624    81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtaYEEMSSL 527
Cdd:cd08624   155 -------------------------------------------------------------------------YEEMSSL 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 VNYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08624   162 VNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVA 241

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08624   242 LNFQTMDLPMQQNMALFEFN 261
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 126-276 9.18e-98

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: 306.80  E-value: 9.18e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  126 DKILVKLKMQLNPEGKIPVKNFFQMFPADRKRVEAALGACHLAKGKNDAINPEDFPESVYKSFLMSLCPRPEIDEIFTSY 205
Cdd:cd16209     1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 595763333  206 HSKAKPYMTKEHLTKFINQKQRDPRLNSLLFPPARPEQVQVLIDKYEPSGINVQRGQLSPEGMVWFLCGPE 276
Cdd:cd16209    81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 291-439 1.68e-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: 250.89  E-value: 1.68e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   291 MTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEAIAE 370
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 595763333   371 SAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLTDPLENfplkPGIPLPSPEDLRGKILIKN 439
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLDD----DLTELPSPEDLKGKILIKG 142
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 951-1126 4.12e-77

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


Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 251.52  E-value: 4.12e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   951 PRVQELKDRLEQELQQQGEEQYRSVLKRKEQHVTEQIAKMMELAREKQAAELKTFKETSETDTKEMKKKLEAKRLERIQA 1030
Cdd:pfam08703    1 KQVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  1031 MTKVTTDKVAQERLKREINNSHIQEVVQAVKQMTETLERHQEKLEERQTACLEQIQAMEKQFQEKALAEYEAKMKGLEAE 1110
Cdd:pfam08703   81 AKKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAE 160

                          170
                   ....*....|....*.
gi 595763333  1111 VKESVRAYFKDCFPTE 1126
Cdd:pfam08703  161 VRESVKSCLKEGFPDE 176
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 525-639 8.70e-63

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


Pssm-ID: 128454 [Multi-domain]  Cd Length: 115  Bit Score: 208.63  E-value: 8.70e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333    525 SSLVNYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQ 604
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 595763333    605 MVALNFQTMDLPMQQNMALFEFNGQSGYLLKHEFM 639
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
PLN02952 PLN02952
phosphoinositide phospholipase C
 287-775 2.58e-57

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 209.47  E-value: 2.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  287 IHQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEePIITHGFTMTTDILFKEAIE 366
Cdd:PLN02952  121 VHHDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGSTKDE-ILVLHGRTLTTPVPLIKCLK 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  367 AIAESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLL---TDPLENFPlkpgiplpSPEDLRGKILIKNKKN- 442
Cdd:PLN02952  200 SIRDYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLYypeSDSLVQFP--------SPESLKHRIIISTKPPk 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  443 ---QFSGPASPSKKpGGVAEGSLPSSVPVEEDTGWTAEDRTEVEEEEVVEEEEEEESGNLDEEEIKKMqsdegtagLEVT 519
Cdd:PLN02952  271 eylESSGPIVIKKK-NNVSPSGRNSSEETEEAQTLESMLFEQEADSRSDSDQDDNKSGELQKPAYKRL--------ITIH 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  520 AYEEMSSLVNYIQptkfisfeFSAQKNRSYvvsSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFW 599
Cdd:PLN02952  342 AGKPKGTLKDAMK--------VAVDKVRRL---SLSEQELEKAATTNGQDVVRFTQRNILRIYPKGTRITSSNYKPLIGW 410

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  600 NAGCQMVALNFQTMDLPMQQNMALFEFNGQSGYLLKHEFMrrLDKQFNPFSVD-RIDVVVATTLSITIISG--------- 669
Cdd:PLN02952  411 MHGAQMIAFNMQGYGKSLWLMHGMFRANGGCGYLKKPDFL--MKKGFHDEVFDpKKKLPVKKTLKVKVYLGdgwrldfsh 488

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  670 -QFLSERSVRTYVEVELFGLPGDPKRRyRTKLspTANSINPVWKEEpFIFeKILMPELASLRIAV----MEEGSKFLGHR 744
Cdd:PLN02952  489 tHFDSYSPPDFYTKMYIVGVPADNAKK-KTKI--IEDNWYPAWNEE-FSF-PLTVPELALLRIEVreydMSEKDDFGGQT 563

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 595763333  745 IIPINALHSGYHHLCLRSE-----SNMALTMPALFV 775
Cdd:PLN02952  564 CLPVSELRPGIRSVPLHDKkgeklKNVRLLMRFIFV 599
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 13-118 9.88e-45

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: 157.93  E-value: 9.88e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333    13 VKAYLSQGERFIKWDDETSIASP-VILRVDPKGYYLYWTYQN-----------------------QSQKLREVFNMDFPD 68
Cdd:pfam17787    2 VPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGkegevleitsirdtrlgkfakipKDPKLREVLSMGGSD 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 595763333    69 NHFLLKTLTVVSGPDMVDLTFYNFVSYKENVGKDWAEDVLALAKHPMTVN 118
Cdd:pfam17787   82 NSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 659-780 1.46e-36

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: 134.21  E-value: 1.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  659 ATTLSITIISGQFLS------ERSVRTYVEVELFGLPGDPKRRYRTKLSPtANSINPVWkEEPFIFEKIlMPELASLRIA 732
Cdd:cd00275     1 PLTLTIKIISGQQLPkpkgdkGSIVDPYVEVEIHGLPADDSAKFKTKVVK-NNGFNPVW-NETFEFDVT-VPELAFLRFV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 595763333  733 VMEE---GSKFLGHRIIPINALHSGYHHLCLRSESNMALTMPALFVFLEMK 780
Cdd:cd00275    78 VYDEdsgDDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-121 7.28e-34

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: 126.53  E-value: 7.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   17 LSQGERFIKWDDETSIASPVILRVDPKGYYLYWTYQNQS-----------------------QKLREVfNMDFPDNHFLL 73
Cdd:cd13361     1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKEtevldlslirdvrtgkypkdpkdLKEREV-NVGGSDEDLED 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 595763333   74 KTLTVVSGPDMVDLTFYNFVSYKENVGKDWAEDVLALAKHPMTVNAPR 121
Cdd:cd13361    80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 661-757 1.20e-13

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: 67.90  E-value: 1.20e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333    661 TLSITIISGQFLSER----SVRTYVEVELFGlpgDPKRRYRTKLSPtaNSINPVWKEEpFIFEkILMPELASLRIAVMEE 736
Cdd:smart00239    1 TLTVKIISARNLPPKdkggKSDPYVKVSLDG---DPKEKKKTKVVK--NTLNPVWNET-FEFE-VPPPELAELEIEVYDK 73

                            90       100
                    ....*....|....*....|....*
gi 595763333    737 GS----KFLGHRIIPINALHSGYHH 757
Cdd:smart00239   74 DRfgrdDFIGQVTIPLSDLLLGGRH 98
C2 pfam00168
C2 domain;
661-754 2.09e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 55.79  E-value: 2.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   661 TLSITIISGQFL----SERSVRTYVEVELfglpGDPKRRYRTKLSPtaNSINPVWKEEpFIFEkILMPELASLRIAVMEE 736
Cdd:pfam00168    2 RLTVTVIEAKNLppkdGNGTSDPYVKVYL----LDGKQKKKTKVVK--NTLNPVWNET-FTFS-VPDPENAVLEIEVYDY 73

                           90       100
                   ....*....|....*....|..
gi 595763333   737 GS----KFLGHRIIPINALHSG 754
Cdd:pfam00168   74 DRfgrdDFIGEVRIPLSELDSG 95
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 853-1113 5.87e-09

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: 60.46  E-value: 5.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   853 EEATKEVTEPQTASLEELRELKGVVKLQRRHEKELRELERRGARRWEELlQRGAAQLAELQTQAAGCKLRPGKGSRKKRT 932
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL-TELEAEIEELEERLEEAEEELAEAEAEIEE 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   933 LpcEETV-------VAPSEPHDRADPRVQELKDRLEQELQQQGEEQYRSVLKRKEQHVTEQIAKMMELAREKQAAELKTF 1005
Cdd:TIGR02168  787 L--EAQIeqlkeelKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  1006 KETSETDTKEMKKKLEAKRlERIQAMtkvttdkvAQERLKREINNSHIQEVVQAVKQMTETLERHQEKLEERQTAcLEQI 1085
Cdd:TIGR02168  865 EELIEELESELEALLNERA-SLEEAL--------ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR-LEGL 934

                          250       260
                   ....*....|....*....|....*...
gi 595763333  1086 QAMEKQFQEKALAEYEAKMKGLEAEVKE 1113
Cdd:TIGR02168  935 EVRIDNLQERLSEEYSLTLEEAEALENK 962
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 192-280 9.75e-09

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


Pssm-ID: 401279 [Multi-domain]  Cd Length: 85  Bit Score: 53.40  E-value: 9.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   192 LCPRPEIDEIFTSYhSKAKPYMTKEHLTKFINQKQRDPRlnsllfppARPEQVQVLIDKYEPSGINVQRGQLSPEGMVWF 271
Cdd:pfam09279    5 LTQREEIDEIFQEY-SGDGQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAMTKDGFLMY 75


                   ....*....
gi 595763333   272 LCGPENSVL 280
Cdd:pfam09279   76 LCSPDGSIF 84
PTZ00121 PTZ00121
MAEBL; Provisional
 853-1152 1.25e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  853 EEATKEVTEPQTASLEELRELKGVVKLQRRHEKELRELERRGAR--RWEELLQRGAAQLAELQTQAAgcKLRPGKGSRKK 930
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEeaRMAHFARRQAAIKAEEARKAD--ELKKAEEKKKA 1292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  931 RTLPCEETVVAPSEPHDRADP--RVQELKDRLEQELQQQGEEQYRSVLKRKEQHVT----EQIAKMMELAREK-QAAELK 1003
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAkaeaEAAADEAEAAEEKaEAAEKK 1372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1004 TFKETSETDtkEMKKKLEAKRlERIQAMTKVTTDKVAQERLKREinnshiqevvQAVKQMTETLERhqeKLEERQTAcle 1083
Cdd:PTZ00121 1373 KEEAKKKAD--AAKKKAEEKK-KADEAKKKAEEDKKKADELKKA----------AAAKKKADEAKK---KAEEKKKA--- 1433

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1084 qiQAMEKQFQEKALAEyEAKMKGLEAEVKESVRAYFKDCFPT-EAEDKPERSCEASEESCPQEPLVSKAD 1152
Cdd:PTZ00121 1434 --DEAKKKAEEAKKAD-EAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKAD 1500
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 981-1113 1.92e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 47.23  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  981 QHVTEQIAKMMELARE--KQAAELKTFKETSETDTKEMKKKLEAKRLERIQAMTKVTTDKVAQERLKREINNSHIQEVVQ 1058
Cdd:COG1579    13 QELDSELDRLEHRLKElpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 595763333 1059 AVKQMTETLERHQEKLEERQTACLEQIQAMEKQFQ--EKALAEYEAKMKGLEAEVKE 1113
Cdd:COG1579    93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAelEAELAELEAELEEKKAELDE 149
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 995-1108 4.29e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 4.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  995 REKQAAE---LKTFKETSETDTKEMKKKLEAKRLERIQAMTKVttDKVAQERLKREINNSHIQEVVQAVKQMTETLERHQ 1071
Cdd:cd16269   177 QSKEAEAeaiLQADQALTEKEKEIEAERAKAEAAEQERKLLEE--QQRELEQKLEDQERSYEEHLRQLKEKMEEERENLL 254

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 595763333 1072 EKLEERQTACL-EQIQAMEKQFQEKAlAEYEAKMKGLE 1108
Cdd:cd16269   255 KEQERALESKLkEQEALLEEGFKEQA-ELLQEEIRSLK 291
 
Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 288-627 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: 543.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDILFKEAIEA 367
Cdd:cd08624     1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVDSPRQQAKMAEYCRSMFGETLLTDPLENFPLKPGIPLPSPEDLRGKILIKNKKnqfsgp 447
Cdd:cd08624    81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtaYEEMSSL 527
Cdd:cd08624   155 -------------------------------------------------------------------------YEEMSSL 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 VNYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08624   162 VNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVA 241

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08624   242 LNFQTMDLPMQQNMALFEFN 261
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
 288-627 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: 534.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDILFKEAIEA 367
Cdd:cd08591     1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVDSPrQQAKMAEYCRSMFGETLLTDPLENFPLKPGIPLPSPEDLRGKILIKNKKnqfsgp 447
Cdd:cd08591    81 IAETAFKTSEYPVILSFENHCSSK-QQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSL 527
Cdd:cd08591   154 ----------------------------------------------------------------------------LSSL 157

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 VNYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08591   158 VNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQLSRIYPKGTRVDSSNYMPQIFWNAGCQMVA 237

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08591   238 LNFQTPDLPMQLNQGKFEYN 257
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
 290-627 8.84e-147

