NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034590989|ref|XP_016877803|]
View 

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 311-662 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: 551.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08624      1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08624     81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtaYEEMSSLV 550
Cdd:cd08624    155 ------------------------------------------------------------------------YEEMSSLV 162

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  551 NYIQPTKFVSFEFSAprlftcifsghkhKKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMP 630
Cdd:cd08624    163 NYIQPTKFVSFEFSA-------------QKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMP 229

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034590989  631 QMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08624    230 QMFWNVGCQMVALNFQTMDLPMQQNMALFEFN 261
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 149-299 5.17e-102

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


:

Pssm-ID: 320039  Cd Length: 151  Bit Score: 319.13  E-value: 5.17e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  149 DKILVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSY 228
Cdd:cd16209      1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034590989  229 HAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16209     81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 991-1173 6.47e-89

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: 284.26  E-value: 6.47e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  991 GRVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLERIQG 1070
Cdd:pfam08703    1 KQVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1071 MTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEkqgsllsPQFQKEALAEYEAR 1150
Cdd:pfam08703   81 AKKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEE-------PQLQAELNAEYEEK 153

                          170       180
                   ....*....|....*....|...
gi 1034590989 1151 MKGLEAEVKESVRACLRTCFPSE 1173
Cdd:pfam08703  154 LKGLPAEVRESVKSCLKEGFPDE 176
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-141 6.11e-69

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


:

Pssm-ID: 465506  Cd Length: 131  Bit Score: 226.88  E-value: 6.11e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989   12 KVKAYLSQGERFIKWDDETTVASP-VILRVDPKGYYLYWTYQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVFNMDFP 90
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034590989   91 DNSFLLKTLTVVSGPDMVDLTFHNFVSYKENVGKAWAEDVLALVKHPLTAN 141
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 694-815 9.13e-38

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


:

Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 137.67  E-value: 9.13e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  694 ATTLSITVISGQFLS------ERSVRTYVEVELFGLPGDPKRRYRTKLSPStNSINPVWkEEPFVFEKIlMPELASLRVA 767
Cdd:cd00275      1 PLTLTIKIISGQQLPkpkgdkGSIVDPYVEVEIHGLPADDSAKFKTKVVKN-NGFNPVW-NETFEFDVT-VPELAFLRFV 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034590989  768 VMEE---GNKFLGHRIIPINALNSGYHHLCLHSESNMPLTMPALFIFLEMK 815
Cdd:cd00275     78 VYDEdsgDDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
892-1087 1.48e-03

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  892 KEAAEPRTASLEELRELKGVVKLQRRHEKELRELERRgARRWEELLQRGAAQLAELGPPGVGGVGACKLGP--GKGSRKK 969
Cdd:COG4717     60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALE 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  970 RSLpreesagaapgegpEGVDGRVRELKDRLE-----LELLRQGEEQYEcVLKRKEQHVAEQISKMMELAREKQAAELKA 1044
Cdd:COG4717    139 AEL--------------AELPERLEELEERLEelrelEEELEELEAELA-ELQEELEELLEQLSLATEEELQDLAEELEE 203

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034590989 1045 L---KETSENDTKEMKKKLETKRlERIQGMTKVTTDKMAQERLKRE 1087
Cdd:COG4717    204 LqqrLAELEEELEEAQEELEELE-EELEQLENELEAAALEERLKEA 248
 
Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 311-662 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: 551.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08624      1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08624     81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtaYEEMSSLV 550
Cdd:cd08624    155 ------------------------------------------------------------------------YEEMSSLV 162

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  551 NYIQPTKFVSFEFSAprlftcifsghkhKKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMP 630
Cdd:cd08624    163 NYIQPTKFVSFEFSA-------------QKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMP 229

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034590989  631 QMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08624    230 QMFWNVGCQMVALNFQTMDLPMQQNMALFEFN 261
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 149-299 5.17e-102

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


Pssm-ID: 320039  Cd Length: 151  Bit Score: 319.13  E-value: 5.17e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  149 DKILVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSY 228
Cdd:cd16209      1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034590989  229 HAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16209     81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 991-1173 6.47e-89

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: 284.26  E-value: 6.47e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  991 GRVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLERIQG 1070
Cdd:pfam08703    1 KQVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1071 MTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEkqgsllsPQFQKEALAEYEAR 1150
Cdd:pfam08703   81 AKKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEE-------PQLQAELNAEYEEK 153

                          170       180
                   ....*....|....*....|...
gi 1034590989 1151 MKGLEAEVKESVRACLRTCFPSE 1173
Cdd:pfam08703  154 LKGLPAEVRESVKSCLKEGFPDE 176
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 314-462 2.08e-79

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


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 256.66  E-value: 2.08e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  314 MTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIAE 393
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034590989  394 SAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKN 462
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLD----DDLTELPSPEDLKGKILIKG 142
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-141 6.11e-69

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


Pssm-ID: 465506  Cd Length: 131  Bit Score: 226.88  E-value: 6.11e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989   12 KVKAYLSQGERFIKWDDETTVASP-VILRVDPKGYYLYWTYQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVFNMDFP 90
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034590989   91 DNSFLLKTLTVVSGPDMVDLTFHNFVSYKENVGKAWAEDVLALVKHPLTAN 141
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 314-463 1.61e-64

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


Pssm-ID: 197543 [Multi-domain]  Cd Length: 143  Bit Score: 214.84  E-value: 1.61e-64
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989   314 MTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIAE 393
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDG--PDGEPVIYHGHTFTLPIKLSEVLEAIKD 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989   394 SAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKpgvpLPSPEDLRGKILIKNK 463
Cdd:smart00148   79 FAFVTSPYPVILSLENHC-SPDQQAKMAQMFKEIFGDMLYTPPLTSSLEV----LPSPEQLRGKILLKVR 143
PLN02228 PLN02228
Phosphoinositide phospholipase C
 217-799 5.56e-57

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 207.97  E-value: 5.56e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  217 PRPEIDEIFTSYHAKAKpyMTKEHLTKFINQKQRDSRlnsllfppARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLC 296
Cdd:PLN02228    22 PPVSIKRLFEAYSRNGK--MSFDELLRFVSEVQGERH--------AGLDYVQDIFHSVKHHNVFHHHGLVHLNAFYRYLF 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  297 GPENSVLAQDKLLlHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKgKPPDEEPIITHGF 376
Cdd:PLN02228    92 SDTNSPLPMSGQV-HHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWP-NPSGNAAEVRHGR 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  377 TMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLL---TEPLEKFplkpgvplPSPED 453
Cdd:PLN02228   170 TLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHL-PPNLQAQVAKMLTKTFRGMLFrctSESTKHF--------PSPEE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  454 LRGKILIKNKKNQFSGPTSSSKDTggeaegssppSAPAGEGTVWAGEEGTeleeeeveeeeeeesgnldEEEIKKMQSDE 533
Cdd:PLN02228   241 LKNKILISTKPPKEYLESKTVQTT----------RTPTVKETSWKRVADA-------------------ENKILEEYKDE 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  534 GTAGLEvtaYEEMSSL--VNYIQPTKfvsfefsaprlfTCIfSGHKHKKNRsyviSSFTELKAYDLLSKASVQFVDYNKR 611
Cdd:PLN02228   292 ESEAVG---YRDLIAIhaANCKDPLK------------DCL-SDDPEKPIR----VSMDEQWLETMVRTRGTDLVRFTQR 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  612 QMSRIYPKGTRMDSSNYMPQMFWNAGCQMVALNFQT--MDLPMQQNMavFEFNGQSGYLLKHEFMRRPDKQFNPFSvdri 689
Cdd:PLN02228   352 NLVRIYPKGTRVDSSNYDPHVGWTHGAQMVAFNMQGhgKQLWIMQGM--FRANGGCGYVKKPRILLDEHTLFDPCK---- 425

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  690 DVVVATTLSITVISGQ----------FLSERSVRTYVEVELFGLPGDPKrRYRTKLspSTNSINPVWKEEPFVFEkILMP 759
Cdd:PLN02228   426 RLPIKTTLKVKIYTGEgwdldfhlthFDQYSPPDFFVKIGIAGVPRDTV-SYRTET--AVDQWFPIWGNDEFLFQ-LRVP 501

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 1034590989  760 ELASLRVAVME----EGNKFLGHRIIPINALNSGYHHLCLHSES 799
Cdd:PLN02228   502 ELALLWFKVQDydndTQNDFAGQTCLPLPELKSGVRAVRLHDRA 545
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-144 1.30e-55

Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is regulated by heterotrimeric G protein-coupled receptors through their C2 domain and long C-terminal extension which forms an autoinhibitory helix. There are four isoforms: PLC-beta1-4. The PH domain of PLC-beta2 and PLC-beta3 plays a dual role, much like PLC-delta1, by binding to the plasma membrane, as well as the interaction site for the catalytic activator. However, PLC-beta binds to the lipid surface independent of PIP2. PLC-beta1 seems to play unspecified roles in cellular proliferation and differentiation. PLC-beta consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves, a C2 domain and a C-terminal PDZ. Members of the Rho GTPase family (e.g., Rac1, Rac2, Rac3, and cdc42) have been implicated in their activation by binding to an alternate site on the N-terminal PH domain. A basic amino acid region within the enzyme's long C-terminal tail appears to function as a Nuclear Localization Signal for import into the nucleus. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.the plasma membrane, but only a few (less than 10%) display strong specificity in binding inositol phosphates. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinases, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, cytoskeletal associated molecules, and in lipid associated enzymes.


Pssm-ID: 270167  Cd Length: 127  Bit Score: 188.93  E-value: 1.30e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989   17 LSQGERFIKWDDETTVASPVILRVDPKGYYLYWTYQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVfNMDFPDNSFLL 96
Cdd:cd13361      1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1034590989   97 KTLTVVSGPDMVDLTFHNFVSYKENVGKAWAEDVLALVKHPLTANASR 144
Cdd:cd13361     80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 694-815 9.13e-38

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


Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 137.67  E-value: 9.13e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  694 ATTLSITVISGQFLS------ERSVRTYVEVELFGLPGDPKRRYRTKLSPStNSINPVWkEEPFVFEKIlMPELASLRVA 767
Cdd:cd00275      1 PLTLTIKIISGQQLPkpkgdkGSIVDPYVEVEIHGLPADDSAKFKTKVVKN-NGFNPVW-NETFEFDVT-VPELAFLRFV 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034590989  768 VMEE---GNKFLGHRIIPINALNSGYHHLCLHSESNMPLTMPALFIFLEMK 815
Cdd:cd00275     78 VYDEdsgDDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 696-792 7.20e-14

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 68.67  E-value: 7.20e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989   696 TLSITVISGQFLSER----SVRTYVEVELFGlpgDPKRRYRTKLSPSTNsiNPVWKEEpFVFEkILMPELASLRVAVMEE 771
Cdd:smart00239    1 TLTVKIISARNLPPKdkggKSDPYVKVSLDG---DPKEKKKTKVVKNTL--NPVWNET-FEFE-VPPPELAELEIEVYDK 73

                            90       100
                    ....*....|....*....|....*
gi 1034590989   772 ----GNKFLGHRIIPINALNSGYHH 792
Cdd:smart00239   74 drfgRDDFIGQVTIPLSDLLLGGRH 98
C2 pfam00168
C2 domain;
696-789 3.60e-10

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 58.10  E-value: 3.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  696 TLSITVISGQFL----SERSVRTYVEVELfglpGDPKRRYRTKLSPstNSINPVWKEEpFVFEkILMPELASLRVAVMEE 771
Cdd:pfam00168    2 RLTVTVIEAKNLppkdGNGTSDPYVKVYL----LDGKQKKKTKVVK--NTLNPVWNET-FTFS-VPDPENAVLEIEVYDY 73