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: 441.03  E-value: 8.84e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  290 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDILFKEAIEAIA 369
Cdd:cd08625     3 DMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEAIA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  370 ESAFKTSPYPVILSFENHVDSPRQQAKMAEYCRSMFGETLLTDPLENFPLKPGIPLPSPEDLRGKILIKNKKnqfsgpas 449
Cdd:cd08625    83 ESAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK-------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  450 pskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSLVN 529
Cdd:cd08625   155 --------------------------------------------------------------------------MSTLVN 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  530 YIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVALN 609
Cdd:cd08625   161 YIEPVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPMEFVEYNKKQLSRIYPKGTRVDSSNYMPQLFWNVGCQMVALN 240

                         330
                  ....*....|....*...
gi 595763333  610 FQTMDLPMQQNMALFEFN 627
Cdd:cd08625   241 FQTLDLAMQLNMGVFEYN 258
PI-PLCc_eukaryota cd08558
Catalytic domain of eukaryotic phosphoinositide-specific phospholipase C and similar proteins; ...
 288-627 1.27e-133

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: 405.30  E-value: 1.27e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEA 367
Cdd:cd08558     1 YQDMTQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGHTLTSKILFKDVIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLTDPLENFPlkpgIPLPSPEDLRGKILIKNKKNQfsgp 447
Cdd:cd08558    79 IKEYAFVTSPYPVILSLENHC-SLEQQKKMAQILKEIFGDKLLTPPLDENP----VQLPSPEQLKGKILIKGKKYH---- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtayeemssl 527
Cdd:cd08558       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 vnyiqptkfisfefsaqknrsyvVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08558   150 -----------------------MSSFSETKALKLLKESPEEFVKYNKRQLSRVYPKGTRVDSSNYNPQPFWNAGCQMVA 206

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08558   207 LNYQTPDLPMQLNQGKFEQN 226
PI-PLCc_beta1 cd08623
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1; This subfamily ...
 289-627 8.15e-129

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: 394.06  E-value: 8.15e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  289 QDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDILFKEAIEAI 368
Cdd:cd08623     2 EDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  369 AESAFKTSPYPVILSFENHVDSPRQQAKMAEYCRSMFGETLLTDPLENFPLKPGIPLPSPEDLRGKILIKNKKnqfsgpa 448
Cdd:cd08623    82 AECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKK------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  449 spskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSLV 528
Cdd:cd08623   155 ---------------------------------------------------------------------------MSNLV 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  529 NYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVAL 608
Cdd:cd08623   160 NYIQPVKFESFEASKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVAL 239

                         330
                  ....*....|....*....
gi 595763333  609 NFQTMDLPMQQNMALFEFN 627
Cdd:cd08623   240 NFQTVDLSMQINMGMYEYN 258
PI-PLCc_beta4 cd08626
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4; This subfamily ...
 288-627 1.29e-128

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: 393.36  E-value: 1.29e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDILFKEAIEA 367
Cdd:cd08626     1 YQDMDQPLAHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCIELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVDSPrQQAKMAEYCRSMFGETLLTDPLENFPLKPGIPLPSPEDLRGKILIKNKKnqfsgp 447
Cdd:cd08626    81 IKDTAFVTSDYPVILSFENHCSKP-QQYKLAKYCEEIFGDLLLTKPLESHPLEPGVPLPSPNKLKRKILIKNKR------ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSL 527
Cdd:cd08626   154 ----------------------------------------------------------------------------LSSL 157

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 VNYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08626   158 VNYAQPVKFQGFDVAEERNIHFNMSSFNESVGLGYLKTSAIEFVNYNKRQMSRIYPKGTRVDSSNYMPQIFWNAGCQMVS 237

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08626   238 LNFQTPDLGMQLNQGKFEYN 257
PI-PLCc_delta cd08593
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta; This subfamily ...
 288-627 4.32e-112

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


Pssm-ID: 176535 [Multi-domain]  Cd Length: 257  Bit Score: 349.71  E-value: 4.32e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEA 367
Cdd:cd08593     1 YQDMTQPLSHYFIASSHNTYLLEDQLKGPSSTEAYIRALKKGCRCVELDCWDG--PDGEPIIYHGHTLTSKILFKDVIQA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLTDPLENfplkPGIPLPSPEDLRGKILIKNKKNQFSgp 447
Cdd:cd08593    79 IREYAFKVSPYPVILSLENHC-SVEQQKVMAQHLKSILGDKLLTQPLDG----VLTALPSPEELKGKILVKGKKLKLA-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSL 527
Cdd:cd08593   152 --------------------------------------------------------------------------KELSDL 157

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 VNYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08593   158 VIYCKSVHFKSFEHSKENYHFYEMSSFSESKALKLAQESGNEFVRHNKRQLSRIYPAGLRTDSSNYDPQEMWNVGCQIVA 237

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08593   238 LNFQTPGEEMDLNDGLFRQN 257
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 288-627 4.05e-103

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: 326.14  E-value: 4.05e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFS-----GLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTtDILFK 362
Cdd:cd00137     1 HHPDTQPLAHYSIPGTHDTYLTAGQFTikqvwGLTQTEMYRQQLLSGCRCVDIRCWDG--KPEEPIIYHGPTFL-DIFLK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  363 EAIEAIAESAFKTSPYPVILSFENHVDS-PRQQAKMAEYCRSMFGETLLTdplenFPLKPGIPLPSPEDLRGKILIKNKK 441
Cdd:cd00137    78 EVIEAIAQFLKKNPPETIIMSLKNEVDSmDSFQAKMAEYCRTIFGDMLLT-----PPLKPTVPLPSLEDLRGKILLLNKK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  442 NQFSGPASPSKKPGGVaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtay 521
Cdd:cd00137   153 NGFSGPTGSSNDTGFV---------------------------------------------------------------- 168

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  522 eemsslvnyiqptkfiSFEFSAQKNRSYVVSSFTELKAYE----LLSKASMQFVDYNKRQMSRVYPKGTR---------M 588
Cdd:cd00137   169 ----------------SFEFSTQKNRSYNISSQDEYKAYDdekvKLIKATVQFVDYNKNQLSRNYPSGTSggtawyyyaM 232

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 595763333  589 DSSNYMPQMFWN---AGCQMVALNFQTMDLPMQQNMALFEFN 627
Cdd:cd00137   233 DSNNYMPQMFWNanpAGCGIVILDFQTMDLPMQQYMAVIEFN 274
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 126-276 9.18e-98

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: 306.80  E-value: 9.18e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  126 DKILVKLKMQLNPEGKIPVKNFFQMFPADRKRVEAALGACHLAKGKNDAINPEDFPESVYKSFLMSLCPRPEIDEIFTSY 205
Cdd:cd16209     1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 595763333  206 HSKAKPYMTKEHLTKFINQKQRDPRLNSLLFPPARPEQVQVLIDKYEPSGINVQRGQLSPEGMVWFLCGPE 276
Cdd:cd16209    81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PI-PLCc_PRIP_metazoa cd08597
Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein; This ...
 288-627 4.57e-92

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


Pssm-ID: 176539 [Multi-domain]  Cd Length: 260  Bit Score: 295.87  E-value: 4.57e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEA 367
Cdd:cd08597     1 CQDMTQPLSHYFIASSHNTYLIEDQLRGPSSVEGYVRALQRGCRCVELDCWDG--PNGEPVIYHGHTLTSKISFRSVIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLTDPlenfPLKPGIPLPSPEDLRGKILIKNKKnqfsgp 447
Cdd:cd08597    79 INEYAFVASEYPLILCIENHC-SEKQQLVMAQYLKEIFGDKLYTEP----PNEGESYLPSPHDLKGKIIIKGKK------ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeIKKMQsdegtaglevtAYEEMSSL 527
Cdd:cd08597   148 --------------------------------------------------------LKRRK-----------LCKELSDL 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 VNYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08597   161 VSLCKSVRFQDFPTSAQNQKYWEVCSFSENLARRLANEFPEDFVNYNKKFLSRVYPSPMRVDSSNYNPQDFWNCGCQIVA 240

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08597   241 MNYQTPGLMMDLNTGKFLEN 260
PI-PLC1c_yeast cd08598
Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This ...
 289-624 3.69e-87

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: 281.44  E-value: 3.69e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  289 QDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEAI 368
Cdd:cd08598     2 EDLSRPLNEYFISSSHNTYLLGRQLAGDSSVEGYIRALQRGCRCVEIDVWDG--DDGEPVVTHGYTLTSSVPFRDVCRAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  369 AESAFKTSPYPVILSFENHVDsPRQQAKMAEYCRSMFGETLLTDPLENFPLKpgipLPSPEDLRGKILIKNKKNqfsgpa 448
Cdd:cd08598    80 KKYAFVTSPYPLILSLEVHCD-AEQQERMVEIMKETFGDLLVTEPLDGLEDE----LPSPEELRGKILIKVKKE------ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  449 spSKKPggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtayeemsslv 528
Cdd:cd08598   149 --SKTP-------------------------------------------------------------------------- 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  529 nyiqptkfiSFEFsaqknrsyvvsSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVAL 608
Cdd:cd08598   153 ---------NHIF-----------SLSERSLLKLLKDKRAALDKHNRRHLMRVYPSGTRISSSNFNPLPFWRAGVQMVAL 212

                         330
                  ....*....|....*.
gi 595763333  609 NFQTMDLPMQQNMALF 624
Cdd:cd08598   213 NWQTYDLGMQLNEAMF 228
PI-PLCc_gamma cd08592
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma; This family ...
 289-627 9.55e-87

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: 280.08  E-value: 9.55e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  289 QDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEAI 368
Cdd:cd08592     2 QDMNNPLSHYWIASSHNTYLTGDQLSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPIIYHGHTLTSKIKFMDVLKTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  369 AESAFKTSPYPVILSFENHVDSPrQQAKMAEYCRSMFGETLLTDPLEnfplKPGIPLPSPEDLRGKILIKNKKnqfsgpa 448
Cdd:cd08592    80 KEHAFVTSEYPVILSIENHCSLP-QQRNMAQAFKEVFGDMLLTQPVD----RNADQLPSPNQLKRKIIIKHKK------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  449 spskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMsslv 528
Cdd:cd08592   148 -----------------------------------------------------------------------LFYEM---- 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  529 nyiqptkfisfefsaqknrsyvvSSFTELKAYELLSKA-SMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08592   153 -----------------------SSFPETKAEKYLNRQkGKIFLKYNRRQLSRVYPKGQRVDSSNYDPVPMWNCGSQMVA 209

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08592   210 LNFQTPDKPMQLNQALFMLN 229
PI-PLCc_delta3 cd08630
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily ...
 288-627 5.22e-86

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


Pssm-ID: 176567 [Multi-domain]  Cd Length: 258  Bit Score: 279.21  E-value: 5.22e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEA 367
Cdd:cd08630     1 FQDMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEG--PGGEPVIYHGHTLTSKILFRDVIQA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLTDPLENFPLKpgiPLPSPEDLRGKILIKNKKNQFSgp 447
Cdd:cd08630    79 VRQHAFTASPYPVILSLENHC-GLEQQAAMARHLQTILGDMLVTQPLDSLNPE---ELPSPEELKGRVLVKGKKLQIS-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSL 527
Cdd:cd08630   153 --------------------------------------------------------------------------PELSAL 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 VNYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08630   159 AVYCQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQEMWNSGCQLVA 238

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08630   239 LNFQTPGYEMDLNAGRFLVN 258
PI-PLCc_zeta cd08595
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta; This family ...
 288-627 1.49e-85

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: 277.97  E-value: 1.49e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKppDEEPIITHGFTMTTDILFKEAIEA 367
Cdd:cd08595     1 YQDMDHPLSDYFISSSHNTYLVSDQLVGPSDLDGYVSALRKGCRCLEIDCWDGA--DNEPVVYHGYTLTSKILFKEVITT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLTDPLENFPLKpgiPLPSPEDLRGKILIKNKKnqfsgp 447
Cdd:cd08595    79 VEKYAFEKSDYPVVLSLENHC-STEQQEIMAHYLVSILGEKLLRAPIDDPATG---ELPSPEALKFKILVKNKK------ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeEIKKMQSDegtaglevtayeemssL 527
Cdd:cd08595   149 -------------------------------------------------------KIAKALSD----------------L 157

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 VNYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08595   158 VIYTKSEKFCSFTHSRDNQHSYENNSIGENKARKLLKSSGADFVGHTQRFITRIYPKGTRASSSNYNPQEFWNVGCQMVA 237

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08595   238 LNFQTLGAPMDLQNGKFLDN 257
PI-PLCc_delta4 cd08631
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4; This subfamily ...
 288-627 3.42e-84