                           90       100
                   ....*....|....*....|..
gi 1034590989  772 ----GNKFLGHRIIPINALNSG 789
Cdd:pfam00168   74 drfgRDDFIGEVRIPLSELDSG 95
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
892-1160 5.17e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.85  E-value: 5.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  892 KEAAEPRTASLEELRELKgvvKLQRRHEKELRELERRgARRWEELlqrgAAQLAELGPPgvggvgacklgpgKGSRKKRS 971
Cdd:PRK03918   196 KEKEKELEEVLREINEIS---SELPELREELEKLEKE-VKELEEL----KEEIEELEKE-------------LESLEGSK 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  972 LPREESAGAAPgEGPEGVDGRVRELKDRL-ELELLRQGEEQYECVLKRKEQHVAE--QISKMMELAREKQAAELKALKET 1048
Cdd:PRK03918   255 RKLEEKIRELE-ERIEELKKEIEELEEKVkELKELKEKAEEYIKLSEFYEEYLDElrEIEKRLSRLEEEINGIEERIKEL 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1049 S--ENDTKEMKKKLET--KRLERIQGMTKVTTD---KMAQ-ERLKREINNSHIQEvvqvIKQMTENLERHQEKLEEKQAA 1120
Cdd:PRK03918   334 EekEERLEELKKKLKEleKRLEELEERHELYEEakaKKEElERLKKRLTGLTPEK----LEKELEELEKAKEEIEEEISK 409

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034590989 1121 CLEQIREMEKQ---------------------GSLLSPQFQKEALAEYEARMKGLEAEVKE 1160
Cdd:PRK03918   410 ITARIGELKKEikelkkaieelkkakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKE 470
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 215-303 8.95e-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: 8.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  215 LCPRPEIDEIFTSYhAKAKPYMTKEHLTKFINQKQRDSRlnsllfppARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWF 294
Cdd:pfam09279    5 LTQREEIDEIFQEY-SGDGQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAMTKDGFLMY 75


                   ....*....
gi 1034590989  295 LCGPENSVL 303
Cdd:pfam09279   76 LCSPDGSIF 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 992-1164 8.08e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 8.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  992 RVRELKDRLE----------LELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEMKKKLE 1061
Cdd:COG1196    214 RYRELKEELKeleaellllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1062 TKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAAcLEQIREMEKQgsllspqfQK 1141
Cdd:COG1196    294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE-LEEAEAELAE--------AE 364

                          170       180
                   ....*....|....*....|...
gi 1034590989 1142 EALAEYEARMKGLEAEVKESVRA 1164
Cdd:COG1196    365 EALLEAEAELAEAEEELEELAEE 387
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 893-1205 1.14e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  893 EAAEPRTASLEElrELKGVVKLQRRHEKELRELERRgarrWEELLQRGAAQLAELGPPGVGGvgacklgpGKGSRKKRSL 972
Cdd:TIGR02168  687 EELEEKIAELEK--ALAELRKELEELEEELEQLRKE----LEELSRQISALRKDLARLEAEV--------EQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  973 PREESAGAAPGEGPEGVDGRVRELKDRLELELLRQgEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSEND 1052
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEEL-EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1053 TKEMKKKletkRLERIQGMTKVTTDKMA-----QERLKREINNSHIQ--EVVQVIKQMTENLERHQEKLEEKQaaclEQI 1125
Cdd:TIGR02168  832 RIAATER----RLEDLEEQIEELSEDIEslaaeIEELEELIEELESEleALLNERASLEEALALLRSELEELS----EEL 903

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1126 REMEKQGSLLSPQFQ--KEALAEYEARMKGLEAEVKEsvracLRTCFPSEAKDKPERACECPPELceqDPLIAKADAQES 1203
Cdd:TIGR02168  904 RELESKRSELRRELEelREKLAQLELRLEGLEVRIDN-----LQERLSEEYSLTLEEAEALENKI---EDDEEEARRRLK 975


                   ..
gi 1034590989 1204 RL 1205
Cdd:TIGR02168  976 RL 977
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
892-1087 1.48e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  892 KEAAEPRTASLEELRELKGVVKLQRRHEKELRELERRgARRWEELLQRGAAQLAELGPPGVGGVGACKLGP--GKGSRKK 969
Cdd:COG4717     60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALE 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  970 RSLpreesagaapgegpEGVDGRVRELKDRLE-----LELLRQGEEQYEcVLKRKEQHVAEQISKMMELAREKQAAELKA 1044
Cdd:COG4717    139 AEL--------------AELPERLEELEERLEelrelEEELEELEAELA-ELQEELEELLEQLSLATEEELQDLAEELEE 203

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034590989 1045 L---KETSENDTKEMKKKLETKRlERIQGMTKVTTDKMAQERLKRE 1087
Cdd:COG4717    204 LqqrLAELEEELEEAQEELEELE-EELEQLENELEAAALEERLKEA 248
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1007-1143 4.37e-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: 4.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1007 QGEEQYECVLKRKEqHVAEQIskmmelarekqaaeLKALKETSENDTKEMKKKLETKRLERIQGMTKVttDKMAQERLKR 1086
Cdd:cd16269    167 KAEEVLQEFLQSKE-AEAEAI--------------LQADQALTEKEKEIEAERAKAEAAEQERKLLEE--QQRELEQKLE 229

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034590989 1087 EINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQGsllspqFQKEA 1143
Cdd:cd16269    230 DQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALLEEG------FKEQA 280
 
Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 311-662 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: 551.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08624      1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08624     81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtaYEEMSSLV 550
Cdd:cd08624    155 ------------------------------------------------------------------------YEEMSSLV 162

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  551 NYIQPTKFVSFEFSAprlftcifsghkhKKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMP 630
Cdd:cd08624    163 NYIQPTKFVSFEFSA-------------QKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMP 229

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034590989  631 QMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08624    230 QMFWNVGCQMVALNFQTMDLPMQQNMALFEFN 261
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
 311-662 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: 536.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08591      1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVDSPrQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08591     81 IAETAFKTSEYPVILSFENHCSSK-QQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------ 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSLV 550
Cdd:cd08591    154 ---------------------------------------------------------------------------LSSLV 158

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  551 NYIQPTKFVSFEFSAprlftcifsghkhKKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMP 630
Cdd:cd08591    159 NYIQPVKFQGFEVAE-------------KRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQLSRIYPKGTRVDSSNYMP 225

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034590989  631 QMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08591    226 QIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN 257
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
 313-662 3.91e-145

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: 437.95  E-value: 3.91e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  313 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEAIA 392
Cdd:cd08625      3 DMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEAIA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  393 ESAFKTSPYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgpts 472
Cdd:cd08625     83 ESAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK-------- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  473 sskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSLVNY 552
Cdd:cd08625    155 -------------------------------------------------------------------------MSTLVNY 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  553 IQPTKFVSFEFSAprlftcifsghkhKKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQM 632
Cdd:cd08625    162 IEPVKFKSFEAAA-------------KRNKFFEMSSFVETKAMEQLTKSPMEFVEYNKKQLSRIYPKGTRVDSSNYMPQL 228

                          330       340       350
                   ....*....|....*....|....*....|
gi 1034590989  633 FWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08625    229 FWNVGCQMVALNFQTLDLAMQLNMGVFEYN 258
PI-PLCc_eukaryota cd08558
Catalytic domain of eukaryotic phosphoinositide-specific phospholipase C and similar proteins; ...
 311-662 1.19e-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: 406.07  E-value: 1.19e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08558      1 YQDMTQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGHTLTSKILFKDVIEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEKFPlkpgVPLPSPEDLRGKILIKNKKNQfsgp 470
Cdd:cd08558     79 IKEYAFVTSPYPVILSLENHC-SLEQQKKMAQILKEIFGDKLLTPPLDENP----VQLPSPEQLKGKILIKGKKYH---- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeemsslv 550
Cdd:cd08558        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  551 nyiqptkfvsfefsaprlftcifsghkhkknrsyvISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMP 630
Cdd:cd08558    150 -----------------------------------MSSFSETKALKLLKESPEEFVKYNKRQLSRVYPKGTRVDSSNYNP 194

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034590989  631 QMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08558    195 QPFWNAGCQMVALNYQTPDLPMQLNQGKFEQN 226
PI-PLCc_beta1 cd08623
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1; This subfamily ...
 313-662 8.36e-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: 394.84  E-value: 8.36e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  313 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEAIA 392
Cdd:cd08623      3 DMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  393 ESAFKTSPYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgpts 472
Cdd:cd08623     83 ECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKK-------- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  473 sskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSLVNY 552
Cdd:cd08623    155 -------------------------------------------------------------------------MSNLVNY 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  553 IQPTKFVSFEFSaprlftcifsghkHKKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQM 632
Cdd:cd08623    162 IQPVKFESFEAS-------------KKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQL 228

                          330       340       350
                   ....*....|....*....|....*....|
gi 1034590989  633 FWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08623    229 FWNAGCQMVALNFQTVDLSMQINMGMYEYN 258
PI-PLCc_beta4 cd08626
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4; This subfamily ...
 311-662 3.14e-127

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: 390.66  E-value: 3.14e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08626      1 YQDMDQPLAHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCIELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVDSPrQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08626     81 IKDTAFVTSDYPVILSFENHCSKP-QQYKLAKYCEEIFGDLLLTKPLESHPLEPGVPLPSPNKLKRKILIKNKR------ 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeeMSSLV 550
Cdd:cd08626    154 ---------------------------------------------------------------------------LSSLV 158

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  551 NYIQPTKFVSFEFSaprlftcifsghkHKKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMP 630
Cdd:cd08626    159 NYAQPVKFQGFDVA-------------EERNIHFNMSSFNESVGLGYLKTSAIEFVNYNKRQMSRIYPKGTRVDSSNYMP 225

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034590989  631 QMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08626    226 QIFWNAGCQMVSLNFQTPDLGMQLNQGKFEYN 257
PI-PLCc_delta cd08593
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta; This subfamily ...
 311-662 3.61e-109

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: 342.40  E-value: 3.61e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08593      1 YQDMTQPLSHYFIASSHNTYLLEDQLKGPSSTEAYIRALKKGCRCVELDCWDG--PDGEPIIYHGHTLTSKILFKDVIQA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKNKKNQFSgp 470
Cdd:cd08593     79 IREYAFKVSPYPVILSLENHC-SVEQQKVMAQHLKSILGDKLLTQPLD----GVLTALPSPEELKGKILVKGKKLKLA-- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSLV 550
Cdd:cd08593    152 -------------------------------------------------------------------------KELSDLV 158

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  551 NYIQPTKFVSFEfsaprlftcifsgHKHKKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMP 630
Cdd:cd08593    159 IYCKSVHFKSFE-------------HSKENYHFYEMSSFSESKALKLAQESGNEFVRHNKRQLSRIYPAGLRTDSSNYDP 225

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034590989  631 QMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08593    226 QEMWNVGCQIVALNFQTPGEEMDLNDGLFRQN 257
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 311-662 9.16e-107

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: 336.93  E-value: 9.16e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFS-----GLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTtDIFFK 385
Cdd:cd00137      1 HHPDTQPLAHYSIPGTHDTYLTAGQFTikqvwGLTQTEMYRQQLLSGCRCVDIRCWDG--KPEEPIIYHGPTFL-DIFLK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  386 EAIEAIAESAFKTSPYPIILSFENHVDS-PRQQAKMAEYCRTIFGDMLLTeplekFPLKPGVPLPSPEDLRGKILIKNKK 464
Cdd:cd00137     78 EVIEAIAQFLKKNPPETIIMSLKNEVDSmDSFQAKMAEYCRTIFGDMLLT-----PPLKPTVPLPSLEDLRGKILLLNKK 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  465 NQFSGPTSSSKDTGgeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtaye 544
Cdd:cd00137    153 NGFSGPTGSSNDTG------------------------------------------------------------------ 166

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  545 emsslvnyiqptkFVSFEFSAprlftcifsghkhKKNRSYVISSFTELKAYD----LLSKASVQFVDYNKRQMSRIYPKG 620
Cdd:cd00137    167 -------------FVSFEFST-------------QKNRSYNISSQDEYKAYDdekvKLIKATVQFVDYNKNQLSRNYPSG 220

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034590989  621 TR---------MDSSNYMPQMFWN---AGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd00137    221 TSggtawyyyaMDSNNYMPQMFWNanpAGCGIVILDFQTMDLPMQQYMAVIEFN 274
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 149-299 5.17e-102