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: 274.13  E-value: 3.42e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEA 367
Cdd:cd08631     1 YQDMTQPLCHYFICSSHNTYLMEDQLRGQSSVEGYIRALKRGCRCVEVDVWDG--PNGEPIVYHGHTFTSKILFKDVVAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLTDPLENfplKPGIPLPSPEDLRGKILIKNKKNQFSgp 447
Cdd:cd08631    79 VAQYAFQVSDYPVILSLENHC-GVEQQQTMAQHLTEILGEKLLSTTLDG---VLPTQLPSPEELRGKILLKGKKIRLS-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSL 527
Cdd:cd08631   153 --------------------------------------------------------------------------PELSDC 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 VNYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08631   159 VIYCKSVSFRSFTHSREHYHFYEISSFTETKARKLIREAGNEFVQHNTWQLSRVYPSGLRTDSSNYNPQEMWNAGCQMVA 238

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08631   239 LNFQTAGLEMDLNDGLFRQN 258
PI-PLCc_delta1 cd08629
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily ...
 288-627 3.05e-81

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: 266.13  E-value: 3.05e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEA 367
Cdd:cd08629     1 YQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDG--PNQEPIIYHGYTFTSKILFCDVLRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLTDPLENFPLKpgipLPSPEDLRGKILIKNKKNQFSgp 447
Cdd:cd08629    79 IRDYAFKASPYPVILSLENHC-SLEQQRVMARHLRAILGPILLDQPLDGVTTS----LPSPEQLKGKILLKGKKLKLV-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSL 527
Cdd:cd08629   152 --------------------------------------------------------------------------PELSDM 157

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 VNYIQPTKFISFEFSAQKNRS-YVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMV 606
Cdd:cd08629   158 IIYCKSVHFGGFSSPGTSGQAfYEMASFSESRALRLLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIV 237

                         330       340
                  ....*....|....*....|.
gi 595763333  607 ALNFQTMDLPMQQNMALFEFN 627
Cdd:cd08629   238 ALNFQTPGPEMDVYLGCFQDN 258
PI-PLCc_epsilon cd08596
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon; This family ...
 289-627 4.74e-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: 262.86  E-value: 4.74e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  289 QDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKppDEEPIITHGFTMTTDILFKEAIEAI 368
Cdd:cd08596     2 EDLQYPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLTGCRCVELDCWDGD--DGMPIIYHGHTLTTKIPFKDVVEAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  369 AESAFKTSPYPVILSFENHVDSPrQQAKMAEYCRSMFGETLLTDPL--ENFPLKPGipLPSPEDLRGKILIKNKKNQfsg 446
Cdd:cd08596    80 NRSAFITSDYPVILSIENHCSLQ-QQRKMAEIFKTVFGEKLVTKFLfeSDFSDDPS--LPSPLQLKNKILLKNKKAP--- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  447 paspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtayeEMSS 526
Cdd:cd08596   154 ----------------------------------------------------------------------------ELSD 157

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  527 LVNYIQPTKFISFEFSaqknRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMV 606
Cdd:cd08596   158 LVIYCQAVKFPGLSTP----KCYHISSLNENAAKRLCRRYPQKLVQHTRCQLLRTYPAATRIDSSNPNPLIFWLHGLQLV 233

                         330       340
                  ....*....|....*....|.
gi 595763333  607 ALNFQTMDLPMQQNMALFEFN 627
Cdd:cd08596   234 ALNYQTDDLPMHLNAAMFEAN 254
PI-PLCc_eta cd08594
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta; This family ...
 288-627 7.12e-78

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


Pssm-ID: 176536 [Multi-domain]  Cd Length: 227  Bit Score: 255.50  E-value: 7.12e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEA 367
Cdd:cd08594     1 NQDMTQPLSHYFIASSHNTYLTGDQLLSQSRVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKILFRDVIET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLtdpLENFPLKPGIPLPSPEDLRGKILIKNKKNQfsgp 447
Cdd:cd08594    79 INKYAFIKNEYPVILSIENHC-SVQQQKKMAQYLKEILGDKLD---LSSVISGDSKQLPSPQSLKGKILIKGKKWQ---- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtayeemssl 527
Cdd:cd08594       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 vnyiqptkfisfefsaqknrsyvVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08594   151 -----------------------VSSFSETRAHQIVQQKAAQFLRFNQRQLSRIYPSAYRIDSSNFNPQPYWNAGCQLVA 207

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08594   208 LNYQTEGRMLQLNRAKFRAN 227
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 291-439 1.68e-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: 250.89  E-value: 1.68e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   291 MTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEAIAE 370
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 595763333   371 SAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLTDPLENfplkPGIPLPSPEDLRGKILIKN 439
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLDD----DLTELPSPEDLKGKILIKG 142
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 951-1126 4.12e-77

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


Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 251.52  E-value: 4.12e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   951 PRVQELKDRLEQELQQQGEEQYRSVLKRKEQHVTEQIAKMMELAREKQAAELKTFKETSETDTKEMKKKLEAKRLERIQA 1030
Cdd:pfam08703    1 KQVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  1031 MTKVTTDKVAQERLKREINNSHIQEVVQAVKQMTETLERHQEKLEERQTACLEQIQAMEKQFQEKALAEYEAKMKGLEAE 1110
Cdd:pfam08703   81 AKKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAE 160

                          170
                   ....*....|....*.
gi 595763333  1111 VKESVRAYFKDCFPTE 1126
Cdd:pfam08703  161 VRESVKSCLKEGFPDE 176
PI-PLCc_eta2 cd08633
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily ...
 288-627 4.55e-77

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: 254.58  E-value: 4.55e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEA 367
Cdd:cd08633     1 NQDMTQPLSHYFITSSHNTYLSGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDG--PDGEPIVHHGYTLTSKILFKDVIET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVDSPrQQAKMAEYCRSMFGETLLTDPLENfplKPGIPLPSPEDLRGKILIKNKKnqfsgp 447
Cdd:cd08633    79 INKYAFIKNEYPVILSIENHCSVP-QQKKMAQYLTEILGDKLDLSSVIS---NDCTRLPSPEILKGKILVKGKK------ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMSSL 527
Cdd:cd08633   149 ------------------------------------------------------------------------LSRALSDL 156

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 VNYIQPTKFISFEfsAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08633   157 VKYTKSVRVHDIE--TEATSSWQVSSFSETKAHQILQQKPAQYLRFNQRQLSRIYPSSYRVDSSNYNPQPFWNAGCQMVA 234

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08633   235 LNYQSEGRMLQLNRAKFSAN 254
PI-PLCc_gamma2 cd08628
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2; This subfamily ...
 289-627 3.09e-72

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: 241.11  E-value: 3.09e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  289 QDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEAI 368
Cdd:cd08628     2 QDMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRMGCRCIELDCWDG--PDGKPIIYHGWTRTTKIKFDDVVQAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  369 AESAFKTSPYPVILSFENHVDSpRQQAKMAEYCRSMFGETLLTDPLEnfplKPGIPLPSPEDLRGKILIKNKKnqfsgpa 448
Cdd:cd08628    80 KDHAFVTSEYPVILSIEEHCSV-EQQRHMAKVFKEVFGDKLLMKPLE----ASADQLPSPTQLKEKIIIKHKK------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  449 spskkpggvaegsLPSSvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtayeEMSSLV 528
Cdd:cd08628   148 -------------LIAI---------------------------------------------------------ELSDLV 157

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  529 NYIQPTkfiSFEFSAQKNRSYV-VSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08628   158 VYCKPT---SKTKDNLENPDFKeIRSFVETKAPSIIRQKPVQLLKYNRKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVA 234

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08628   235 LNFQTADKYMQLNHALFSLN 254
PI-PLCc_eta1 cd08632
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily ...
 288-627 3.20e-68

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: 229.53  E-value: 3.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEA 367
Cdd:cd08632     1 NQDMDQPLCNYFIASSHNTYLTGDQLLSQSKVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKITFRDVIET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLTDPLENFPLKpgiPLPSPEDLRGKILIKNKKnqfsgp 447
Cdd:cd08632    79 INKYAFVKNEFPVILSIENHC-SIQQQKKIAQYLKEIFGDKLDLSSVLTGDPK---QLPSPQLLKGKILVKGKK------ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMSSL 527
Cdd:cd08632   149 ------------------------------------------------------------------------LCRDLSDL 156

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 VNYiqpTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08632   157 VVY---TNSVAAQDIVDDGSTGNVLSFSETRAHQLVQQKAEQFMTYNQKQLTRIYPSAYRIDSSNFNPLPYWNVGCQLVA 233

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08632   234 LNYQSEGRMMQLNRAKFMVN 253
PI-PLCc_gamma1 cd08627
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily ...
 289-627 9.57e-68

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


Pssm-ID: 176564 [Multi-domain]  Cd Length: 229  Bit Score: 227.22  E-value: 9.57e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  289 QDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEAI 368
Cdd:cd08627     2 EEMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPVIYHGHTLTTKIKFSDVLHTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  369 AESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLTDPLEnfplKPGIPLPSPEDLRGKILIKNKKnqfsgpa 448
Cdd:cd08627    80 KEHAFVTSEYPIILSIEDHC-SIVQQRNMAQHFKKVFGDMLLTKPVD----INADGLPSPNQLKRKILIKHKK------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  449 spskkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMsslv 528
Cdd:cd08627   148 -----------------------------------------------------------------------LYRDM---- 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  529 nyiqptkfisfefsaqknrsyvvSSFTELKAYELLSKAS-MQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08627   153 -----------------------SSFPETKAEKYVNRSKgKKFLQYNRRQLSRIYPKGQRLDSSNYDPLPMWICGSQLVA 209

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08627   210 LNFQTPDKPMQMNQALFMLG 229
EFh_PI-PLCbeta cd16200
EF-hand motif found in metazoan phosphoinositide-specific phospholipase C (PI-PLC)-beta ...
 126-276 1.57e-64

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: 215.19  E-value: 1.57e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  126 DKILVKLKMQLNPEGKIPVKNFFQMFPAD--RKRVEAALGACHLAKGKNDAINPEDFPESVYKSFLMSLCPRPEIDEIFT 203
Cdd:cd16200     1 KKLYTKLKLSVNITGKIPVKNIIKCFSSDkkRKRVLKALKALGLPDGKNDEIDPEDFTFEKFFKLYNKLCPRPDIDEIFK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 595763333  204 SYHSKAKPYMTKEHLTKFINQKQRDPRLNSLLFPPARPEQVQVLIDKYEPSGINVQRGQLSPEGMVWFLCGPE 276
Cdd:cd16200    81 ELGGKRKPYLTLEQLVDFLNEEQRDPRLNEILFPFHTKEQAKKLIDKYEPNEKNKKKGQLTLEGFLRYLMSDE 153
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 525-639 8.70e-63

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


Pssm-ID: 128454 [Multi-domain]  Cd Length: 115  Bit Score: 208.63  E-value: 8.70e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333    525 SSLVNYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQ 604
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 595763333    605 MVALNFQTMDLPMQQNMALFEFNGQSGYLLKHEFM 639
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 291-440 2.60e-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: 208.29  E-value: 2.60e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333    291 MTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDILFKEAIEAIAE 370
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDG--PDGEPVIYHGHTFTLPIKLSEVLEAIKD 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333    371 SAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLTDPLENFPLKpgipLPSPEDLRGKILIKNK 440
Cdd:smart00148   79 FAFVTSPYPVILSLENHC-SPDQQAKMAQMFKEIFGDMLYTPPLTSSLEV----LPSPEQLRGKILLKVR 143
EFh_PI-PLCbeta1 cd16208
EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1); PI-PLC-beta1, ...
 126-276 5.10e-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: 202.42  E-value: 5.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  126 DKILVKLKMQLNPEGKIPVKNFFQMFPADRKRVEAALGACHLAKGKNDAINPEDFPESVYKSFLMSLCPRPEIDEIFTSY 205
Cdd:cd16208     1 EKAYTKLKLQVNPEGRIPVKNIYRLFSADRKRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDHIFSEF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 595763333  206 HSKAKPYMTKEHLTKFINQKQRDPRLNSLLFPPARPEQVQVLIDKYEPSGINVQRGQLSPEGMVWFLCGPE 276
Cdd:cd16208    81 GAKSKPYLSVDQMTEFINSKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSTLAKKGQISVDGFMRYLSGEE 151
PI-PLCc_plant cd08599
Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family ...
 288-627 6.88e-59

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: 202.22  E-value: 6.88e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDeePIITHGFTMTTDILFKEAIEA 367
Cdd:cd08599     1 HHDMTAPLSHYFIFSSHNSYLTGNQLSSRSSTAPIIEALLRGCRVIELDLWPGGRGD--ICVLHGGTLTKPVKFEDCIKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  368 IAESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLTDPlenfPLKPGIPLPSPEDLRGKILIknkknqfsgp 447
Cdd:cd08599    79 IKENAFTASEYPVIITLENHL-SPELQAKAAQILRETLGDKLFYPD----SEDLPEEFPSPEELKGKILI---------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  448 aspSKKPggvaegslpssvPVEedtgwtaedrteveeeevveeeeeeeSGNLDEEEIKkmqsdegtaglevtayeemssl 527
Cdd:cd08599   144 ---SDKP------------PVI--------------------------RNSLSETQLK---------------------- 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  528 vnyiqptkfisfefsaqknrsyvvssftelKAYELLSKASMqfVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVA 607
Cdd:cd08599   161 ------------------------------KVIEGEHPTDL--IEFTQKNLLRVYPAGLRITSSNYDPMLAWMHGAQMVA 208

                         330       340
                  ....*....|....*....|
gi 595763333  608 LNFQTMDLPMQQNMALFEFN 627
Cdd:cd08599   209 LNMQGYDRPLWLNRGKFRAN 228
PLN02952 PLN02952
phosphoinositide phospholipase C
 287-775 2.58e-57

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 209.47  E-value: 2.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  287 IHQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEePIITHGFTMTTDILFKEAIE 366
Cdd:PLN02952  121 VHHDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGSTKDE-ILVLHGRTLTTPVPLIKCLK 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  367 AIAESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLL---TDPLENFPlkpgiplpSPEDLRGKILIKNKKN- 442
Cdd:PLN02952  200 SIRDYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLYypeSDSLVQFP--------SPESLKHRIIISTKPPk 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  443 ---QFSGPASPSKKpGGVAEGSLPSSVPVEEDTGWTAEDRTEVEEEEVVEEEEEEESGNLDEEEIKKMqsdegtagLEVT 519
Cdd:PLN02952  271 eylESSGPIVIKKK-NNVSPSGRNSSEETEEAQTLESMLFEQEADSRSDSDQDDNKSGELQKPAYKRL--------ITIH 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  520 AYEEMSSLVNYIQptkfisfeFSAQKNRSYvvsSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFW 599
Cdd:PLN02952  342 AGKPKGTLKDAMK--------VAVDKVRRL---SLSEQELEKAATTNGQDVVRFTQRNILRIYPKGTRITSSNYKPLIGW 410

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  600 NAGCQMVALNFQTMDLPMQQNMALFEFNGQSGYLLKHEFMrrLDKQFNPFSVD-RIDVVVATTLSITIISG--------- 669
Cdd:PLN02952  411 MHGAQMIAFNMQGYGKSLWLMHGMFRANGGCGYLKKPDFL--MKKGFHDEVFDpKKKLPVKKTLKVKVYLGdgwrldfsh 488

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  670 -QFLSERSVRTYVEVELFGLPGDPKRRyRTKLspTANSINPVWKEEpFIFeKILMPELASLRIAV----MEEGSKFLGHR 744
Cdd:PLN02952  489 tHFDSYSPPDFYTKMYIVGVPADNAKK-KTKI--IEDNWYPAWNEE-FSF-PLTVPELALLRIEVreydMSEKDDFGGQT 563

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 595763333  745 IIPINALHSGYHHLCLRSE-----SNMALTMPALFV 775
Cdd:PLN02952  564 CLPVSELRPGIRSVPLHDKkgeklKNVRLLMRFIFV 599
PI-PLC-Y pfam00387
Phosphatidylinositol-specific phospholipase C, Y domain; This associates with pfam00388 to ...
 524-638 3.00e-57

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


Pssm-ID: 459794  Cd Length: 114  Bit Score: 192.68  E-value: 3.00e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   524 MSSLVNYIQPTKFISFEfSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGC 603
Cdd:pfam00387    1 LSDLVVYTQSVKFKSFS-TPESKTPNHIFSFSESKALKLIKSSSAAFVKHNRRHLMRVYPKGTRVDSSNFNPQPFWNCGV 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 595763333   604 QMVALNFQTMDLPMQQNMALFEFNGQSGYLLKHEF 638
Cdd:pfam00387   80 QMVALNWQTPDEGMQLNEGMFADNGGCGYVLKPEF 114
PLN02222 PLN02222
phosphoinositide phospholipase C 2
 196-778 7.75e-56

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 204.49  E-value: 7.75e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  196 PEIDEIFTSYHSKAkpYMTKEHLTKFINQKQRDPRlnsllfppARPEQVQVLIDKyepSGINVQRGQLSPEGMVWFLCGP 275
Cdd:PLN02222   25 REIKTIFEKYSENG--VMTVDHLHRFLIDVQKQDK--------ATREDAQSIINS---ASSLLHRNGLHLDAFFKYLFGD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  276 ENSVLAHDTllIHQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIItHGFTM 355
Cdd:PLN02222   92 NNPPLALHE--VHHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSDKDDIDVL-HGMTL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  356 TTDILFKEAIEAIAESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLTDP----LENFPlkpgiplpSPEDL 431
Cdd:PLN02222  169 TTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHL-TPDLQSKVAEMVTEIFGEILFTPPvgesLKEFP--------SPNSL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  432 RGKILIKNKknqfsgpaSPSKKPGGVAEGSLPSSVPVEEDTGWTAEdrTEVEEEEVVEEEEEEESGNLDEEEikkmqsDE 511
Cdd:PLN02222  240 KKRIIISTK--------PPKEYKEGKDDEVVQKGKDLGDEEVWGRE--VPSFIQRNKSVDKNDSNGDDDDDD------DD 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  512 GTAGLEVTAYEEMSSLV--NYIQPTKFIS--FEFSAQKNRSYVVSSFTELKAYEllsKASMQFVDYNKRQMSRVYPKGTR 587
Cdd:PLN02222  304 GEDKSKKNAPPQYKHLIaiHAGKPKGGITecLKVDPDKVRRLSLSEEQLEKAAE---KYAKQIVRFTQHNLLRIYPKGTR 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  588 MDSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMALFEFNGQSGYLLKHEFMRRLDKQFNPFSvDRIDVVVATTLSITII 667
Cdd:PLN02222  381 VTSSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKKPDLLLKSGSDSDIFD-PKATLPVKTTLRVTIY 459

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  668 SGQ----------FLSERSVRTYVEVELFGLPGDPKRRyrtKLSPTANSINPVWKEepfIFE-KILMPELASLRIAV--- 733
Cdd:PLN02222  460 MGEgwyfdfrhthFDQYSPPDFYTRVGIAGVPGDTVMK---KTKTLEDNWIPAWDE---VFEfPLTVPELALLRLEVhey 533

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*.
gi 595763333  734 -MEEGSKFLGHRIIPINALHSGYHHLCLRSESNMALTMPALFVFLE 778
Cdd:PLN02222  534 dMSEKDDFGGQTCLPVWELSQGIRAFPLHSRKGEKYKSVKLLVKVE 579
PLN02228 PLN02228
Phosphoinositide phospholipase C
 194-754 1.81e-53

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 197.18  E-value: 1.81e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  194 PRPEIDEIFTSYHSKAKpyMTKEHLTKFINQKQRDPRlnsllfppARPEQVQVLIDKYEPSGINVQRGQLSPEGMVWFLC 273
Cdd:PLN02228   22 PPVSIKRLFEAYSRNGK--MSFDELLRFVSEVQGERH--------AGLDYVQDIFHSVKHHNVFHHHGLVHLNAFYRYLF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  274 GPENSVLAHdTLLIHQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKgKPPDEEPIITHGF 353
Cdd:PLN02228   92 SDTNSPLPM-SGQVHHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWP-NPSGNAAEVRHGR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  354 TMTTDILFKEAIEAIAESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLL---TDPLENFPlkpgiplpSPED 430
Cdd:PLN02228  170 TLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHL-PPNLQAQVAKMLTKTFRGMLFrctSESTKHFP--------SPEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  431 LRGKILIKNKknqfsgpasPSKK--PGGVAEGSlpsSVPVEEDTGWTAEDRTeveeeevveeeeeeesgnldEEEIKKMQ 508
Cdd:PLN02228  241 LKNKILISTK---------PPKEylESKTVQTT---RTPTVKETSWKRVADA--------------------ENKILEEY 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  509 SDEGTAGLEvtaYEEMSSL--VNYIQPTKFIsfeFSAQKNRSYVVSsFTELKAYELLSKASMQFVDYNKRQMSRVYPKGT 586
Cdd:PLN02228  289 KDEESEAVG---YRDLIAIhaANCKDPLKDC---LSDDPEKPIRVS-MDEQWLETMVRTRGTDLVRFTQRNLVRIYPKGT 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  587 RMDSSNYMPQMFWNAGCQMVALNFQT--MDLPMQQNMalFEFNGQSGYLLKHEFMRRLDKQFNPFSvdriDVVVATTLSI 664
Cdd:PLN02228  362 RVDSSNYDPHVGWTHGAQMVAFNMQGhgKQLWIMQGM--FRANGGCGYVKKPRILLDEHTLFDPCK----RLPIKTTLKV 435

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  665 TIISGQ----------FLSERSVRTYVEVELFGLPGDPKrRYRTKLSptANSINPVWKEEPFIFEkILMPELASLRIAVM 734
Cdd:PLN02228  436 KIYTGEgwdldfhlthFDQYSPPDFFVKIGIAGVPRDTV-SYRTETA--VDQWFPIWGNDEFLFQ-LRVPELALLWFKVQ 511

                         570       580
                  ....*....|....*....|....
gi 595763333  735 EEGSK----FLGHRIIPINALHSG 754
Cdd:PLN02228  512 DYDNDtqndFAGQTCLPLPELKSG 535
EFh_PI-PLCbeta3 cd16210
EF-hand motif found in phosphoinositide phospholipase C beta 3 (PI-PLC-beta3); PI-PLC-beta3, ...
 127-276 8.09e-50

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


Pssm-ID: 320040  Cd Length: 151  Bit Score: 173.18  E-value: 8.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  127 KILVKLKMQLNPEGKIPVKNFFQMFPADRKRVEAALGACHLAKGKNDAINPEDFPESVYKSFLMSLCPRPEIDEIFTSYH 206
Cdd:cd16210     2 KAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILLEIG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  207 SKAKPYMTKEHLTKFINQKQRDPRLNSLLFPPARPEQVQVLIDKYEPSGINVQRGQLSPEGMVWFLCGPE 276
Cdd:cd16210    82 AKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQVRQLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 151
EFh_PI-PLC21 cd16213
EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family ...
 127-272 1.17e-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: 1.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  127 KILVKLKMQLNPEGKIPVKNFFQMFPA---DRKRVEAALGACHLAKGKNDAINPEDFPESVYKSFLMSLCPRPEIDEIFT 203
Cdd:cd16213     2 KAYTKLTLQTDKEGKIPVKNIVKMFAQhkdDRKRVEKALEAIGLPSGKNDAIDPKKFTFEDFFNFYRRLTGRQEVEKIFD 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 595763333  204 SYHSKAKPYMTKEHLTKFINQKQRDPRLNSLLFPPARPEQVQVLIDKYEPSGINVQRGQLSPEGMVWFL 272
Cdd:cd16213    82 ELGAKKKPYLTTEQFVDFLNKTQRDPRLNEILYPYANPKRARDLINQYEPNKSFAKKGHLSVEGFLRYL 150
PLN02230 PLN02230
phosphoinositide phospholipase C 4
 287-778 2.72e-45

phosphoinositide phospholipase C 4


Pssm-ID: 177875 [Multi-domain]  Cd Length: 598  Bit Score: 173.74  E-value: 2.72e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  287 IHQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDeePIITHGFTMTTDILFKEAIE 366
Cdd:PLN02230  113 VHQNMDAPLSHYFIFTGHNSYLTGNQLSSNCSELPIADALRRGVRVVELDLWPRGTDD--VCVKHGRTLTKEVKLGKCLD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  367 AIAESAFKTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLLTDPLENFPlkpgiPLPSPEDLRGKILIKNKKNQFSG 446
Cdd:PLN02230  191 SIKANAFAISKYPVIITLEDHL-TPKLQFKVAKMITQTFGDMLYYHDSEGCQ-----EFPSPEELKEKILISTKPPKEYL 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  447 PASPSKKPGGVAEGSlpssvPVEEDTGWTAEDRTEVEEEEVVEEEEEEESGNLDEEEIKKMQSDEgTAGLEVTAYEEMSS 526
Cdd:PLN02230  265 EANDAKEKDNGEKGK-----DSDEDVWGKEPEDLISTQSDLDKVTSSVNDLNQDDEERGSCESDT-SCQLQAPEYKRLIA 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  527 lVNYIQPTKFISFEFSAQKNRSYVVSSftelkAYELLSKASMQF----VDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAG 602
Cdd:PLN02230  339 -IHAGKPKGGLRMALKVDPNKIRRLSL-----SEQLLEKAVASYgadvIRFTQKNFLRIYPKGTRFNSSNYKPQIGWMSG 412