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


Pssm-ID: 320039  Cd Length: 151  Bit Score: 319.13  E-value: 5.17e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  149 DKILVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSY 228
Cdd:cd16209      1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034590989  229 HAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16209     81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 991-1173 6.47e-89

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: 284.26  E-value: 6.47e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  991 GRVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLERIQG 1070
Cdd:pfam08703    1 KQVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1071 MTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEkqgsllsPQFQKEALAEYEAR 1150
Cdd:pfam08703   81 AKKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEE-------PQLQAELNAEYEEK 153

                          170       180
                   ....*....|....*....|...
gi 1034590989 1151 MKGLEAEVKESVRACLRTCFPSE 1173
Cdd:pfam08703  154 LKGLPAEVRESVKSCLKEGFPDE 176
PI-PLCc_PRIP_metazoa cd08597
Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein; This ...
 311-662 3.61e-88

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: 285.85  E-value: 3.61e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08597      1 CQDMTQPLSHYFIASSHNTYLIEDQLRGPSSVEGYVRALQRGCRCVELDCWDG--PNGEPVIYHGHTLTSKISFRSVIEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPlekfPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08597     79 INEYAFVASEYPLILCIENHC-SEKQQLVMAQYLKEIFGDKLYTEP----PNEGESYLPSPHDLKGKIIIKGKK------ 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeIKKMQsdegtaglevtAYEEMSSLV 550
Cdd:cd08597    148 -------------------------------------------------------LKRRK-----------LCKELSDLV 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  551 NYIQPTKFVSFEFSAprlftcifsghkhKKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMP 630
Cdd:cd08597    162 SLCKSVRFQDFPTSA-------------QNQKYWEVCSFSENLARRLANEFPEDFVNYNKKFLSRVYPSPMRVDSSNYNP 228

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034590989  631 QMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08597    229 QDFWNCGCQIVAMNYQTPGLMMDLNTGKFLEN 260
PI-PLC1c_yeast cd08598
Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This ...
 312-659 8.90e-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: 280.67  E-value: 8.90e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  312 HDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAI 391
Cdd:cd08598      2 EDLSRPLNEYFISSSHNTYLLGRQLAGDSSVEGYIRALQRGCRCVEIDVWDG--DDGEPVVTHGYTLTSSVPFRDVCRAI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  392 AESAFKTSPYPIILSFENHVDsPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKpgvpLPSPEDLRGKILIKNKKNqfsgpt 471
Cdd:cd08598     80 KKYAFVTSPYPLILSLEVHCD-AEQQERMVEIMKETFGDLLVTEPLDGLEDE----LPSPEELRGKILIKVKKE------ 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  472 ssskdtggeaegSSPPSapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeemsslvn 551
Cdd:cd08598    149 ------------SKTPN--------------------------------------------------------------- 153

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  552 yiqptkfvsfefsaprlftcifsgHkhkknrsyvISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQ 631
Cdd:cd08598    154 ------------------------H---------IFSLSERSLLKLLKDKRAALDKHNRRHLMRVYPSGTRISSSNFNPL 200

                          330       340
                   ....*....|....*....|....*...
gi 1034590989  632 MFWNAGCQMVALNFQTMDLPMQQNMAVF 659
Cdd:cd08598    201 PFWRAGVQMVALNWQTYDLGMQLNEAMF 228
PI-PLCc_gamma cd08592
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma; This family ...
 312-662 7.43e-86

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: 278.16  E-value: 7.43e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  312 HDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAI 391
Cdd:cd08592      2 QDMNNPLSHYWIASSHNTYLTGDQLSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPIIYHGHTLTSKIKFMDVLKTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  392 AESAFKTSPYPIILSFENHVDSPrQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKNKKnqfsgpt 471
Cdd:cd08592     80 KEHAFVTSEYPVILSIENHCSLP-QQRNMAQAFKEVFGDMLLTQPVD----RNADQLPSPNQLKRKIIIKHKK------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  472 ssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMsslvn 551
Cdd:cd08592    148 ----------------------------------------------------------------------LFYEM----- 152

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  552 yiqptkfvsfefsaprlftcifsghkhkknrsyviSSFTELKAYDLLSKA-SVQFVDYNKRQMSRIYPKGTRMDSSNYMP 630
Cdd:cd08592    153 -----------------------------------SSFPETKAEKYLNRQkGKIFLKYNRRQLSRVYPKGQRVDSSNYDP 197

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034590989  631 QMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08592    198 VPMWNCGSQMVALNFQTPDKPMQLNQALFMLN 229
PI-PLCc_delta3 cd08630
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily ...
 311-662 1.20e-83

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: 273.05  E-value: 1.20e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08630      1 FQDMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEG--PGGEPVIYHGHTLTSKILFRDVIQA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKpgvPLPSPEDLRGKILIKNKKNQFSgp 470
Cdd:cd08630     79 VRQHAFTASPYPVILSLENHC-GLEQQAAMARHLQTILGDMLVTQPLDSLNPE---ELPSPEELKGRVLVKGKKLQIS-- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSLV 550
Cdd:cd08630    153 -------------------------------------------------------------------------PELSALA 159

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  551 NYIQPTKFVSFEfSAPrlftcifsghkhKKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMP 630
Cdd:cd08630    160 VYCQATRLRTLE-PAP------------VQPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSP 226

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034590989  631 QMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08630    227 QEMWNSGCQLVALNFQTPGYEMDLNAGRFLVN 258
PI-PLCc_delta1 cd08629
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily ...
 311-662 7.88e-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: 265.36  E-value: 7.88e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08629      1 YQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDG--PNQEPIIYHGYTFTSKILFCDVLRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKNKKNQFSgp 470
Cdd:cd08629     79 IRDYAFKASPYPVILSLENHC-SLEQQRVMARHLRAILGPILLDQPLD----GVTTSLPSPEQLKGKILLKGKKLKLV-- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSLV 550
Cdd:cd08629    152 -------------------------------------------------------------------------PELSDMI 158

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  551 NYIQPTKFVSFEFSaprlftcifsghKHKKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMP 630
Cdd:cd08629    159 IYCKSVHFGGFSSP------------GTSGQAFYEMASFSESRALRLLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSP 226

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034590989  631 QMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08629    227 VEMWNGGCQIVALNFQTPGPEMDVYLGCFQDN 258
PI-PLCc_zeta cd08595
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta; This family ...
 311-662 1.29e-80

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: 264.88  E-value: 1.29e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKppDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08595      1 YQDMDHPLSDYFISSSHNTYLVSDQLVGPSDLDGYVSALRKGCRCLEIDCWDGA--DNEPVVYHGYTLTSKILFKEVITT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKpgvPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08595     79 VEKYAFEKSDYPVVLSLENHC-STEQQEIMAHYLVSILGEKLLRAPIDDPATG---ELPSPEALKFKILVKNKK------ 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeEIKKMQSDegtaglevtayeemssLV 550
Cdd:cd08595    149 ------------------------------------------------------KIAKALSD----------------LV 158

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  551 NYIQPTKFVSFEfsaprlftcifsgHKHKKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMP 630
Cdd:cd08595    159 IYTKSEKFCSFT-------------HSRDNQHSYENNSIGENKARKLLKSSGADFVGHTQRFITRIYPKGTRASSSNYNP 225

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034590989  631 QMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08595    226 QEFWNVGCQMVALNFQTLGAPMDLQNGKFLDN 257
PI-PLCc_delta4 cd08631
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4; This subfamily ...
 311-662 1.06e-79

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: 262.19  E-value: 1.06e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08631      1 YQDMTQPLCHYFICSSHNTYLMEDQLRGQSSVEGYIRALKRGCRCVEVDVWDG--PNGEPIVYHGHTFTSKILFKDVVAA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLE-KFPlkpgVPLPSPEDLRGKILIKNKKNQFSg 469
Cdd:cd08631     79 VAQYAFQVSDYPVILSLENHC-GVEQQQTMAQHLTEILGEKLLSTTLDgVLP----TQLPSPEELRGKILLKGKKIRLS- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  470 ptssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayEEMSSL 549
Cdd:cd08631    153 --------------------------------------------------------------------------PELSDC 158

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  550 VNYIQPTKFVSFEfsaprlftcifsgHKHKKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYM 629
Cdd:cd08631    159 VIYCKSVSFRSFT-------------HSREHYHFYEISSFTETKARKLIREAGNEFVQHNTWQLSRVYPSGLRTDSSNYN 225

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1034590989  630 PQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08631    226 PQEMWNAGCQMVALNFQTAGLEMDLNDGLFRQN 258
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 314-462 2.08e-79

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


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 256.66  E-value: 2.08e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  314 MTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIAE 393
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034590989  394 SAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKN 462
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLD----DDLTELPSPEDLKGKILIKG 142
PI-PLCc_epsilon cd08596
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon; This family ...
 313-662 3.82e-79

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: 260.55  E-value: 3.82e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  313 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKppDEEPIITHGFTMTTDIFFKEAIEAIA 392
Cdd:cd08596      3 DLQYPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLTGCRCVELDCWDGD--DGMPIIYHGHTLTTKIPFKDVVEAIN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  393 ESAFKTSPYPIILSFENHVDSPrQQAKMAEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgpts 472
Cdd:cd08596     81 RSAFITSDYPVILSIENHCSLQ-QQRKMAEIFKTVFGEKLVTKFLFESDFSDDPSLPSPLQLKNKILLKNKK-------- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  473 sskdtggeaegssppsAPagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeEMSSLVNY 552
Cdd:cd08596    152 ----------------AP------------------------------------------------------ELSDLVIY 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  553 IQPTKFVSfeFSAPrlfTCifsghkhkknrsYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQM 632
Cdd:cd08596    162 CQAVKFPG--LSTP---KC------------YHISSLNENAAKRLCRRYPQKLVQHTRCQLLRTYPAATRIDSSNPNPLI 224

                          330       340       350
                   ....*....|....*....|....*....|
gi 1034590989  633 FWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08596    225 FWLHGLQLVALNYQTDDLPMHLNAAMFEAN 254
PI-PLCc_eta cd08594
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta; This family ...
 311-662 5.23e-76

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: 250.87  E-value: 5.23e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08594      1 NQDMTQPLSHYFIASSHNTYLTGDQLLSQSRVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKILFRDVIET 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLtepLEKFPLKPGVPLPSPEDLRGKILIKNKKNQfsgp 470
Cdd:cd08594     79 INKYAFIKNEYPVILSIENHC-SVQQQKKMAQYLKEILGDKLD---LSSVISGDSKQLPSPQSLKGKILIKGKKWQ---- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtayeemsslv 550
Cdd:cd08594        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  551 nyiqptkfvsfefsaprlftcifsghkhkknrsyvISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMP 630
Cdd:cd08594    151 -----------------------------------VSSFSETRAHQIVQQKAAQFLRFNQRQLSRIYPSAYRIDSSNFNP 195

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034590989  631 QMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08594    196 QPYWNAGCQLVALNYQTEGRMLQLNRAKFRAN 227
PI-PLCc_eta2 cd08633
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily ...
 311-662 4.39e-74

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: 246.49  E-value: 4.39e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08633      1 NQDMTQPLSHYFITSSHNTYLSGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDG--PDGEPIVHHGYTLTSKILFKDVIET 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVDSPrQQAKMAEYCRTIFGDMLltePLEKFPLKPGVPLPSPEDLRGKILIKNKKnqfsgp 470
Cdd:cd08633     79 INKYAFIKNEYPVILSIENHCSVP-QQKKMAQYLTEILGDKL---DLSSVISNDCTRLPSPEILKGKILVKGKK------ 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  471 tssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMSSLV 550
Cdd:cd08633    149 -----------------------------------------------------------------------LSRALSDLV 157

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  551 NYIQPTKFVSFEFSAprlftcifsghkhkkNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMP 630
Cdd:cd08633    158 KYTKSVRVHDIETEA---------------TSSWQVSSFSETKAHQILQQKPAQYLRFNQRQLSRIYPSSYRVDSSNYNP 222