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  603 CQMVALNFQTMDLPMQQNMALFEFNGQSGYLLKHEFMRRLDKQFNPFsVDRIDVVVATTLSITIISGQF----LSERSVR 678
Cdd:PLN02230  413 AQMIAFNMQGYGRALWLMEGMFRANGGCGYVKKPDFLMDAGPNGQDF-YPKDNSCPKKTLKVKVCMGDGwlldFKKTHFD 491

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  679 TYVEVELF---GLPGDPKRRYRTKLSPTANSINPVWKEEpFIFeKILMPELASLRIAVME----EGSKFLGHRIIPINAL 751
Cdd:PLN02230  492 SYSPPDFFvrvGIAGAPVDEVMEKTKIEYDTWTPIWNKE-FIF-PLAVPELALLRVEVHEhdinEKDDFGGQTCLPVSEI 569

                         490       500
                  ....*....|....*....|....*..
gi 595763333  752 HSGYHHLCLRSESNMALTMPALFVFLE 778
Cdd:PLN02230  570 RQGIHAVPLFNRKGVKYSSTRLLMRFE 596
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 13-118 9.88e-45

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: 157.93  E-value: 9.88e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333    13 VKAYLSQGERFIKWDDETSIASP-VILRVDPKGYYLYWTYQN-----------------------QSQKLREVFNMDFPD 68
Cdd:pfam17787    2 VPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGkegevleitsirdtrlgkfakipKDPKLREVLSMGGSD 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 595763333    69 NHFLLKTLTVVSGPDMVDLTFYNFVSYKENVGKDWAEDVLALAKHPMTVN 118
Cdd:pfam17787   82 NSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 659-780 1.46e-36

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: 134.21  E-value: 1.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  659 ATTLSITIISGQFLS------ERSVRTYVEVELFGLPGDPKRRYRTKLSPtANSINPVWkEEPFIFEKIlMPELASLRIA 732
Cdd:cd00275     1 PLTLTIKIISGQQLPkpkgdkGSIVDPYVEVEIHGLPADDSAKFKTKVVK-NNGFNPVW-NETFEFDVT-VPELAFLRFV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 595763333  733 VMEE---GSKFLGHRIIPINALHSGYHHLCLRSESNMALTMPALFVFLEMK 780
Cdd:cd00275    78 VYDEdsgDDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-121 7.28e-34

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: 126.53  E-value: 7.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   17 LSQGERFIKWDDETSIASPVILRVDPKGYYLYWTYQNQS-----------------------QKLREVfNMDFPDNHFLL 73
Cdd:cd13361     1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKEtevldlslirdvrtgkypkdpkdLKEREV-NVGGSDEDLED 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 595763333   74 KTLTVVSGPDMVDLTFYNFVSYKENVGKDWAEDVLALAKHPMTVNAPR 121
Cdd:cd13361    80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
 131-272 3.28e-30

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: 117.14  E-value: 3.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  131 KLKMQLNPEGKIPVKNFFQMFPADR--KRVEAALGACHLAKGKNDAINPEDFPESVYKSFLMSLCPRPEIDEIFTSYHSK 208
Cdd:cd16211     6 RLCFLVNPNGKIPVRSITRTFASGKteKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFKKINGD 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 595763333  209 AKPYMTKEHLTKFINQKQRDPRLNSLLFPPARPEQVQVLIDKYEPSGINVQRGQLSPEGMVWFL 272
Cdd:cd16211    86 KKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYL 149
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 301-610 1.67e-24

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: 101.74  E-value: 1.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  301 NSSHNTYLTAGQfsgLSSAEMYRQVLLSGCRCVELDCWKGKppDEEPIITHGFTMT------TDILFKEAIEAIAESAFk 374
Cdd:cd08555     1 VLSHRGYSQNGQ---ENTLEAFYRALDAGARGLELDVRLTK--DGELVVYHGPTLDrttagiLPPTLEEVLELIADYLK- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  375 TSPYPVILSFENHVDS---PRQQAKMAEYCRSMFGetlltdplenfplkpgiplpspEDLRGKILIKnkknqfsgpasps 451
Cdd:cd08555    75 NPDYTIILSLEIKQDSpeyDEFLAKVLKELRVYFD----------------------YDLRGKVVLS------------- 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  452 kkpggvaegslpssvpveedtgwtaedrteveeeevveeeeeeesgnldeeeikkmqsdegtaglevtayeemsslvnyi 531
Cdd:cd08555       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  532 qptkfisfefsaqknrSYVVSSFTELKAYELLSKASMQFVDYNK-RQMSRVYPKGTrmdsSNYMPQMFWNAGCQMVALNF 610
Cdd:cd08555   120 ----------------SFNALGVDYYNFSSKLIKDTELIASANKlGLLSRIWTVND----NNEIINKFLNLGVDGLITDF 179
EFh_NorpA_like cd16212
EF-hand motif found in Drosophila melanogaster No receptor potential A protein (NorpA) and ...
 130-276 3.42e-24

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: 99.93  E-value: 3.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  130 VKLKMQLNPEGKIPVKNFFQMFPADR--KRVEAALGACHLAKGKNDAINPEDFPESVYKSFLMSLCPRPEIDEIFTSYHS 207
Cdd:cd16212     5 MRLGFMVDSGGKIPVKHIARTFASGKteKLVYQCLAEMGLPSGKGDSIEKEDFTFEKFYALYHKICPRNDIEELFTSITK 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 595763333  208 KAKPYMTKEHLTKFINQKQRDPRLNSLLFPPARPEQVQVLIDKYEPSGINVQRGQLSPEGMVWFLCGPE 276
Cdd:cd16212    85 GKGEHISLAQLINFMNDKQRDPRLNEILYPLYDEKRCTEIIKAYEQNEENIKNKRMSKDGFIRYLMSDE 153
PLN02223 PLN02223
phosphoinositide phospholipase C
 288-769 1.90e-23

phosphoinositide phospholipase C


Pssm-ID: 165867 [Multi-domain]  Cd Length: 537  Bit Score: 105.88  E-value: 1.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  288 HQDMTQPLNHYFINSSHNTYLTAGQ-FSGLSSAEMYRQVLLSGCRCVELDCWkgkPPDEEPI-ITHGFTMTTDILFKEAI 365
Cdd:PLN02223  105 HHDMHAPLSHYFIHTSLKSYFTGNNvFGKLYSIEPIIDALEQGVRVVELDLL---PDGKDGIcVRPKWNFEKPLELQECL 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  366 EAIAESAF-KTSPYPVILSFENHVdSPRQQAKMAEYCRSMFGETLL-TDP---LENFplkpgiplPSPEDLRGKILIknk 440
Cdd:PLN02223  182 DAIKEHAFtKCRSYPLIITFKDGL-KPDLQSKATQMIDQTFGDMVYhEDPqhsLEEF--------PSPAELQNKILI--- 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  441 knqfsgpaspSKKPggvaegslPSSVPVEEDTgwtaedrteveeeevveeeeEEESGNLDEEEIKKMQSDEGtaglevta 520
Cdd:PLN02223  250 ----------SRRP--------PKELLYAKAD--------------------DGGVGVRNELEIQEGPADKN-------- 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  521 YEEMSSLvNYIQPTKFIsfefsaQKNRSYVVSSFTELKAYEllskasMQFVDYNKRQMSRVYPKGTRMDS-SNYMPQMFW 599
Cdd:PLN02223  284 YQSLVGF-HAVEPRGML------QKALTGKADDIQQPGWYE------RDIISFTQKKFLRTRPKKKNLLInAPYKPQRAW 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  600 NAGCQMVALNFQTMDLPMQQNMALFEFNGQSGYLLKHEFMRRLDKQ--FNPfsvdRIDVVVATTLSITIISGQF----LS 673
Cdd:PLN02223  351 MHGAQLIALSRKDDKEKLWLMQGMFRANGGCGYVKKPDFLLNAGPSgvFYP----TENPVVVKILKVKIYMGDGwivdFK 426

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  674 ERSVR-----TYVEVELFGLPGDPKrryRTKLSPTANSINPVWKEEpFIFeKILMPELASLRIAV----MEEGSKFLGHR 744
Cdd:PLN02223  427 KRIGRlskpdLYVRISIAGVPHDEK---IMKTTVKNNEWKPTWGEE-FTF-PLTYPDLALISFEVydyeVSTADAFCGQT 501

                         490       500       510
                  ....*....|....*....|....*....|.
gi 595763333  745 IIPINALHSGYHHLCLRSE------SNMALT 769
Cdd:PLN02223  502 CLPVSELIEGIRAVPLYDErgkacsSTMLLT 532
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 661-757 1.20e-13

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: 67.90  E-value: 1.20e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333    661 TLSITIISGQFLSER----SVRTYVEVELFGlpgDPKRRYRTKLSPtaNSINPVWKEEpFIFEkILMPELASLRIAVMEE 736
Cdd:smart00239    1 TLTVKIISARNLPPKdkggKSDPYVKVSLDG---DPKEKKKTKVVK--NTLNPVWNET-FEFE-VPPPELAELEIEVYDK 73

                            90       100
                    ....*....|....*....|....*
gi 595763333    737 GS----KFLGHRIIPINALHSGYHH 757
Cdd:smart00239   74 DRfgrdDFIGQVTIPLSDLLLGGRH 98
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 172-276 1.81e-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: 68.79  E-value: 1.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  172 NDAINPEDFPEsvyksFLMSLCPRPEIDEIFTSYhSKAKPYMTKEHLTKFINQKQRDPRLNsllfpparPEQVQVLIDKY 251
Cdd:cd16202    50 EDVLDEEEFVQ-----FYNRLTKRPEIEELFKKY-SGDDEALTVEELRRFLQEEQKVKDVT--------LEWAEQLIETY 115

                          90       100
                  ....*....|....*....|....*
gi 595763333  252 EPSGINVQRGQLSPEGMVWFLCGPE 276
Cdd:cd16202   116 EPSEDLKAQGLMSLDGFTLFLLSPD 140
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 132-276 3.10e-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: 59.22  E-value: 3.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  132 LKMQLNPEGKIPVKNFFQM-----FPADRKRVEAALGACHlaKGKNDAINPEDFpesvyKSFLMSLCPRPEIDEIFTSYH 206
Cdd:cd15898     7 IKADKDGDGKLSLKEIKKLlkrlnIRVSEKELKKLFKEVD--TNGDGTLTFDEF-----EELYKSLTERPELEPIFKKYA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  207 SKAKPYMTKEHLTKFINQKQRDPRlnsllfppaRPEQVQVLIDKYEPsgiNVQRGQLSPEGMVWFLCGPE 276
Cdd:cd15898    80 GTNRDYMTLEEFIRFLREEQGENV---------SEEECEELIEKYEP---ERENRQLSFEGFTNFLLSPE 137
C2 pfam00168
C2 domain;
661-754 2.09e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 55.79  E-value: 2.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   661 TLSITIISGQFL----SERSVRTYVEVELfglpGDPKRRYRTKLSPtaNSINPVWKEEpFIFEkILMPELASLRIAVMEE 736
Cdd:pfam00168    2 RLTVTVIEAKNLppkdGNGTSDPYVKVYL----LDGKQKKKTKVVK--NTLNPVWNET-FTFS-VPDPENAVLEIEVYDY 73

                           90       100
                   ....*....|....*....|..
gi 595763333   737 GS----KFLGHRIIPINALHSG 754
Cdd:pfam00168   74 DRfgrdDFIGEVRIPLSELDSG 95
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 853-1113 5.87e-09

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: 60.46  E-value: 5.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   853 EEATKEVTEPQTASLEELRELKGVVKLQRRHEKELRELERRGARRWEELlQRGAAQLAELQTQAAGCKLRPGKGSRKKRT 932
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL-TELEAEIEELEERLEEAEEELAEAEAEIEE 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   933 LpcEETV-------VAPSEPHDRADPRVQELKDRLEQELQQQGEEQYRSVLKRKEQHVTEQIAKMMELAREKQAAELKTF 1005
Cdd:TIGR02168  787 L--EAQIeqlkeelKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  1006 KETSETDTKEMKKKLEAKRlERIQAMtkvttdkvAQERLKREINNSHIQEVVQAVKQMTETLERHQEKLEERQTAcLEQI 1085
Cdd:TIGR02168  865 EELIEELESELEALLNERA-SLEEAL--------ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR-LEGL 934

                          250       260
                   ....*....|....*....|....*...
gi 595763333  1086 QAMEKQFQEKALAEYEAKMKGLEAEVKE 1113
Cdd:TIGR02168  935 EVRIDNLQERLSEEYSLTLEEAEALENK 962
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 192-280 9.75e-09

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


Pssm-ID: 401279 [Multi-domain]  Cd Length: 85  Bit Score: 53.40  E-value: 9.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   192 LCPRPEIDEIFTSYhSKAKPYMTKEHLTKFINQKQRDPRlnsllfppARPEQVQVLIDKYEPSGINVQRGQLSPEGMVWF 271
Cdd:pfam09279    5 LTQREEIDEIFQEY-SGDGQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAMTKDGFLMY 75


                   ....*....
gi 595763333   272 LCGPENSVL 280
Cdd:pfam09279   76 LCSPDGSIF 84
PTZ00121 PTZ00121
MAEBL; Provisional
 853-1152 1.25e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  853 EEATKEVTEPQTASLEELRELKGVVKLQRRHEKELRELERRGAR--RWEELLQRGAAQLAELQTQAAgcKLRPGKGSRKK 930
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEeaRMAHFARRQAAIKAEEARKAD--ELKKAEEKKKA 1292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  931 RTLPCEETVVAPSEPHDRADP--RVQELKDRLEQELQQQGEEQYRSVLKRKEQHVT----EQIAKMMELAREK-QAAELK 1003
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAkaeaEAAADEAEAAEEKaEAAEKK 1372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1004 TFKETSETDtkEMKKKLEAKRlERIQAMTKVTTDKVAQERLKREinnshiqevvQAVKQMTETLERhqeKLEERQTAcle 1083
Cdd:PTZ00121 1373 KEEAKKKAD--AAKKKAEEKK-KADEAKKKAEEDKKKADELKKA----------AAAKKKADEAKK---KAEEKKKA--- 1433

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1084 qiQAMEKQFQEKALAEyEAKMKGLEAEVKESVRAYFKDCFPT-EAEDKPERSCEASEESCPQEPLVSKAD 1152
Cdd:PTZ00121 1434 --DEAKKKAEEAKKAD-EAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKAD 1500
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 662-756 2.66e-06

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: 47.06  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  662 LSITIISGQFL----SERSVRTYVEVELfglpgDPKRRYRTKLSPtaNSINPVWKEEpFIFEkILMPELASLRIAVMEEG 737
Cdd:cd00030     1 LRVTVIEARNLpakdLNGKSDPYVKVSL-----GGKQKFKTKVVK--NTLNPVWNET-FEFP-VLDPESDTLTVEVWDKD 71

                          90       100
                  ....*....|....*....|...
gi 595763333  738 S----KFLGHRIIPINALHSGYH 756
Cdd:cd00030    72 RfskdDFLGEVEIPLSELLDSGK 94
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
 186-276 2.88e-06

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


Pssm-ID: 320047 [Multi-domain]  Cd Length: 139  Bit Score: 47.81  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  186 KSFLMSLCPRPEIDEIFTSYhSKAKPYMTKEHLTKFINQKQRDPrlnsllfppARPEQVQVLIDKYEPSGINVQRGQLSP 265
Cdd:cd16217    59 EEFYKLLTKREEIDVIFGEY-AKSDGTMSRNNLLNFLQEEQREE---------VAPAYALSLIEKYEPDETAKAQRQMTK 128

                          90
                  ....*....|.
gi 595763333  266 EGMVWFLCGPE 276
Cdd:cd16217   129 DGFLMYLLSPE 139
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 662-778 5.45e-06

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


Pssm-ID: 176060 [Multi-domain]  Cd Length: 126  Bit Score: 46.98  E-value: 5.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  662 LSITIISGQFLSER--SVRTYVEVELfglpGDPKRRYRTklSPTANSINPVWkEEPFIFEkiLMPELASLRIAVMEEG-- 737
Cdd:cd08678     1 LLVKNIKANGLSEAagSSNPYCVLEM----DEPPQKYQS--STQKNTSNPFW-DEHFLFE--LSPNSKELLFEVYDNGkk 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 595763333  738 --SKFLGHRIIPINAL---HSGYHHLCLRS----ESNMALTMPALFVFLE 778
Cdd:cd08678    72 sdSKFLGLAIVPFDELrknPSGRQIFPLQGrpyeGDSVSGSITVEFLFME 121
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 857-1155 1.63e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.97  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   857 KEVTEPQTASLEELRELKgvvKLQRRHEKELRELERRgaRRWEEllqRGAAQLAELQTQAAgcklrpgkgsrkkrtLPCE 936
Cdd:pfam17380  282 KAVSERQQQEKFEKMEQE---RLRQEKEEKAREVERR--RKLEE---AEKARQAEMDRQAA---------------IYAE 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   937 ETVVAPSEPHDRADPRVQELKdrleqelqqqgeeqyRSVLKRKEQHVTEQIAKMMELAREKQAAELKTFKETSETDTKEM 1016
Cdd:pfam17380  339 QERMAMERERELERIRQEERK---------------RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARK 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  1017 KKKLEAKRLERIQamtkvtTDKVAQERLKREINNSHIQEVVQAVKQMTETLERHQEKLEERQTAC--LEQIQA------- 1087
Cdd:pfam17380  404 VKILEEERQRKIQ------QQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVerLRQQEEerkrkkl 477

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  1088 -MEKQFQEKALAEyEAKMKGLEAEVKESVRAYFKD-----CFPTEAEDK------PERSCEASEESCPQEPLVSKADTQE 1155
Cdd:pfam17380  478 eLEKEKRDRKRAE-EQRRKILEKELEERKQAMIEEerkrkLLEKEMEERqkaiyeEERRREAEEERRKQQEMEERRRIQE 556
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 981-1113 1.92e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 47.23  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  981 QHVTEQIAKMMELARE--KQAAELKTFKETSETDTKEMKKKLEAKRLERIQAMTKVTTDKVAQERLKREINNSHIQEVVQ 1058
Cdd:COG1579    13 QELDSELDRLEHRLKElpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 595763333 1059 AVKQMTETLERHQEKLEERQTACLEQIQAMEKQFQ--EKALAEYEAKMKGLEAEVKE 1113
Cdd:COG1579    93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAelEAELAELEAELEEKKAELDE 149
EFh_PI-PLCdelta4 cd16219
EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, ...
 188-276 2.61e-05

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


Pssm-ID: 320049 [Multi-domain]  Cd Length: 140  Bit Score: 45.22  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  188 FLMSLCPRPEIDEIFTSYhSKAKPYMTKEHLTKFINQKQRDPRLNSllfpparpEQVQVLIDKYEPSGINVQRGQLSPEG 267
Cdd:cd16219    61 FYKALTQREDVLKIFQDF-SADGQKLTLLEFVDFLQQEQLERENTE--------ELAMELIDRYEPSDTAKKLHALSIDG 131


                  ....*....
gi 595763333  268 MVWFLCGPE 276
Cdd:cd16219   132 FLMYLCSPE 140
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 976-1113 2.61e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.84  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  976 LKRKEQHVTEQIAKMMELAREKQAaELKTFKETSEtDTKEMKKKLEA------KRLERIQA-MTKVTTDKVAQ------E 1042
Cdd:COG1579    22 LEHRLKELPAELAELEDELAALEA-RLEAAKTELE-DLEKEIKRLELeieeveARIKKYEEqLGNVRNNKEYEalqkeiE 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 595763333 1043 RLKREIN--NSHIQEVVQAVKQMTETLERHQEKLEERQtaclEQIQAMEKQFqEKALAEYEAKMKGLEAEVKE 1113
Cdd:COG1579   100 SLKRRISdlEDEILELMERIEELEEELAELEAELAELE----AELEEKKAEL-DEELAELEAELEELEAEREE 167
PRK15422 PRK15422
septal ring assembly protein ZapB; Provisional
 1015-1094 3.38e-05

septal ring assembly protein ZapB; Provisional


Pssm-ID: 185320 [Multi-domain]  Cd Length: 79  Bit Score: 43.15  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1015 EMKKKLEAKRLeriQAMTKVTTDKVAQERLKrEINNSHIQEVvQAVKQMTETLERHQEKLEERQTACLEQIQAMEKQFQE 1094
Cdd:PRK15422    4 EVFEKLEAKVQ---QAIDTITLLQMEIEELK-EKNNSLSQEV-QNAQHQREELERENNHLKEQQNGWQERLQALLGRMEE 78
PTZ00121 PTZ00121
MAEBL; Provisional
 849-1140 4.47e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  849 KATGEEATKEVTEPQTAslEELR----ELKGVVKLQRRHEKELRELERrgARRWEELLQRGAAQLAELQTQAAgcKLRPG 924
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKA--DEAKkkaeEAKKKADEAKKAAEAKKKADE--AKKAEEAKKADEAKKAEEAKKAD--EAKKA 1542

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  925 KGSRKKRTLPCEETVvAPSEPHDRADPRVQELKDRLEQELQQqgeeqyrSVLKRKEQHVTEQIAKMMELAREKQAAELKt 1004
Cdd:PTZ00121 1543 EEKKKADELKKAEEL-KKAEEKKKAEEAKKAEEDKNMALRKA-------EEAKKAEEARIEEVMKLYEEEKKMKAEEAK- 1613

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1005 fKETSETDTKEMKKKLEAKRLERIQAMTKVTTDKVAQERLKREINNSHIQEVVQAVKQmtETLERHQEKLEERQTACLEQ 1084
Cdd:PTZ00121 1614 -KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA--EEDKKKAEEAKKAEEDEKKA 1690

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 595763333 1085 IQAMEKQFQEKALAEY------EAKMKGLEAEVKESVRAYFKDCFPTEAEDKPERSCEASEE 1140
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEElkkkeaEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 868-1119 5.24e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  868 EELR----ELKGVVKL-QRRHE--KELRE----LERRGARRwEELlqrgAAQLAELQTQAagcklrpgkgsRKKRtlpce 936
Cdd:COG1196   155 EERRaiieEAAGISKYkERKEEaeRKLEAteenLERLEDIL-GEL----ERQLEPLERQA-----------EKAE----- 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  937 etvvapsephdradpRVQELKDRLEQELQQQGEEQYRSV---LKRKEQHVTEQIAKMMELAREKQA--AELKTFKETSET 1011
Cdd:COG1196   214 ---------------RYRELKEELKELEAELLLLKLRELeaeLEELEAELEELEAELEELEAELAEleAELEELRLELEE 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1012 DTKEMKKKLEA-----KRLERIQAMTKVTTDKVAQERLKREINNSHIQEVVQAVKQMTETLERHQEKLEERQTAcLEQIQ 1086
Cdd:COG1196   279 LELELEEAQAEeyellAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE-LEEAE 357

                         250       260       270
                  ....*....|....*....|....*....|...
gi 595763333 1087 AMEKQfQEKALAEYEAKMKGLEAEVKESVRAYF 1119
Cdd:COG1196   358 AELAE-AEEALLEAEAELAEAEEELEELAEELL 389
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 858-1118 9.50e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 46.89  E-value: 9.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   858 EVTEPQTASLEELRELKGvvKLQRRHEKELRELERRGAR-RWEELLQRGAAQLAELQTQ-AAGCKLRPGKGSRKK--RTL 933
Cdd:TIGR00618  219 ERKQVLEKELKHLREALQ--QTQQSHAYLTQKREAQEEQlKKQQLLKQLRARIEELRAQeAVLEETQERINRARKaaPLA 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   934 PCEETVVAPSEPHDRADPRVQE---------------LKDRLEQELQQQGEEQYRSVLKRKEQHVTEQIAKMMELAREKQ 998
Cdd:TIGR00618  297 AHIKAVTQIEQQAQRIHTELQSkmrsrakllmkraahVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   999 AAE-LKTFKETSETDT---KEMKKKLE--------------AKRLERIQAMTKVTTDKVAQERLkrEINNSHIQEVVQAV 1060
Cdd:TIGR00618  377 LTQhIHTLQQQKTTLTqklQSLCKELDilqreqatidtrtsAFRDLQGQLAHAKKQQELQQRYA--ELCAAAITCTAQCE 454

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  1061 KQMTETLERHQEKLEERqTACLEQIQAMEKQFQEKALAEYEAK--MKGLEAEVKESVRAY 1118
Cdd:TIGR00618  455 KLEKIHLQESAQSLKER-EQQLQTKEQIHLQETRKKAVVLARLleLQEEPCPLCGSCIHP 513
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 978-1109 2.35e-04

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: 43.88  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   978 RKEQHVTEQIAKMMELAREKQAAELKTFK-ETSETDT--------KEMKKKLEAKRLERIQAMTKVTTDK-VAQERLkRE 1047
Cdd:pfam15665   61 SLEQHERMKRQALTEFEQYKRRVEERELKaEAEHRQRvvelsrevEEAKRAFEEKLESFEQLQAQFEQEKrKALEEL-RA 139