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034590989  631 QMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08633    223 QPFWNAGCQMVALNYQSEGRMLQLNRAKFSAN 254
PI-PLCc_gamma2 cd08628
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2; This subfamily ...
 313-662 1.20e-71

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: 239.57  E-value: 1.20e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  313 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIA 392
Cdd:cd08628      3 DMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRMGCRCIELDCWDG--PDGKPIIYHGWTRTTKIKFDDVVQAIK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  393 ESAFKTSPYPIILSFENHVDSpRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKNKKnqfsgpts 472
Cdd:cd08628     81 DHAFVTSEYPVILSIEEHCSV-EQQRHMAKVFKEVFGDKLLMKPLE----ASADQLPSPTQLKEKIIIKHKK-------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  473 sskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevTAYEEMSSLVNY 552
Cdd:cd08628    148 --------------------------------------------------------------------LIAIELSDLVVY 159

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  553 IQPTKFVSFEFSAPrlftcifsghKHKKNRSYVissftELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYMPQM 632
Cdd:cd08628    160 CKPTSKTKDNLENP----------DFKEIRSFV-----ETKAPSIIRQKPVQLLKYNRKGLTRVYPKGQRVDSSNYDPFR 224

                          330       340       350
                   ....*....|....*....|....*....|
gi 1034590989  633 FWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08628    225 LWLCGSQMVALNFQTADKYMQLNHALFSLN 254
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-141 6.11e-69

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


Pssm-ID: 465506  Cd Length: 131  Bit Score: 226.88  E-value: 6.11e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989   12 KVKAYLSQGERFIKWDDETTVASP-VILRVDPKGYYLYWTYQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVFNMDFP 90
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034590989   91 DNSFLLKTLTVVSGPDMVDLTFHNFVSYKENVGKAWAEDVLALVKHPLTAN 141
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
PI-PLCc_eta1 cd08632
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily ...
 311-662 4.54e-67

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: 226.45  E-value: 4.54e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08632      1 NQDMDQPLCNYFIASSHNTYLTGDQLLSQSKVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKITFRDVIET 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDML-LTEPLEKFPLKpgvpLPSPEDLRGKILIKNKKnqfsg 469
Cdd:cd08632     79 INKYAFVKNEFPVILSIENHC-SIQQQKKIAQYLKEIFGDKLdLSSVLTGDPKQ----LPSPQLLKGKILVKGKK----- 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  470 ptssskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMSSL 549
Cdd:cd08632    149 ------------------------------------------------------------------------LCRDLSDL 156

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  550 VNYiqpTKFVSFEfsaprlfTCIFSGHKHKknrsyvISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSNYM 629
Cdd:cd08632    157 VVY---TNSVAAQ-------DIVDDGSTGN------VLSFSETRAHQLVQQKAEQFMTYNQKQLTRIYPSAYRIDSSNFN 220

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1034590989  630 PQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08632    221 PLPYWNVGCQLVALNYQSEGRMMQLNRAKFMVN 253
PI-PLCc_gamma1 cd08627
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily ...
 313-662 1.80e-66

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: 223.75  E-value: 1.80e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  313 DMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIA 392
Cdd:cd08627      3 EMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPVIYHGHTLTTKIKFSDVLHTIK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  393 ESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEkfplKPGVPLPSPEDLRGKILIKNKKnqfsgpts 472
Cdd:cd08627     81 EHAFVTSEYPIILSIEDHC-SIVQQRNMAQHFKKVFGDMLLTKPVD----INADGLPSPNQLKRKILIKHKK-------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  473 sskdtggeaegssppsapagegtvwageegteleeeeveeeeeeesgnldeeeikkmqsdegtaglevtAYEEMsslvny 552
Cdd:cd08627    148 ---------------------------------------------------------------------LYRDM------ 152

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  553 iqptkfvsfefsaprlftcifsghkhkknrsyviSSFTELKAYDLLSKAS-VQFVDYNKRQMSRIYPKGTRMDSSNYMPQ 631
Cdd:cd08627    153 ----------------------------------SSFPETKAEKYVNRSKgKKFLQYNRRQLSRIYPKGQRLDSSNYDPL 198

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1034590989  632 MFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08627    199 PMWICGSQLVALNFQTPDKPMQMNQALFMLG 229
EFh_PI-PLCbeta cd16200
EF-hand motif found in metazoan phosphoinositide-specific phospholipase C (PI-PLC)-beta ...
 149-299 5.62e-65

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


Pssm-ID: 320030 [Multi-domain]  Cd Length: 153  Bit Score: 216.34  E-value: 5.62e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  149 DKILVKLKMQLNSEGKIPVKNFFQMFPAD--RKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFT 226
Cdd:cd16200      1 KKLYTKLKLSVNITGKIPVKNIIKCFSSDkkRKRVLKALKALGLPDGKNDEIDPEDFTFEKFFKLYNKLCPRPDIDEIFK 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034590989  227 SYHAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16200     81 ELGGKRKPYLTLEQLVDFLNEEQRDPRLNEILFPFHTKEQAKKLIDKYEPNEKNKKKGQLTLEGFLRYLMSDE 153
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 314-463 1.61e-64

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


Pssm-ID: 197543 [Multi-domain]  Cd Length: 143  Bit Score: 214.84  E-value: 1.61e-64
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989   314 MTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTDIFFKEAIEAIAE 393
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDG--PDGEPVIYHGHTFTLPIKLSEVLEAIKD 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989   394 SAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPLEKFPLKpgvpLPSPEDLRGKILIKNK 463
Cdd:smart00148   79 FAFVTSPYPVILSLENHC-SPDQQAKMAQMFKEIFGDMLYTPPLTSSLEV----LPSPEQLRGKILLKVR 143
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 547-674 6.61e-61

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: 203.24  E-value: 6.61e-61
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989   547 SSLVNYIQPTKFVSFEFSaprlftcifsghkHKKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSS 626
Cdd:smart00149    1 SDLVIYCAPVKFRSFESA-------------ESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSS 67

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 1034590989   627 NYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFM 674
Cdd:smart00149   68 NYNPQVFWNHGCQMVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
EFh_PI-PLCbeta1 cd16208
EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1); PI-PLC-beta1, ...
 149-299 5.65e-59

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


Pssm-ID: 320038  Cd Length: 151  Bit Score: 199.33  E-value: 5.65e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  149 DKILVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSY 228
Cdd:cd16208      1 EKAYTKLKLQVNPEGRIPVKNIYRLFSADRKRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDHIFSEF 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034590989  229 HAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16208     81 GAKSKPYLSVDQMTEFINSKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSTLAKKGQISVDGFMRYLSGEE 151
PI-PLCc_plant cd08599
Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family ...
 311-662 4.58e-58

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


Pssm-ID: 176541 [Multi-domain]  Cd Length: 228  Bit Score: 199.91  E-value: 4.58e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDeePIITHGFTMTTDIFFKEAIEA 390
Cdd:cd08599      1 HHDMTAPLSHYFIFSSHNSYLTGNQLSSRSSTAPIIEALLRGCRVIELDLWPGGRGD--ICVLHGGTLTKPVKFEDCIKA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  391 IAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEPlekfPLKPGVPLPSPEDLRGKILIKNKknqfsgp 470
Cdd:cd08599     79 IKENAFTASEYPVIITLENHL-SPELQAKAAQILRETLGDKLFYPD----SEDLPEEFPSPEELKGKILISDK------- 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  471 tssskdtggeaegssPPsapagegtvwageegteleeeeveeeeeEESGNLDEEEIKKMQSDEGTAGLevtayeemsslv 550
Cdd:cd08599    147 ---------------PP----------------------------VIRNSLSETQLKKVIEGEHPTDL------------ 171

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  551 nyiqptkfvsfefsaprlftcifsghkhkknrsyvissftelkaydllskasvqfVDYNKRQMSRIYPKGTRMDSSNYMP 630
Cdd:cd08599    172 -------------------------------------------------------IEFTQKNLLRVYPAGLRITSSNYDP 196

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034590989  631 QMFWNAGCQMVALNFQTMDLPMQQNMAVFEFN 662
Cdd:cd08599    197 MLAWMHGAQMVALNMQGYDRPLWLNRGKFRAN 228
PLN02228 PLN02228
Phosphoinositide phospholipase C
 217-799 5.56e-57

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 207.97  E-value: 5.56e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  217 PRPEIDEIFTSYHAKAKpyMTKEHLTKFINQKQRDSRlnsllfppARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLC 296
Cdd:PLN02228    22 PPVSIKRLFEAYSRNGK--MSFDELLRFVSEVQGERH--------AGLDYVQDIFHSVKHHNVFHHHGLVHLNAFYRYLF 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  297 GPENSVLAQDKLLlHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKgKPPDEEPIITHGF 376
Cdd:PLN02228    92 SDTNSPLPMSGQV-HHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWP-NPSGNAAEVRHGR 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  377 TMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLL---TEPLEKFplkpgvplPSPED 453
Cdd:PLN02228   170 TLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHL-PPNLQAQVAKMLTKTFRGMLFrctSESTKHF--------PSPEE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  454 LRGKILIKNKKNQFSGPTSSSKDTggeaegssppSAPAGEGTVWAGEEGTeleeeeveeeeeeesgnldEEEIKKMQSDE 533
Cdd:PLN02228   241 LKNKILISTKPPKEYLESKTVQTT----------RTPTVKETSWKRVADA-------------------ENKILEEYKDE 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  534 GTAGLEvtaYEEMSSL--VNYIQPTKfvsfefsaprlfTCIfSGHKHKKNRsyviSSFTELKAYDLLSKASVQFVDYNKR 611
Cdd:PLN02228   292 ESEAVG---YRDLIAIhaANCKDPLK------------DCL-SDDPEKPIR----VSMDEQWLETMVRTRGTDLVRFTQR 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  612 QMSRIYPKGTRMDSSNYMPQMFWNAGCQMVALNFQT--MDLPMQQNMavFEFNGQSGYLLKHEFMRRPDKQFNPFSvdri 689
Cdd:PLN02228   352 NLVRIYPKGTRVDSSNYDPHVGWTHGAQMVAFNMQGhgKQLWIMQGM--FRANGGCGYVKKPRILLDEHTLFDPCK---- 425

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  690 DVVVATTLSITVISGQ----------FLSERSVRTYVEVELFGLPGDPKrRYRTKLspSTNSINPVWKEEPFVFEkILMP 759
Cdd:PLN02228   426 RLPIKTTLKVKIYTGEgwdldfhlthFDQYSPPDFFVKIGIAGVPRDTV-SYRTET--AVDQWFPIWGNDEFLFQ-LRVP 501

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 1034590989  760 ELASLRVAVME----EGNKFLGHRIIPINALNSGYHHLCLHSES 799
Cdd:PLN02228   502 ELALLWFKVQDydndTQNDFAGQTCLPLPELKSGVRAVRLHDRA 545
PLN02222 PLN02222
phosphoinositide phospholipase C 2
 219-813 3.15e-56

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 206.03  E-value: 3.15e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  219 PEIDEIFTSYHAKAkpYMTKEHLTKFINQKQRDSRlnsllfppARPDQVQGLIDKyepSGINAQRGQLSPEGMVWFLCGP 298
Cdd:PLN02222    25 REIKTIFEKYSENG--VMTVDHLHRFLIDVQKQDK--------ATREDAQSIINS---ASSLLHRNGLHLDAFFKYLFGD 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  299 ENSVLAQDKLllHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIItHGFTM 378
Cdd:PLN02222    92 NNPPLALHEV--HHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSDKDDIDVL-HGMTL 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  379 TTDIFFKEAIEAIAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTEP----LEKFplkpgvplPSPEDL 454
Cdd:PLN02222   169 TTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHL-TPDLQSKVAEMVTEIFGEILFTPPvgesLKEF--------PSPNSL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  455 RGKILIKNKKNQfsgPTSSSKDTGGEAEGSSppsapAGEGTVWaGEEGTELEEEEVEEEEEEESGNLDEEEikkmqsDEG 534
Cdd:PLN02222   240 KKRIIISTKPPK---EYKEGKDDEVVQKGKD-----LGDEEVW-GREVPSFIQRNKSVDKNDSNGDDDDDD------DDG 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  535 TAGLEVTAYEEMSSLvnyiqptkfVSFEFSAPR--LFTCIfsGHKHKKNRSYVISSFTELKAYDLLSKasvQFVDYNKRQ 612
Cdd:PLN02222   305 EDKSKKNAPPQYKHL---------IAIHAGKPKggITECL--KVDPDKVRRLSLSEEQLEKAAEKYAK---QIVRFTQHN 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  613 MSRIYPKGTRMDSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFMRRPDKQFNPFSvDRIDVV 692
Cdd:PLN02222   371 LLRIYPKGTRVTSSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKKPDLLLKSGSDSDIFD-PKATLP 449

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  693 VATTLSITVISGQ----------FLSERSVRTYVEVELFGLPGDPKRRyRTKlSPSTNSInPVWKEepfVFE-KILMPEL 761
Cdd:PLN02222   450 VKTTLRVTIYMGEgwyfdfrhthFDQYSPPDFYTRVGIAGVPGDTVMK-KTK-TLEDNWI-PAWDE---VFEfPLTVPEL 523

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034590989  762 ASLRVAV----MEEGNKFLGHRIIPINALNSGYHHLCLHSESNMPLTMPALFIFLE 813
Cdd:PLN02222   524 ALLRLEVheydMSEKDDFGGQTCLPVWELSQGIRAFPLHSRKGEKYKSVKLLVKVE 579
PLN02952 PLN02952
phosphoinositide phospholipase C
 310-796 7.93e-56

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 205.23  E-value: 7.93e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  310 LHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDeEPIITHGFTMTTDIFFKEAIE 389
Cdd:PLN02952   121 VHHDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGSTKD-EILVLHGRTLTTPVPLIKCLK 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  390 AIAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLteplekFPLKPG-VPLPSPEDLRGKILIKNKKnqfs 468
Cdd:PLN02952   200 SIRDYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLY------YPESDSlVQFPSPESLKHRIIISTKP---- 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  469 gPTSSSKDTGGEAEGSSPPSAPAGEGTvwageegteLEEEEVEEEEEEESGNLD-EEEIKKMQSDEGTAGLEVTAYEems 547
Cdd:PLN02952   269 -PKEYLESSGPIVIKKKNNVSPSGRNS---------SEETEEAQTLESMLFEQEaDSRSDSDQDDNKSGELQKPAYK--- 335

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  548 slvnyiqptKFVSFEFSAPRlfTCIFSGHKHKKNRSYVIsSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDSSN 627
Cdd:PLN02952   336 ---------RLITIHAGKPK--GTLKDAMKVAVDKVRRL-SLSEQELEKAATTNGQDVVRFTQRNILRIYPKGTRITSSN 403

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  628 YMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFM--RRPDKQ-FNPfsvdRIDVVVATTLSITVISG 704
Cdd:PLN02952   404 YKPLIGWMHGAQMIAFNMQGYGKSLWLMHGMFRANGGCGYLKKPDFLmkKGFHDEvFDP----KKKLPVKKTLKVKVYLG 479

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  705 ----------QFLSERSVRTYVEVELFGLPGDPKRRyRTKLspSTNSINPVWKEEpFVFeKILMPELASLRVAV----ME 770
Cdd:PLN02952   480 dgwrldfshtHFDSYSPPDFYTKMYIVGVPADNAKK-KTKI--IEDNWYPAWNEE-FSF-PLTVPELALLRIEVreydMS 554

                          490       500
                   ....*....|....*....|....*.
gi 1034590989  771 EGNKFLGHRIIPINALNSGYHHLCLH 796
Cdd:PLN02952   555 EKDDFGGQTCLPVSELRPGIRSVPLH 580
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-144 1.30e-55

Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is regulated by heterotrimeric G protein-coupled receptors through their C2 domain and long C-terminal extension which forms an autoinhibitory helix. There are four isoforms: PLC-beta1-4. The PH domain of PLC-beta2 and PLC-beta3 plays a dual role, much like PLC-delta1, by binding to the plasma membrane, as well as the interaction site for the catalytic activator. However, PLC-beta binds to the lipid surface independent of PIP2. PLC-beta1 seems to play unspecified roles in cellular proliferation and differentiation. PLC-beta consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves, a C2 domain and a C-terminal PDZ. Members of the Rho GTPase family (e.g., Rac1, Rac2, Rac3, and cdc42) have been implicated in their activation by binding to an alternate site on the N-terminal PH domain. A basic amino acid region within the enzyme's long C-terminal tail appears to function as a Nuclear Localization Signal for import into the nucleus. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.the plasma membrane, but only a few (less than 10%) display strong specificity in binding inositol phosphates. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinases, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, cytoskeletal associated molecules, and in lipid associated enzymes.


Pssm-ID: 270167  Cd Length: 127  Bit Score: 188.93  E-value: 1.30e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989   17 LSQGERFIKWDDETTVASPVILRVDPKGYYLYWTYQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVfNMDFPDNSFLL 96
Cdd:cd13361      1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1034590989   97 KTLTVVSGPDMVDLTFHNFVSYKENVGKAWAEDVLALVKHPLTANASR 144
Cdd:cd13361     80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
PI-PLC-Y pfam00387
Phosphatidylinositol-specific phospholipase C, Y domain; This associates with pfam00388 to ...
 546-673 1.71e-54

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


Pssm-ID: 459794  Cd Length: 114  Bit Score: 184.97  E-value: 1.71e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  546 MSSLVNYIQPTKFVSFEFSAPRLFTCIFSghkhkknrsyvissFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRMDS 625
Cdd:pfam00387    1 LSDLVVYTQSVKFKSFSTPESKTPNHIFS--------------FSESKALKLIKSSSAAFVKHNRRHLMRVYPKGTRVDS 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1034590989  626 SNYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEF 673
Cdd:pfam00387   67 SNFNPQPFWNCGVQMVALNWQTPDEGMQLNEGMFADNGGCGYVLKPEF 114
EFh_PI-PLCbeta3 cd16210
EF-hand motif found in phosphoinositide phospholipase C beta 3 (PI-PLC-beta3); PI-PLC-beta3, ...
 150-299 9.59e-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: 9.59e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  150 KILVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSYH 229
Cdd:cd16210      2 KAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILLEIG 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  230 AKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16210     82 AKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQVRQLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 151
EFh_PI-PLC21 cd16213
EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family ...
 150-295 3.36e-48

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


Pssm-ID: 320043  Cd Length: 154  Bit Score: 168.63  E-value: 3.36e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  150 KILVKLKMQLNSEGKIPVKNFFQMFPA---DRKRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFT 226
Cdd:cd16213      2 KAYTKLTLQTDKEGKIPVKNIVKMFAQhkdDRKRVEKALEAIGLPSGKNDAIDPKKFTFEDFFNFYRRLTGRQEVEKIFD 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034590989  227 SYHAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFL 295
Cdd:cd16213     82 ELGAKKKPYLTTEQFVDFLNKTQRDPRLNEILYPYANPKRARDLINQYEPNKSFAKKGHLSVEGFLRYL 150
PLN02230 PLN02230
phosphoinositide phospholipase C 4
 217-813 3.16e-46

phosphoinositide phospholipase C 4


Pssm-ID: 177875 [Multi-domain]  Cd Length: 598  Bit Score: 176.43  E-value: 3.16e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  217 PRPEIDEIFTSYhAKAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQV---QGLIDKYepsginaQRGQLSPEGMVW 293
Cdd:PLN02230    27 PVADVRDLFEKY-ADGDAHMSPEQLQKLMAEEGGGEGETSLEEAERIVDEVlrrKHHIAKF-------TRRNLTLDDFNY 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  294 FLCGPENSVLAQDKLllHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDeePIIT 373
Cdd:PLN02230    99 YLFSTDLNPPIADQV--HQNMDAPLSHYFIFTGHNSYLTGNQLSSNCSELPIADALRRGVRVVELDLWPRGTDD--VCVK 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  374 HGFTMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLL---TEPLEKFplkpgvplPS 450
Cdd:PLN02230   175 HGRTLTKEVKLGKCLDSIKANAFAISKYPVIITLEDHL-TPKLQFKVAKMITQTFGDMLYyhdSEGCQEF--------PS 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  451 PEDLRGKILIKNK--KNQFSGPTSSSKDTGGEAEGSsppsapagEGTVWAGEEGTELEEEEVEEEEEEESGNL--DEEEI 526
Cdd:PLN02230   246 PEELKEKILISTKppKEYLEANDAKEKDNGEKGKDS--------DEDVWGKEPEDLISTQSDLDKVTSSVNDLnqDDEER 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  527 KKMQSDEgTAGLEVTAYEemsslvnyiqptKFVSFEFSAPRLFTCIFSGHKHKKNRSYVISSftelkayDLLSKASVQF- 605
Cdd:PLN02230   318 GSCESDT-SCQLQAPEYK------------RLIAIHAGKPKGGLRMALKVDPNKIRRLSLSE-------QLLEKAVASYg 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  606 ---VDYNKRQMSRIYPKGTRMDSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFMRRPDKQFN 682
Cdd:PLN02230   378 advIRFTQKNFLRIYPKGTRFNSSNYKPQIGWMSGAQMIAFNMQGYGRALWLMEGMFRANGGCGYVKKPDFLMDAGPNGQ 457

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  683 PFsVDRIDVVVATTLSITVISGQF----LSERSVRTYVEVELF---GLPGDPKRRYRTKLSPSTNSINPVWKEEpFVFeK 755
Cdd:PLN02230   458 DF-YPKDNSCPKKTLKVKVCMGDGwlldFKKTHFDSYSPPDFFvrvGIAGAPVDEVMEKTKIEYDTWTPIWNKE-FIF-P 534

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034590989  756 ILMPELASLRVAVME----EGNKFLGHRIIPINALNSGYHHLCLHSESNMPLTMPALFIFLE 813
Cdd:PLN02230   535 LAVPELALLRVEVHEhdinEKDDFGGQTCLPVSEIRQGIHAVPLFNRKGVKYSSTRLLMRFE 596
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 694-815 9.13e-38

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


Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 137.67  E-value: 9.13e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  694 ATTLSITVISGQFLS------ERSVRTYVEVELFGLPGDPKRRYRTKLSPStNSINPVWkEEPFVFEKIlMPELASLRVA 767
Cdd:cd00275      1 PLTLTIKIISGQQLPkpkgdkGSIVDPYVEVEIHGLPADDSAKFKTKVVKN-NGFNPVW-NETFEFDVT-VPELAFLRFV 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034590989  768 VMEE---GNKFLGHRIIPINALNSGYHHLCLHSESNMPLTMPALFIFLEMK 815
Cdd:cd00275     78 VYDEdsgDDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
 154-295 2.83e-28

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


Pssm-ID: 320041  Cd Length: 153  Bit Score: 111.74  E-value: 2.83e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  154 KLKMQLNSEGKIPVKNFFQMFPADR--KRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSYHAK 231
Cdd:cd16211      6 RLCFLVNPNGKIPVRSITRTFASGKteKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFKKINGD 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034590989  232 AKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFL 295
Cdd:cd16211     86 KKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYL 149
PLN02223 PLN02223
phosphoinositide phospholipase C
 311-804 5.45e-27

phosphoinositide phospholipase C


Pssm-ID: 165867 [Multi-domain]  Cd Length: 537  Bit Score: 117.05  E-value: 5.45e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  311 HHDMTQPLNHYFINSSHNTYLTAGQ-FSGLSSAEMYRQVLLSGCRCVELDCWkgkPPDEEPI-ITHGFTMTTDIFFKEAI 388
Cdd:PLN02223   105 HHDMHAPLSHYFIHTSLKSYFTGNNvFGKLYSIEPIIDALEQGVRVVELDLL---PDGKDGIcVRPKWNFEKPLELQECL 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  389 EAIAESAF-KTSPYPIILSFENHVdSPRQQAKMAEYCRTIFGDMLLTE----PLEKFplkpgvplPSPEDLRGKILIKNK 463
Cdd:PLN02223   182 DAIKEHAFtKCRSYPLIITFKDGL-KPDLQSKATQMIDQTFGDMVYHEdpqhSLEEF--------PSPAELQNKILISRR 252