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 595763333  1048 INNSHIQEVVQAVKQMTETLERHQEKLEERQTACLEQIQA----MEKQFQeKALAEYEAKMKGLEA 1109
Cdd:pfam15665  140 KHRQEIQELLTTQRAQSASSLAEQEKLEELHKAELESLRKevedLRKEKK-KLAEEYEQKLSKAQA 204
PTZ00121 PTZ00121
MAEBL; Provisional
 853-1152 2.48e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  853 EEATKEVTEPQTAslEELRELKGVVKLQ--RRHEKELR-ELERRG--ARRWEELLQRGAAQLAELQTQA----AGCKLRP 923
Cdd:PTZ00121 1118 EEAKKKAEDARKA--EEARKAEDARKAEeaRKAEDAKRvEIARKAedARKAEEARKAEDAKKAEAARKAeevrKAEELRK 1195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  924 GKGSRKKRTLPCEETVVAPSEPHDRADPRVQELKDRLEQELQQQGEEQYRSVLKRKEQHVTEQIAKMMELAREKQAAELK 1003
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1004 TFKETSETDTKEMKKKL-EAKRLERIQAMTKVTtdKVAQERLKREINNSHIQEV---VQAVKQMTETLERHQEKLEERQT 1079
Cdd:PTZ00121 1276 EARKADELKKAEEKKKAdEAKKAEEKKKADEAK--KKAEEAKKADEAKKKAEEAkkkADAAKKKAEEAKKAAEAAKAEAE 1353

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 595763333 1080 ACLEQIQAMEKQFQEKALAEYEAKMKGLEAEVK-ESVRAyfkdcfPTEAEDKPERSCEASEESCPQEPLVSKAD 1152
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKaEEKKK------ADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
847-1113 2.68e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  847 GTKATGEEATKEVTEPQTASLEELRELKGVVK-----------------LQRRHEKELRELERRGArRWEELLQRGAAQL 909
Cdd:PRK03918  252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKelkelkekaeeyiklseFYEEYLDELREIEKRLS-RLEEEINGIEERI 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  910 AELQTQAAgcklRPGKGSRKKRTLPCEETVVAPS-EPHDRADP---RVQELKDRLEQELQQQGEEQYRSVLKRKEQ---- 981
Cdd:PRK03918  331 KELEEKEE----RLEELKKKLKELEKRLEELEERhELYEEAKAkkeELERLKKRLTGLTPEKLEKELEELEKAKEEieee 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  982 --HVTEQIAKMMELAREKQAA--ELKTFK--------ETSETDTKEMKKKLEAKrLERIQAMTKVTTDKvaQERLKREIN 1049
Cdd:PRK03918  407 isKITARIGELKKEIKELKKAieELKKAKgkcpvcgrELTEEHRKELLEEYTAE-LKRIEKELKEIEEK--ERKLRKELR 483

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1050 NSHI----QEVVQAVKQMTETLERHQEKLEERQtacLEQIQAMEKQFQE--KALAEYEAKMKGLEAEVKE 1113
Cdd:PRK03918  484 ELEKvlkkESELIKLKELAEQLKELEEKLKKYN---LEELEKKAEEYEKlkEKLIKLKGEIKSLKKELEK 550
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
947-1118 2.72e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  947 DRADPRVQelKDRLEQELQQQGEEQYRSVLKRKEQHVTEQIAKMMELAREKQA--AELKTFKETSETDTKEMKKKLEAKR 1024
Cdd:COG4372     2 DRLGEKVG--KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREelEQAREELEQLEEELEQARSELEQLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1025 LERIQAMTKVTTDKVAQERLKREINNshIQEVVQAVKQMTETLERHQEKLEERQTACLEQIQAMEKQF--QEKALAEYEA 1102
Cdd:COG4372    80 EELEELNEQLQAAQAELAQAQEELES--LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIaeREEELKELEE 157

                         170
                  ....*....|....*.
gi 595763333 1103 KMKGLEAEVKESVRAY 1118
Cdd:COG4372   158 QLESLQEELAALEQEL 173
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
853-1113 2.92e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  853 EEATKEVTEPQTASLEE-LRELKGVVKLQRRHEKELRELERRgARRWEELlqrgAAQLAELQTQAAgcKLRPGKGSRKKR 931
Cdd:PRK03918  188 TENIEELIKEKEKELEEvLREINEISSELPELREELEKLEKE-VKELEEL----KEEIEELEKELE--SLEGSKRKLEEK 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  932 TLPCEETVVAPSEPHDRADPRVQELKDRLEQELQQQGEEQYRSVLKRKEQHVTEQIAKMMELAR--EKQAAELktfkETS 1009
Cdd:PRK03918  261 IRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINgiEERIKEL----EEK 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1010 ETDTKEMKKKLEA--KRLERI----QAMTKVTTDKVAQERLKREINNSHIQEVvqavKQMTETLERHQEKLEERQTACLE 1083
Cdd:PRK03918  337 EERLEELKKKLKEleKRLEELeerhELYEEAKAKKEELERLKKRLTGLTPEKL----EKELEELEKAKEEIEEEISKITA 412

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 595763333 1084 QIQAMEKQFQEKA----------------------------LAEYEAKMKGLEAEVKE 1113
Cdd:PRK03918  413 RIGELKKEIKELKkaieelkkakgkcpvcgrelteehrkelLEEYTAELKRIEKELKE 470
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 868-1113 3.63e-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: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   868 EELRELKGVVKLQR--RHEKELRELERRgARRWEELLQRGAAQLAELQTQAAGCKLRPGKGSRKKRTLpcEETVVAPSEP 945
Cdd:TIGR02168  220 AELRELELALLVLRleELREELEELQEE-LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL--QKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   946 HDRADPRVQELKDRLEQELQQQGEEQYRSV-LKRKEQH------------------VTEQIAKMMELAREKQAAE----- 1001
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEeLESKLDElaeelaeleekleelkeeLESLEAELEELEAELEELEsrlee 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  1002 LKTFKETSETDTKEMKKKLEAKRLERIQAMTKVTTDKVAQERLKREINNSHIQEVVQAVKQMTETLERHQEKLEERQtAC 1081
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ-EE 455

                          250       260       270
                   ....*....|....*....|....*....|..
gi 595763333  1082 LEQIQAMEKQfQEKALAEYEAKMKGLEAEVKE 1113
Cdd:TIGR02168  456 LERLEEALEE-LREELEEAEQALDAAERELAQ 486
PTZ00121 PTZ00121
MAEBL; Provisional
 849-1157 4.32e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  849 KATGEEATKEVTEPQTASleelrELKGVVKLQRRHEKELRELERrgARRWEELLQRgaaqlAELQTQAAGCKLRPGKGSR 928
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKAD-----EAKKKAEEAKKAEEAKKKAEE--AKKADEAKKK-----AEEAKKADEAKKKAEEAKK 1497

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  929 KkrtlpCEETVVAPSEPHDRADPRVQELKDRLEQELQQQGEEQYRSVLKRKEQHVTEQIAKMMEL--AREKQAAELKTFK 1006
Cdd:PTZ00121 1498 K-----ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKA 1572

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1007 ETSETDTK---EMKKKLEAKRLERIQAMTKVTTDKVAQERLKREINNSHIQEVVQA--VKQMTETLERHQEklEERQTAc 1081
Cdd:PTZ00121 1573 EEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeeEKKKVEQLKKKEA--EEKKKA- 1649

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1082 lEQIQAMEKQFQ----EKALAEYEAKMKGLEAEVKEsvrayfkdcfptEAEDKPERSCEASEESCPQEPLVSKADTQESR 1157
Cdd:PTZ00121 1650 -EELKKAEEENKikaaEEAKKAEEDKKKAEEAKKAE------------EDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
PRK12704 PRK12704
phosphodiesterase; Provisional
 987-1113 5.02e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 5.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  987 IAKMMELAREKQAAEL-KTFKETSETDTKEMKKK--LEAKrlERIQAMtKVTTDKVAQERlkreinNSHIQEVVQAVKQM 1063
Cdd:PRK12704   24 VRKKIAEAKIKEAEEEaKRILEEAKKEAEAIKKEalLEAK--EEIHKL-RNEFEKELRER------RNELQKLEKRLLQK 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 595763333 1064 TETLERHQEKLEERQTACLEQIQAMEKQFQEkaLAEYEAKMKGLEAEVKE 1113
Cdd:PRK12704   95 EENLDRKLELLEKREEELEKKEKELEQKQQE--LEKKEEELEELIEEQLQ 142
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 993-1113 5.97e-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: 44.28  E-value: 5.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   993 LAREKQAAELKTFKETSETDTKEMKKKLEAKRLERIQAMTKVTTDKVAQERLKREINNShiQEVVQAVKQMTETLERHQE 1072
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL--RKDLARLEAEVEQLEERIA 750

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 595763333  1073 KLEERQTACLEQIQAMEKQFQE--KALAEYEAKMKGLEAEVKE 1113
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEaeEELAEAEAEIEELEAQIEQ 793
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 294-437 1.05e-03

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


Pssm-ID: 176500 [Multi-domain]  Cd Length: 271  Bit Score: 42.46  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  294 PLNHYFINSSHNTY-LTAGQFSGLSSA-----EMY-RQVLLSGCRCVELDCWKgKPPDEEPIITHGFTMTTDILFKEAIE 366
Cdd:cd08557     8 PLSQLSIPGTHNSYaYTIDGNSPIVSKwsktqDLSiTDQLDAGVRYLDLRVAY-DPDDGDLYVCHGLFLLNGQTLEDVLN 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 595763333  367 AIAesAF-KTSPY-PVILSFENHVDSPRQQAKMAEycRSMFGETLLTDPLENFPLKPGIP-LpspEDLR-GKILI 437
Cdd:cd08557    87 EVK--DFlDAHPSeVVILDLEHEYGGDNGEDHDEL--DALLRDVLGDPLYRPPVRAGGWPtL---GELRaGKRVL 154
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 977-1105 1.05e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 43.07  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   977 KRKEQHVTEQIAKMMELAREKQAAELKTFKETSETDTKEMKKKlEAKRLERIQAMTKVTTDKVAQERLKREINNSHIQev 1056
Cdd:pfam05262  213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQ-EAKNLPKPADTSSPKEDKQVAENQKREIEKAQIE-- 289

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 595763333  1057 vqaVKQMTETLERHQE------KLEERQTACLEQIQAMEKQFQEKALAEYEAKMK 1105
Cdd:pfam05262  290 ---IKKNDEEALKAKDhkafdlKQESKASEKEAEDKELEAQKKREPVAEDLQKTK 341
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 985-1113 1.21e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 43.13  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   985 EQIAKMMELAREKQAAELKTFKETSETDTKEM-----KKKLEAKRLEriqAMTKVTTDKVAQErlkreinnshIQEVVQA 1059
Cdd:pfam13166  304 AQLPAVSDLASLLSAFELDVEDIESEAEVLNSqldglRRALEAKRKD---PFKSIELDSVDAK----------IESINDL 370

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 595763333  1060 VKQMTETLERHQE---KLEERQTACLEQIQAMEKQFQEKALAEYEAKMKGLEAEVKE 1113
Cdd:pfam13166  371 VASINELIAKHNEitdNFEEEKNKAKKKLRLHLVEEFKSEIDEYKDKYAGLEKAINS 427
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 877-1089 1.30e-03

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 41.29  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   877 VKLQRRHEKELRELERRgaRRweELLQRGAAQLAELQTQaagCKLRPGKGSRKKRTLPCEETVVAPSEPHDRadpRVQEL 956
Cdd:pfam14988   21 EKLWNQYVQECEEIERR--RQ--ELASRYTQQTAELQTQ---LLQKEKEQASLKKELQALRPFAKLKESQER---EIQDL 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   957 KDRLEQElqqqgeeqyRSVLKRKEQHVTEQIAKmmELAR-EKQAAELKtFKETSETDTKEMKKKLEAKRLERIQAMTKVT 1035
Cdd:pfam14988   91 EEEKEKV---------RAETAEKDREAHLQFLK--EKALlEKQLQELR-ILELGERATRELKRKAQALKLAAKQALSEFC 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 595763333  1036 tdkvaqERLKREinNSHIQEVVQAVKQMTETLERHQEKLEERQTACLEQIQAME 1089
Cdd:pfam14988  159 ------RSIKRE--NRQLQKELLQLIQETQALEAIKSKLENRKQRLKEEQWYLE 204
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 861-1094 1.54e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   861 EPQTASLEELRELKGVVKLQRR-HEKELRELERRGARRWEELlqrgaaQLAELQTQAAGCKLRPGKGSRKKRTLPCEEtv 939
Cdd:pfam17380  410 ERQRKIQQQKVEMEQIRAEQEEaRQREVRRLEEERAREMERV------RLEEQERQQQVERLRQQEEERKRKKLELEK-- 481

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   940 vapsEPHDRAdpRVQELKdrleqelqqqgeeqyRSVLkrkEQHVTEQIAKMMELAREKQAAElktfketsetdtKEMKkk 1019
Cdd:pfam17380  482 ----EKRDRK--RAEEQR---------------RKIL---EKELEERKQAMIEEERKRKLLE------------KEME-- 523