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  464 knqfsgptssskdtggeaegssPPS----APAGEGTVwageegteleeeeveeeeeeesGNLDEEEIKKMQSDEgtagle 539
Cdd:PLN02223   253 ----------------------PPKellyAKADDGGV----------------------GVRNELEIQEGPADK------ 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  540 vtayeemsslvNYiqpTKFVSFEFSAPR-LFTCIFSGHKHKKNRSYVISSftelkayDLLSKASVQFVDYN-KRQMSRIY 617
Cdd:PLN02223   283 -----------NY---QSLVGFHAVEPRgMLQKALTGKADDIQQPGWYER-------DIISFTQKKFLRTRpKKKNLLIN 341

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  618 PKgtrmdssnYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFMRR--PDKQFNPfsvdRIDVVVAT 695
Cdd:PLN02223   342 AP--------YKPQRAWMHGAQLIALSRKDDKEKLWLMQGMFRANGGCGYVKKPDFLLNagPSGVFYP----TENPVVVK 409

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  696 TLSITVISGQF----LSERSVR-----TYVEVELFGLPGDPKrryRTKLSPSTNSINPVWKEEpFVFeKILMPELASLRV 766
Cdd:PLN02223   410 ILKVKIYMGDGwivdFKKRIGRlskpdLYVRISIAGVPHDEK---IMKTTVKNNEWKPTWGEE-FTF-PLTYPDLALISF 484

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1034590989  767 AV----MEEGNKFLGHRIIPINALNSGYHHLCLHSE------SNMPLT 804
Cdd:PLN02223   485 EVydyeVSTADAFCGQTCLPVSELIEGIRAVPLYDErgkacsSTMLLT 532
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 324-482 6.28e-25

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: 102.90  E-value: 6.28e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  324 NSSHNTYLTAGQfsgLSSAEMYRQVLLSGCRCVELDCWKGKppDEEPIITHGFTMT------TDIFFKEAIEAIAESAFk 397
Cdd:cd08555      1 VLSHRGYSQNGQ---ENTLEAFYRALDAGARGLELDVRLTK--DGELVVYHGPTLDrttagiLPPTLEEVLELIADYLK- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  398 TSPYPIILSFENHVDS---PRQQAKMAEYCRTIFGDmllteplekfplkpgvplpspeDLRGKILIKNkKNQFS-----G 469
Cdd:cd08555     75 NPDYTIILSLEIKQDSpeyDEFLAKVLKELRVYFDY----------------------DLRGKVVLSS-FNALGvdyynF 131

                          170
                   ....*....|...
gi 1034590989  470 PTSSSKDTGGEAE 482
Cdd:cd08555    132 SSKLIKDTELIAS 144
EFh_NorpA_like cd16212
EF-hand motif found in Drosophila melanogaster No receptor potential A protein (NorpA) and ...
 153-299 2.38e-23

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


Pssm-ID: 320042 [Multi-domain]  Cd Length: 153  Bit Score: 97.62  E-value: 2.38e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  153 VKLKMQLNSEGKIPVKNFFQMFPADR--KRVEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSYHA 230
Cdd:cd16212      5 MRLGFMVDSGGKIPVKHIARTFASGKteKLVYQCLAEMGLPSGKGDSIEKEDFTFEKFYALYHKICPRNDIEELFTSITK 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034590989  231 KAKPYMTKEHLTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16212     85 GKGEHISLAQLINFMNDKQRDPRLNEILYPLYDEKRCTEIIKAYEQNEENIKNKRMSKDGFIRYLMSDE 153
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 696-792 7.20e-14

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 68.67  E-value: 7.20e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989   696 TLSITVISGQFLSER----SVRTYVEVELFGlpgDPKRRYRTKLSPSTNsiNPVWKEEpFVFEkILMPELASLRVAVMEE 771
Cdd:smart00239    1 TLTVKIISARNLPPKdkggKSDPYVKVSLDG---DPKEKKKTKVVKNTL--NPVWNET-FEFE-VPPPELAELEIEVYDK 73

                            90       100
                    ....*....|....*....|....*
gi 1034590989   772 ----GNKFLGHRIIPINALNSGYHH 792
Cdd:smart00239   74 drfgRDDFIGQVTIPLSDLLLGGRH 98
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 195-299 1.01e-12

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


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 66.48  E-value: 1.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  195 NDAINPEDFPEpvyksFLMSLCPRPEIDEIFTSYhAKAKPYMTKEHLTKFINQKQRdsrlnsllFPPARPDQVQGLIDKY 274
Cdd:cd16202     50 EDVLDEEEFVQ-----FYNRLTKRPEIEELFKKY-SGDDEALTVEELRRFLQEEQK--------VKDVTLEWAEQLIETY 115

                           90       100
                   ....*....|....*....|....*
gi 1034590989  275 EPSGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16202    116 EPSEDLKAQGLMSLDGFTLFLLSPD 140
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 155-299 2.43e-11

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 62.69  E-value: 2.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  155 LKMQLNSEGKIPVKNFFQM-----FPADRKRVEAALSACHlpKGKNDAINPEDFpepvyKSFLMSLCPRPEIDEIFTSYH 229
Cdd:cd15898      7 IKADKDGDGKLSLKEIKKLlkrlnIRVSEKELKKLFKEVD--TNGDGTLTFDEF-----EELYKSLTERPELEPIFKKYA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  230 AKAKPYMTKEHLTKFINQKQRDSRlnsllfppaRPDQVQGLIDKYEPSGinaQRGQLSPEGMVWFLCGPE 299
Cdd:cd15898     80 GTNRDYMTLEEFIRFLREEQGENV---------SEEECEELIEKYEPER---ENRQLSFEGFTNFLLSPE 137
C2 pfam00168
C2 domain;
696-789 3.60e-10

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 58.10  E-value: 3.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  696 TLSITVISGQFL----SERSVRTYVEVELfglpGDPKRRYRTKLSPstNSINPVWKEEpFVFEkILMPELASLRVAVMEE 771
Cdd:pfam00168    2 RLTVTVIEAKNLppkdGNGTSDPYVKVYL----LDGKQKKKTKVVK--NTLNPVWNET-FTFS-VPDPENAVLEIEVYDY 73

                           90       100
                   ....*....|....*....|..
gi 1034590989  772 ----GNKFLGHRIIPINALNSG 789
Cdd:pfam00168   74 drfgRDDFIGEVRIPLSELDSG 95
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
892-1160 5.17e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.85  E-value: 5.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  892 KEAAEPRTASLEELRELKgvvKLQRRHEKELRELERRgARRWEELlqrgAAQLAELGPPgvggvgacklgpgKGSRKKRS 971
Cdd:PRK03918   196 KEKEKELEEVLREINEIS---SELPELREELEKLEKE-VKELEEL----KEEIEELEKE-------------LESLEGSK 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  972 LPREESAGAAPgEGPEGVDGRVRELKDRL-ELELLRQGEEQYECVLKRKEQHVAE--QISKMMELAREKQAAELKALKET 1048
Cdd:PRK03918   255 RKLEEKIRELE-ERIEELKKEIEELEEKVkELKELKEKAEEYIKLSEFYEEYLDElrEIEKRLSRLEEEINGIEERIKEL 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1049 S--ENDTKEMKKKLET--KRLERIQGMTKVTTD---KMAQ-ERLKREINNSHIQEvvqvIKQMTENLERHQEKLEEKQAA 1120
Cdd:PRK03918   334 EekEERLEELKKKLKEleKRLEELEERHELYEEakaKKEElERLKKRLTGLTPEK----LEKELEELEKAKEEIEEEISK 409

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034590989 1121 CLEQIREMEKQ---------------------GSLLSPQFQKEALAEYEARMKGLEAEVKE 1160
Cdd:PRK03918   410 ITARIGELKKEikelkkaieelkkakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKE 470
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 215-303 8.95e-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: 8.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  215 LCPRPEIDEIFTSYhAKAKPYMTKEHLTKFINQKQRDSRlnsllfppARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWF 294
Cdd:pfam09279    5 LTQREEIDEIFQEY-SGDGQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAMTKDGFLMY 75


                   ....*....
gi 1034590989  295 LCGPENSVL 303
Cdd:pfam09279   76 LCSPDGSIF 84
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 895-1131 6.85e-07

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 53.59  E-value: 6.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  895 AEPRTASLEELRELKGVVKLQRRHEKE-------------LRELERrgarrweelLQRGAAQLAELGPPGVGGVGACKLG 961
Cdd:pfam17380  337 AEQERMAMERERELERIRQEERKRELErirqeeiameisrMRELER---------LQMERQQKNERVRQELEAARKVKIL 407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  962 PGKGSRKKRSLPREESAGAAPGEGPEGVDGRVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQ--- 1038
Cdd:pfam17380  408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRdrk 487

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1039 -AAELKAL---KETSENDTK----EMKKKLETKRLE-RIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTEnlER 1109
Cdd:pfam17380  488 rAEEQRRKileKELEERKQAmieeERKRKLLEKEMEeRQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE--ER 565

                          250       260
                   ....*....|....*....|..
gi 1034590989 1110 HQEKLEEKQAACLEQIREMEKQ 1131
Cdd:pfam17380  566 SRLEAMEREREMMRQIVESEKA 587
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 697-786 7.45e-07

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


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 48.60  E-value: 7.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  697 LSITVISGQFL----SERSVRTYVEVELfglpgDPKRRYRTKLSPstNSINPVWKEEpFVFEkILMPELASLRVAVMEE- 771
Cdd:cd00030      1 LRVTVIEARNLpakdLNGKSDPYVKVSL-----GGKQKFKTKVVK--NTLNPVWNET-FEFP-VLDPESDTLTVEVWDKd 71

                           90
                   ....*....|....*...
gi 1034590989  772 ---GNKFLGHRIIPINAL 786
Cdd:cd00030     72 rfsKDDFLGEVEIPLSEL 89
PTZ00121 PTZ00121
MAEBL; Provisional
 891-1183 1.65e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 1.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  891 MKEAAEPRTAslEELRELKGVVKLQ--RRHEKELRELERR--GARRWEELLQRGAAQLAELGppgvggvgacKLGPGKGS 966
Cdd:PTZ00121  1539 AKKAEEKKKA--DELKKAEELKKAEekKKAEEAKKAEEDKnmALRKAEEAKKAEEARIEEVM----------KLYEEEKK 1606

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  967 RKKRSLPREESAgaapgegpegvdgrvrelkdRLELELLRQGEEQYECVLKRKEQHvAEQISKMMELAREKQAAELKALK 1046
Cdd:PTZ00121  1607 MKAEEAKKAEEA--------------------KIKAEELKKAEEEKKKVEQLKKKE-AEEKKKAEELKKAEEENKIKAAE 1665

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1047 ETSENDtkEMKKKLETKRLERiqgmtkvTTDKMAQERLKREINNshiqevvqviKQMTENLERHQEklEEKQAAclEQIR 1126
Cdd:PTZ00121  1666 EAKKAE--EDKKKAEEAKKAE-------EDEKKAAEALKKEAEE----------AKKAEELKKKEA--EEKKKA--EELK 1722

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034590989 1127 EMEKQGSLLSPQFQKEalaEYEARMKGLEAEVKESVRACLRTCFPSEAKDKPERACE 1183
Cdd:PTZ00121  1723 KAEEENKIKAEEAKKE---AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
 209-299 2.48e-06

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


Pssm-ID: 320047 [Multi-domain]  Cd Length: 139  Bit Score: 48.20  E-value: 2.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  209 KSFLMSLCPRPEIDEIFTSYhAKAKPYMTKEHLTKFINQKQRDsrlnsllfpPARPDQVQGLIDKYEPSGINAQRGQLSP 288
Cdd:cd16217     59 EEFYKLLTKREEIDVIFGEY-AKSDGTMSRNNLLNFLQEEQRE---------EVAPAYALSLIEKYEPDETAKAQRQMTK 128

                           90
                   ....*....|.
gi 1034590989  289 EGMVWFLCGPE 299
Cdd:cd16217    129 DGFLMYLLSPE 139
PTZ00121 PTZ00121
MAEBL; Provisional
 892-1163 4.69e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 4.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  892 KEAAEPRTAslEELR---ELKGVVKLQRRHEKELRELERR-------GARRWEELLQRGAAQLAELGppgvggvgacKLG 961
Cdd:PTZ00121  1534 KKADEAKKA--EEKKkadELKKAEELKKAEEKKKAEEAKKaeedknmALRKAEEAKKAEEARIEEVM----------KLY 1601

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  962 PGKGSRKKRSLPREESAgaapgegpegvdgrvrelkdRLELELLRQGEEQYECVLKRKEQHvAEQISKMMELAREKQ--- 1038
Cdd:PTZ00121  1602 EEEKKMKAEEAKKAEEA--------------------KIKAEELKKAEEEKKKVEQLKKKE-AEEKKKAEELKKAEEenk 1660

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1039 --AAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVV----QVIKQMTENLERHQE 1112
Cdd:PTZ00121  1661 ikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELkkaeEENKIKAEEAKKEAE 1740

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034590989 1113 klEEKQAAclEQIREMEKQGSLLSpQFQKEALAEYEARMKGLEAEVKESVR 1163
Cdd:PTZ00121  1741 --EDKKKA--EEAKKDEEEKKKIA-HLKKEEEKKAEEIRKEKEAVIEEELD 1786
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 992-1164 8.08e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 8.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  992 RVRELKDRLE----------LELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEMKKKLE 1061
Cdd:COG1196    214 RYRELKEELKeleaellllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1062 TKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAAcLEQIREMEKQgsllspqfQK 1141
Cdd:COG1196    294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE-LEEAEAELAE--------AE 364

                          170       180
                   ....*....|....*....|...
gi 1034590989 1142 EALAEYEARMKGLEAEVKESVRA 1164
Cdd:COG1196    365 EALLEAEAELAEAEEELEELAEE 387
PTZ00121 PTZ00121
MAEBL; Provisional
 891-1204 9.44e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 9.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  891 MKEAAEPRTAslEELRELKGVVKLQ--RRHEKELR-ELERRG--ARRWEELLQRGAAQLAELGPPGVGGVGACKLGPGKG 965
Cdd:PTZ00121  1121 KKKAEDARKA--EEARKAEDARKAEeaRKAEDAKRvEIARKAedARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAED 1198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  966 SRKKRSLPREESAGAAPgegpegvdgRVRELKDRLELELLRQGEE---QYECVLKRKEQHVAEQISKMMELAREKQAAEL 1042
Cdd:PTZ00121  1199 ARKAEAARKAEEERKAE---------EARKAEDAKKAEAVKKAEEakkDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ 1269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1043 KALKETSENDTKEMKKKLETKRLERIqgmtkvttdKMAQERLKREINNSHIQEvvqviKQMTENLERHQEKLEEKQAACL 1122
Cdd:PTZ00121  1270 AAIKAEEARKADELKKAEEKKKADEA---------KKAEEKKKADEAKKKAEE-----AKKADEAKKKAEEAKKKADAAK 1335

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1123 EQIREMEKQGSLlspqfqkeALAEYEARMKGLEAEVKESVRACLRTcfpSEAKDKPERACECPPELCEQDPLIAKADAQE 1202
Cdd:PTZ00121  1336 KKAEEAKKAAEA--------AKAEAEAAADEAEAAEEKAEAAEKKK---EEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404


                   ..
gi 1034590989 1203 SR 1204
Cdd:PTZ00121  1405 KK 1406
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 893-1205 1.14e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  893 EAAEPRTASLEElrELKGVVKLQRRHEKELRELERRgarrWEELLQRGAAQLAELGPPGVGGvgacklgpGKGSRKKRSL 972
Cdd:TIGR02168  687 EELEEKIAELEK--ALAELRKELEELEEELEQLRKE----LEELSRQISALRKDLARLEAEV--------EQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  973 PREESAGAAPGEGPEGVDGRVRELKDRLELELLRQgEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSEND 1052
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEEL-EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1053 TKEMKKKletkRLERIQGMTKVTTDKMA-----QERLKREINNSHIQ--EVVQVIKQMTENLERHQEKLEEKQaaclEQI 1125
Cdd:TIGR02168  832 RIAATER----RLEDLEEQIEELSEDIEslaaeIEELEELIEELESEleALLNERASLEEALALLRSELEELS----EEL 903

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1126 REMEKQGSLLSPQFQ--KEALAEYEARMKGLEAEVKEsvracLRTCFPSEAKDKPERACECPPELceqDPLIAKADAQES 1203
Cdd:TIGR02168  904 RELESKRSELRRELEelREKLAQLELRLEGLEVRIDN-----LQERLSEEYSLTLEEAEALENKI---EDDEEEARRRLK 975


                   ..
gi 1034590989 1204 RL 1205
Cdd:TIGR02168  976 RL 977
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 993-1161 1.51e-05

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: 49.58  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  993 VRELKDRLELELLRQGEEQYECVL--KRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEMKKKLETKRLERIQG 1070
Cdd:pfam02463  203 KEQAKKALEYYQLKEKLELEEEYLlyLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1071 MTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQGSLLSPQFQKEALAEYEAR 1150
Cdd:pfam02463  283 LQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE 362

                          170
                   ....*....|.
gi 1034590989 1151 MKGLEAEVKES 1161
Cdd:pfam02463  363 KLQEKLEQLEE 373
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 1021-1162 2.80e-05

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


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 46.10  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1021 QHVAEQISKMMELAREKQAAELKALKETSENDTKEMKKKLEtKRLERIQGMTKVTTDKMaQERLKREInnSHIQEVV-QV 1099
Cdd:pfam01442   25 QELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLG-QNVEELRQRLEPYTEEL-RKRLNADA--EELQEKLaPY 100

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034590989 1100 IKQMTENLERHQEKLEEKQAACLEQIRE-MEKQGSLLSpQFQKEALAEYEARMKGLEAEVKESV 1162
Cdd:pfam01442  101 GEELRERLEQNVDALRARLAPYAEELRQkLAERLEELK-ESLAPYAEEVQAQLSQRLQELREKL 163
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 903-1131 5.46e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.76  E-value: 5.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  903 EELRELKGVVklqRRHEKELRELERRGARR------WEELLQRGAAQLAELGPPGVGGVGACKLGPGKGSRKKRSLPREE 976
Cdd:TIGR02169  798 AELSKLEEEV---SRIEARLREIEQKLNRLtlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  977 SAGAAPGEGPEGVDGRVRELKDrlELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQA--AELKALKETSENDTK 1054
Cdd:TIGR02169  875 AALRDLESRLGDLKKERDELEA--QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEieDPKGEDEEIPEEELS 952

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034590989 1055 EMKKKLETKRLERiqgmtkvttDKMAQErlkrEINNSHIQEVVQVIKQMTEnLERHQEKLEEKQAACLEQIREMEKQ 1131
Cdd:TIGR02169  953 LEDVQAELQRVEE---------EIRALE----PVNMLAIQEYEEVLKRLDE-LKEKRAKLEEERKAILERIEEYEKK 1015
EFh_PI-PLCdelta4 cd16219
EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, ...
 211-299 1.08e-04

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


Pssm-ID: 320049 [Multi-domain]  Cd Length: 140  Bit Score: 43.68  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  211 FLMSLCPRPEIDEIFTSYHAKAKPyMTKEHLTKFINQKQRDsrlnsllfPPARPDQVQGLIDKYEPSGINAQRGQLSPEG 290
Cdd:cd16219     61 FYKALTQREDVLKIFQDFSADGQK-LTLLEFVDFLQQEQLE--------RENTEELAMELIDRYEPSDTAKKLHALSIDG 131


                   ....*....
gi 1034590989  291 MVWFLCGPE 299
Cdd:cd16219    132 FLMYLCSPE 140
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
892-1157 1.70e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  892 KEAAEPRTASLEELreLKGVVKLQRRHEKELRELERRgARRWEELlqRGAAQ----LAELGPPGVGGVGACKLGPGKGSR 967
Cdd:PRK03918   247 LESLEGSKRKLEEK--IRELEERIEELKKEIEELEEK-VKELKEL--KEKAEeyikLSEFYEEYLDELREIEKRLSRLEE 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  968 KKRSLPREESAGAAPGEGPEGVDGRVRELKDRLELelLRQGEEQYECVLKRKEQhvAEQISKMME-LAREKQAAELKALK 1046
Cdd:PRK03918   322 EINGIEERIKELEEKEERLEELKKKLKELEKRLEE--LEERHELYEEAKAKKEE--LERLKKRLTgLTPEKLEKELEELE 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1047 ETSENDTKEMKK------KLETKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAA 1120
Cdd:PRK03918   398 KAKEEIEEEISKitarigELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERK 477

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1034590989 1121 CLEQIREMEK---QGSLLSPQFQ-KEALAEYEARMKGLEAE 1157
Cdd:PRK03918   478 LRKELRELEKvlkKESELIKLKElAEQLKELEEKLKKYNLE 518
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 992-1120 1.84e-04

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 42.21  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  992 RVRELKDRLELEL-LRQGEEQyecvLKRKEQHVAEQISKMMELAREKQAAELkalkETSENDTKEMKKKLETKRLERIQG 1070
Cdd:pfam20492    1 REEAEREKQELEErLKQYEEE----TKKAQEELEESEETAEELEEERRQAEE----EAERLEQKRQEAEEEKERLEESAE 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1071 MTKVTTDKMAQERLKREinnSHIQEVVQVIKQMTENLERHQEKLEEKQAA 1120
Cdd:pfam20492   73 MEAEEKEQLEAELAEAQ---EEIARLEEEVERKEEEARRLQEELEEAREE 119
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 312-460 2.33e-04

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


Pssm-ID: 176500 [Multi-domain]  Cd Length: 271  Bit Score: 44.39  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  312 HDMTQPLNHYFINSSHNTY-LTAGQFSGLSSA-----EMY-RQVLLSGCRCVELDCWKgKPPDEEPIITHGFTMTTDIFF 384
Cdd:cd08557      3 LLDDLPLSQLSIPGTHNSYaYTIDGNSPIVSKwsktqDLSiTDQLDAGVRYLDLRVAY-DPDDGDLYVCHGLFLLNGQTL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  385 KEAIEAIAesAF-KTSPY-PIILSFENHV--DSPRQQAKMAEYCRTIFGDMLLTeplekfPLKPGVPLPSPEDLR-GKIL 459
Cdd:cd08557     82 EDVLNEVK--DFlDAHPSeVVILDLEHEYggDNGEDHDELDALLRDVLGDPLYR------PPVRAGGWPTLGELRaGKRV 153


                   .
gi 1034590989  460 I 460
Cdd:cd08557    154 L 154
PTZ00121 PTZ00121
MAEBL; Provisional
 892-1204 2.41e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 2.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  892 KEAAEPRTAslEELRELKGVVKLQ--RRHEKELRELErrgARRWEEllQRGAAQLAELGPPGVGGVGACKLGPGKGSRKK 969
Cdd:PTZ00121  1182 RKAEEVRKA--EELRKAEDARKAEaaRKAEEERKAEE---ARKAED--AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEI 1254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  970 RSLPREESAGAAPGEGPEgvdgrvrELKDRLELELLRQGEEqyecVLKRKEQHVAEQISKMMELARE----KQAAELKAL 1045
Cdd:PTZ00121  1255 RKFEEARMAHFARRQAAI-------KAEEARKADELKKAEE----KKKADEAKKAEEKKKADEAKKKaeeaKKADEAKKK 1323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1046 KETSENDTKEMKKKLE--TKRLERIQGMTKVTTDKMAQERLKREINNSHIQEV---VQVIKQMTENLERHQE---KLEE- 1116
Cdd:PTZ00121  1324 AEEAKKKADAAKKKAEeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkADAAKKKAEEKKKADEakkKAEEd 1403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1117 -KQAACLEQIREMEKQGSLLSPQFQKEALAEyEARMKGLEAEVKESVRAclrtcfPSEAKDKPERACECPPELCEQDPli 1195
Cdd:PTZ00121  1404 kKKADELKKAAAAKKKADEAKKKAEEKKKAD-EAKKKAEEAKKADEAKK------KAEEAKKAEEAKKKAEEAKKADE-- 1474