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 595763333  1020 leakrlERIQAMTKVTTDKVAQERLKREINNSHIQEVVQAVKQMTEtlERHQEKLEERQTACLEQIQAMEKQFQE 1094
Cdd:pfam17380  524 ------ERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE--ERSRLEAMEREREMMRQIVESEKARAE 590
PTZ00121 PTZ00121
MAEBL; Provisional
 849-1141 1.92e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  849 KATGEEATKEVTEPQTASLEELRELKGVVKLQRRHEK----ELRELERrgARRWEELLQRGAAQLAELQTQAAGCKLRPG 924
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkadELKKAEE--LKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  925 KGSRKKRTLPCEETVVAPSEPHDRADPRVQELKDRLEQELQQQGEEQYRSVLKRKEQhvtEQIAKMMELAREKQAAELKT 1004
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA---EEKKKAEELKKAEEENKIKA 1663

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1005 FKETSETDtKEMKKKLEAKRLERIQAMTKVTTDKVAQERLKREINNSHIQEVVQAVKQMTETLERHQEKLEERQTACLEQ 1084
Cdd:PTZ00121 1664 AEEAKKAE-EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED 1742

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 595763333 1085 IQAMEKQFQEKALAEYEAKMKGLEAEVKESVRAYFKDCFPTEAEDKPERSCEASEES 1141
Cdd:PTZ00121 1743 KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 974-1113 3.50e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  974 SVLKRKEQHVTEQIAKMmelarEKQAAELKTFKETSETDTKEMKKKLeAKRLERIQAMTKVTTDKV--AQERLKREINNS 1051
Cdd:COG4942    65 AALARRIRALEQELAAL-----EAELAELEKEIAELRAELEAQKEEL-AELLRALYRLGRQPPLALllSPEDFLDAVRRL 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 595763333 1052 H-IQEVVQAVKQMTETLERHQEKLEErqtacLEQIQAMEKQFQEKALAEYEAKMKGLEAEVKE 1113
Cdd:COG4942   139 QyLKYLAPARREQAEELRADLAELAA-----LRAELEAERAELEALLAELEEERAALEALKAE 196
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
 693-757 3.53e-03

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


Pssm-ID: 176064 [Multi-domain]  Cd Length: 126  Bit Score: 38.59  E-value: 3.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 595763333  693 KRRYRTklSPTANSINPVWKEE-PFIFEKILM--PELASLRIAVMEEGS----KFLGHRIIPINALHSGYHH 757
Cdd:cd08682    30 KEKYST--SVKEKTTSPVWKEEcSFELPGLLSgnGNRATLQLTVMHRNLlgldKFLGQVSIPLNDLDEDKGR 99
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
976-1115 3.58e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  976 LKRKEQHVTEQIAKMM-ELAREKQaaELKTFKETSETDTKEMKKKLEA-----KRLERIQAMTKVTTDKVAQ---ERLKR 1046
Cdd:COG4372    50 LREELEQAREELEQLEeELEQARS--ELEQLEEELEELNEQLQAAQAElaqaqEELESLQEEAEELQEELEElqkERQDL 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 595763333 1047 EINNSHIQEVVQAVKQMTETLERHQEKLEERQTACLEQIQAMEKQFQEKALAEYEAKMKGLEAEVKESV 1115
Cdd:COG4372   128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNA 196
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 976-1114 3.94e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.50  E-value: 3.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   976 LKRKEQHVTEQIAKMMELAREKQAAELKTFKETSETDTKEMKKKLEAKRLERIQAMTKVTTDKVA-------QERLKREI 1048
Cdd:pfam02463  228 YLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAkeeeelkSELLKLER 307

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 595763333  1049 NNSHIQEVVQAVKQMTETLERHQEKLEERQTACLEQIQAMEKQFQEKALAEYEAKMKGLEAEVKES 1114
Cdd:pfam02463  308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE 373
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 946-1121 4.13e-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: 39.55  E-value: 4.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   946 HDRADPRVQELKDRLEQELQQQgeeqyRSVLKRKEQHVTEQIAKMMELAREKQAAELKTFKETSETDTKEMKKKLeAKRL 1025
Cdd:pfam01442   17 QEQLGPVAQELVDRLEKETEAL-----RERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKRL-NADA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  1026 ERIQAMTKVTTDKvAQERLKREInnSHIQEvvqavkQMTETLERHQEKLEERqtacleqIQAMEKQFQEKAlAEYEAKMK 1105
Cdd:pfam01442   91 EELQEKLAPYGEE-LRERLEQNV--DALRA------RLAPYAEELRQKLAER-------LEELKESLAPYA-EEVQAQLS 153

                          170
                   ....*....|....*.
gi 595763333  1106 GLEAEVKESVRAYFKD 1121
Cdd:pfam01442  154 QRLQELREKLEPQAED 169
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 995-1108 4.29e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 4.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  995 REKQAAE---LKTFKETSETDTKEMKKKLEAKRLERIQAMTKVttDKVAQERLKREINNSHIQEVVQAVKQMTETLERHQ 1071
Cdd:cd16269   177 QSKEAEAeaiLQADQALTEKEKEIEAERAKAEAAEQERKLLEE--QQRELEQKLEDQERSYEEHLRQLKEKMEEERENLL 254

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 595763333 1072 EKLEERQTACL-EQIQAMEKQFQEKAlAEYEAKMKGLE 1108
Cdd:cd16269   255 KEQERALESKLkEQEALLEEGFKEQA-ELLQEEIRSLK 291
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 973-1105 4.73e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.19  E-value: 4.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   973 RSVLKRKEQHVTEQIAKMMELAREKQAAELKTFKETSETDTKEMKKK--LEAKRLEriQAMTKVTTDKVaqeRLKREI-N 1049
Cdd:TIGR01612 1513 KELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKfiLEAEKSE--QKIKEIKKEKF---RIEDDAaK 1587

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 595763333  1050 NSHIQEVVQAVKQMTETLERHQEKLEERQTA---CLEQIQAMEKQFQEKALAEYEAKMK 1105
Cdd:TIGR01612 1588 NDKSNKAAIDIQLSLENFENKFLKISDIKKKindCLKETESIEKKISSFSIDSQDTELK 1646
CR6_interact pfam10147
Growth arrest and DNA-damage-inducible proteins-interacting protein 1; Members of this family ...
 977-1103 5.13e-03

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


Pssm-ID: 431088 [Multi-domain]  Cd Length: 204  Bit Score: 39.45  E-value: 5.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   977 KRKEQHvtEQIAKMMELAREKQAAELKTFKETSETDTKEMKK------KLEAKRLERIQamtKVTTDKVAQERLKREINN 1050
Cdd:pfam10147   81 EEREWY--PSLAQMLESNRAQKAEKEARRQAREQEIAKKMAKmpqwiaDWNAQKAKREA---EAQAAKERKERLVAEARE 155

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 595763333  1051 S---HIQEVVQAVKQMTETLERHQEKleerqtaclEQIQAMEKQFQEKALAEYEAK 1103
Cdd:pfam10147  156 HfgfKVDPRDERFKEMLQQKEKEDKK---------KVKEAKRKEKEEKRMAKLVEA 202
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 865-1101 5.21e-03

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: 39.91  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  865 ASLEELRELkgvVKLQRRhEKELRELERRgarrweelLQRGAAQLAELQTQAAGCKLRpgkgsrkkrtlpceetvvapse 944
Cdd:COG1579     1 AMPEDLRAL---LDLQEL-DSELDRLEHR--------LKELPAELAELEDELAALEAR---------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  945 pHDRADPRVQELKDRleqelqqqgeeqyrsvLKRKE---QHVTEQIAKMmelarEKQAAELKTFKE----TSETDT-KEM 1016
Cdd:COG1579    47 -LEAAKTELEDLEKE----------------IKRLEleiEEVEARIKKY-----EEQLGNVRNNKEyealQKEIESlKRR 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1017 KKKLEAKRLEriqAMTKVTTDKVAQERLKREInnshiQEVVQAVKQMTETLERHQEKLEERQTACLEQIQAMEKQFQEKA 1096
Cdd:COG1579   105 ISDLEDEILE---LMERIEELEEELAELEAEL-----AELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEL 176


                  ....*
gi 595763333 1097 LAEYE 1101
Cdd:COG1579   177 LALYE 181
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
878-1110 6.18e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 6.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  878 KLQRRhEKELRELERRgARRWEELLQRGAAQLAELQTQAAGCKLRPGKGSRKKRTLPCEETVVAPSEPHDR---ADPRVQ 954
Cdd:COG4913   611 KLAAL-EAELAELEEE-LAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERldaSSDDLA 688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  955 ELKDRleqelqqqgeeqyRSVLKRKEQHVTEQIAkmmelAREKQAAELktfkETSETDTKEMKKKLEAkRLERIQAMTKV 1034
Cdd:COG4913   689 ALEEQ-------------LEELEAELEELEEELD-----ELKGEIGRL----EKELEQAEEELDELQD-RLEAAEDLARL 745

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333 1035 TTDKVAQERLKREINNSHIQEVVQAVKQMTETLERHQEKLEERQTACLEQI---------------------QAMEKQFQ 1093
Cdd:COG4913   746 ELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFnrewpaetadldadleslpeyLALLDRLE 825

                         250
                  ....*....|....*..
gi 595763333 1094 EKALAEYEAKMKGLEAE 1110
Cdd:COG4913   826 EDGLPEYEERFKELLNE 842
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 662-736 6.54e-03

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


Pssm-ID: 176001 [Multi-domain]  Cd Length: 119  Bit Score: 37.63  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  662 LSITIISGQFLSERSVRT----YVEVELfglPGDPKRRYRTKLSPtaNSINPVWKEEpfiFEKILMPELAS-LRIAVMEE 736
Cdd:cd04036     2 LTVRVLRATNITKGDLLStpdcYVELWL---PTASDEKKRTKTIK--NSINPVWNET---FEFRIQSQVKNvLELTVMDE 73
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
 179-272 6.55e-03

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


Pssm-ID: 320037 [Multi-domain]  Cd Length: 142  Bit Score: 38.38  E-value: 6.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  179 DFPEsvYKSFLMSLCPRPEIDEIFTSYHSKAKPYMTKEHLTKFINQKQRDPRlnsllfppaRPEQVQVLIDKYEPSGINV 258
Cdd:cd16207    56 NFEE--FQEFVKLLKRRKDIKAIFKQLTKPGSDGLTLEEFLKFLRDVQKEDV---------DRETWEKIFEKFARRIDDS 124

                          90
                  ....*....|....
gi 595763333  259 QRGQLSPEGMVWFL 272
Cdd:cd16207   125 DSLTMTLEGFTSFL 138
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
879-1110 8.42e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 8.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  879 LQRRHEKELRELERRGARRWEELLQrgaaQLAELQTQAAGCKLRPGKGSRKKRTLpceetvvapsephDRADPRVQELKD 958
Cdd:COG4717    47 LLERLEKEADELFKPQGRKPELNLK----ELKELEEELKEAEEKEEEYAELQEEL-------------EELEEELEELEA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  959 RleqelqqqgeeqyRSVLKRKEQHVTEQIAKMMELAREKQA-AELKTFKETSEtdtkemkkKLEAKRLERIQAMTKVTTD 1037
Cdd:COG4717   110 E-------------LEELREELEKLEKLLQLLPLYQELEALeAELAELPERLE--------ELEERLEELRELEEELEEL 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 595763333 1038 KVAQERLKREINNSHIQ---EVVQAVKQMTETLERHQEKLEERQTAcLEQIQAmEKQFQEKALAEYEAKMKGLEAE 1110
Cdd:COG4717   169 EAELAELQEELEELLEQlslATEEELQDLAEELEELQQRLAELEEE-LEEAQE-ELEELEEELEQLENELEAAALE 242
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 868-1102 8.72e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 8.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   868 EELRELKGVV-----KLQRRH-EKELRELERRGA----RRWEELLQRGAAQLAELQTQAAGCKLRPGKGSRKKRTLpcEE 937
Cdd:TIGR02169  805 EEVSRIEARLreieqKLNRLTlEKEYLEKEIQELqeqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL--ES 882

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333   938 TVVAPSEPHDRADPRVQELKDRLEQELQQQGEEQYR-SVLKRKEQHVTEQIAkmmELAREKQAAELKTFKETSETDTKEM 1016
Cdd:TIGR02169  883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRlSELKAKLEALEEELS---EIEDPKGEDEEIPEEELSLEDVQAE 959

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763333  1017 KKKLEakrlERIQAMtkvttdkvaqerlkREINNSHIQEVVQAVKQMTEtLERHQEKLEERQTACLEQIQAMEKQFQEKA 1096
Cdd:TIGR02169  960 LQRVE----EEIRAL--------------EPVNMLAIQEYEEVLKRLDE-LKEKRAKLEEERKAILERIEEYEKKKREVF 1020


                   ....*.
gi 595763333  1097 LAEYEA 1102
Cdd:TIGR02169 1021 MEAFEA 1026
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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