                   ....*....
gi 1034590989 1196 AKADAQESR 1204
Cdd:PTZ00121  1475 AKKKAEEAK 1483
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 1001-1156 3.20e-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: 43.50  E-value: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1001 ELELLRQGEEQYECVlkrkEQHVAEQISKMMELAREKQAAELKALKETSENDTK---------EMKKKLEtkrlERIQGM 1071
Cdd:pfam15665   48 ELDLKRRIQTLEESL----EQHERMKRQALTEFEQYKRRVEERELKAEAEHRQRvvelsreveEAKRAFE----EKLESF 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1072 TKVTTdKMAQERLK-----REINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIRE----MEKQgsllspqfQKE 1142
Cdd:pfam15665  120 EQLQA-QFEQEKRKaleelRAKHRQEIQELLTTQRAQSASSLAEQEKLEELHKAELESLRKevedLRKE--------KKK 190

                          170
                   ....*....|....
gi 1034590989 1143 ALAEYEARMKGLEA 1156
Cdd:pfam15665  191 LAEEYEQKLSKAQA 204
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 1010-1163 3.20e-04

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: 45.43  E-value: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1010 EQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEMKKK--LETKRLEriQGMTKVTTDKMaqeRLKRE 1087
Cdd:TIGR01612 1510 EKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKfiLEAEKSE--QKIKEIKKEKF---RIEDD 1584

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1088 I-NNSHIQEVVQVIKQMTENLERHQEK---LEEKQAACLEQIREMEKQGSLLSPQFQKEALAEYEARMKGLEaEVKESVR 1163
Cdd:TIGR01612 1585 AaKNDKSNKAAIDIQLSLENFENKFLKisdIKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNLNSLQ-EFLESLK 1663
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 903-1164 3.76e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 3.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  903 EELRELKGVVKLQRRHEKELR-ELERRGARRWEELLQRGAAQLAELgppgvggvgacklgpgkgsrkkrslpreesagaa 981
Cdd:COG1196    220 EELKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAEL---------------------------------- 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  982 pgegpegvDGRVRELK---DRLELELLRQGEEQYEcVLKRKEQHVAEQISkmmeLAREKQAAELKALKETSENDTKEMKK 1058
Cdd:COG1196    266 --------EAELEELRlelEELELELEEAQAEEYE-LLAELARLEQDIAR----LEERRRELEERLEELEEELAELEEEL 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1059 KLETKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQGSLLspQ 1138
Cdd:COG1196    333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE--E 410

                          250       260
                   ....*....|....*....|....*.
gi 1034590989 1139 FQKEALAEYEARMKGLEAEVKESVRA 1164
Cdd:COG1196    411 ALLERLERLEEELEELEEALAELEEE 436
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 989-1160 5.69e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.99  E-value: 5.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  989 VDGRVRELKDRLElELLRQgeeqyecvLKRKEQHVAEQISKMMELarEKQAAELKALKETSENDTKEMKKKLetKRLERI 1068
Cdd:COG1579     15 LDSELDRLEHRLK-ELPAE--------LAELEDELAALEARLEAA--KTELEDLEKEIKRLELEIEEVEARI--KKYEEQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1069 QGMtkVTTDKMAQ------ERLKREIN--NSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEkqgsllspqfq 1140
Cdd:COG1579     82 LGN--VRNNKEYEalqkeiESLKRRISdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD----------- 148

                          170       180
                   ....*....|....*....|
gi 1034590989 1141 kEALAEYEARMKGLEAEVKE 1160
Cdd:COG1579    149 -EELAELEAELEELEAEREE 167
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
994-1180 5.71e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 5.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  994 RELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQA------AELKALKE---TSENDTKEMKKKLE--T 1062
Cdd:COG4372      7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREeleqarEELEQLEEeleQARSELEQLEEELEelN 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1063 KRLERIQGMTKVTTDKMAQ-----ERLKREINNshIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQGSLLSP 1137
Cdd:COG4372     87 EQLQAAQAELAQAQEELESlqeeaEELQEELEE--LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1034590989 1138 QFQKEALAEYEARMKGLEAEVKESVRACLRTCFPSEAKDKPER 1180
Cdd:COG4372    165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 914-1156 6.04e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  914 LQRRHEKELRELERRGARRWEELLQRGAAQLAELGPPGVggvgacklgpgkgsrKKRSLPREESAGAAPGEGPEGVDGRV 993
Cdd:COG1196    544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI---------------RARAALAAALARGAIGAAVDLVASDL 608

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  994 RELK-----------------DRLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSENDTKEM 1056
Cdd:COG1196    609 READaryyvlgdtllgrtlvaARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1057 KKKLETKRLERIQGMTKVTTDKMAQERLKREINNshiqevvQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQGSLLS 1136
Cdd:COG1196    689 AEEELELEEALLAEEEEERELAEAEEERLEEELE-------EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761

                          250       260
                   ....*....|....*....|
gi 1034590989 1137 PQFQKEALAEYEARMKGLEA 1156
Cdd:COG1196    762 LEELERELERLEREIEALGP 781
PRK00106 PRK00106
ribonuclease Y;
992-1160 6.30e-04

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 43.70  E-value: 6.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  992 RVRELKDRLELELLRQgeEQYECVLKRKEQHVAEQISKMMElaREKQAAELKALKETSENDTK---EMKKKLETKRLERI 1068
Cdd:PRK00106    25 KMKSAKEAAELTLLNA--EQEAVNLRGKAERDAEHIKKTAK--RESKALKKELLLEAKEEARKyreEIEQEFKSERQELK 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1069 QGMTKVTTDKMAQERLKREINNSH--IQEVVQVIKQMTENL-ERHQE--KLEEKQAACLEQIREM---EKQGSLLSpQFQ 1140
Cdd:PRK00106   101 QIESRLTERATSLDRKDENLSSKEktLESKEQSLTDKSKHIdEREEQveKLEEQKKAELERVAALsqaEAREIILA-ETE 179

                          170       180
                   ....*....|....*....|
gi 1034590989 1141 KEALAEYEARMKGLEAEVKE 1160
Cdd:PRK00106   180 NKLTHEIATRIREAEREVKD 199
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 697-789 6.86e-04

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


Pssm-ID: 176060 [Multi-domain]  Cd Length: 126  Bit Score: 40.81  E-value: 6.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  697 LSITVISGQFLSER--SVRTYVEVELfglpGDPKRRYRTklSPSTNSINPVWkEEPFVFEkiLMPELASLRVAVMEEG-- 772
Cdd:cd08678      1 LLVKNIKANGLSEAagSSNPYCVLEM----DEPPQKYQS--STQKNTSNPFW-DEHFLFE--LSPNSKELLFEVYDNGkk 71

                           90
                   ....*....|....*....
gi 1034590989  773 --NKFLGHRIIPINALNSG 789
Cdd:cd08678     72 sdSKFLGLAIVPFDELRKN 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1033-1165 7.47e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 7.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1033 LAREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNSHIQevvqvikqmTENLERHQE 1112
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD---------LARLEAEVE 743

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034590989 1113 KLEEKQAACLEQIREMEKQGSLLSPQFQK--EALAEYEARMKGLEAEVKESVRAC 1165
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEaeEELAEAEAEIEELEAQIEQLKEEL 798
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 697-792 8.63e-04

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


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 40.64  E-value: 8.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  697 LSITVISGQFLSERSVR----TYVEVELFGlpgDPKRRYRTKLSPSTNSINPVWKEEpFVFEkilMP----ELASLRVAV 768
Cdd:cd00276     16 LTVVVLKARNLPPSDGKglsdPYVKVSLLQ---GGKKLKKKKTSVKKGTLNPVFNEA-FSFD---VPaeqlEEVSLVITV 88

                           90       100
                   ....*....|....*....|....*...
gi 1034590989  769 MEEG----NKFLGHRIIPINALNSGYHH 792
Cdd:cd00276     89 VDKDsvgrNEVIGQVVLGPDSGGEELEH 116
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
 202-295 8.73e-04

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


Pssm-ID: 320037 [Multi-domain]  Cd Length: 142  Bit Score: 41.08  E-value: 8.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  202 DFPEpvYKSFLMSLCPRPEIDEIFTSYHAKAKPYMTKEHLTKFINQKQRDSRlnsllfppaRPDQVQGLIDKYEPSGINA 281
Cdd:cd16207     56 NFEE--FQEFVKLLKRRKDIKAIFKQLTKPGSDGLTLEEFLKFLRDVQKEDV---------DRETWEKIFEKFARRIDDS 124

                           90
                   ....*....|....
gi 1034590989  282 QRGQLSPEGMVWFL 295
Cdd:cd16207    125 DSLTMTLEGFTSFL 138
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
 728-792 8.96e-04

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


Pssm-ID: 176064 [Multi-domain]  Cd Length: 126  Bit Score: 40.51  E-value: 8.96e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034590989  728 KRRYRTklSPSTNSINPVWKEE-PFVFEKILM--PELASLRVAVMEEGN----KFLGHRIIPINALNSGYHH 792
Cdd:cd08682     30 KEKYST--SVKEKTTSPVWKEEcSFELPGLLSgnGNRATLQLTVMHRNLlgldKFLGQVSIPLNDLDEDKGR 99
PRK12704 PRK12704
phosphodiesterase; Provisional
 1005-1160 9.50e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 9.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1005 LRQGEEQYECVLK--RKEqhvAEQISKMMEL-AREkqaaELKALKETSENDTKEMKKKLEtKRLERIQgmtkvttdkMAQ 1081
Cdd:PRK12704    33 IKEAEEEAKRILEeaKKE---AEAIKKEALLeAKE----EIHKLRNEFEKELRERRNELQ-KLEKRLL---------QKE 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1082 ERLKREINNshIQEVVQVIKQMTENLERHQEKLEEKQAAC----LEQIREMEKQGSLLSPQFQKEAL------AEYEA-- 1149
Cdd:PRK12704    96 ENLDRKLEL--LEKREEELEKKEKELEQKQQELEKKEEELeeliEEQLQELERISGLTAEEAKEILLekveeeARHEAav 173

                          170
                   ....*....|.
gi 1034590989 1150 RMKGLEAEVKE 1160
Cdd:PRK12704   174 LIKEIEEEAKE 184
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
892-1087 1.48e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  892 KEAAEPRTASLEELRELKGVVKLQRRHEKELRELERRgARRWEELLQRGAAQLAELGPPGVGGVGACKLGP--GKGSRKK 969
Cdd:COG4717     60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALE 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  970 RSLpreesagaapgegpEGVDGRVRELKDRLE-----LELLRQGEEQYEcVLKRKEQHVAEQISKMMELAREKQAAELKA 1044
Cdd:COG4717    139 AEL--------------AELPERLEELEERLEelrelEEELEELEAELA-ELQEELEELLEQLSLATEEELQDLAEELEE 203

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034590989 1045 L---KETSENDTKEMKKKLETKRlERIQGMTKVTTDKMAQERLKRE 1087
Cdd:COG4717    204 LqqrLAELEEELEEAQEELEELE-EELEQLENELEAAALEERLKEA 248
EFh_PRIP cd16206
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ...
 197-299 1.62e-03

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


Pssm-ID: 320036 [Multi-domain]  Cd Length: 143  Bit Score: 40.27  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  197 AINPEDFPEpVYKSflmsLCPRPEIDEIFTSYhAKAKPYMTKEHLTKFINQKQRDSRLNsllfpparPDQVQGLIDKYEP 276
Cdd:cd16206     55 RVSSDEFVE-LFKE----LATRPEIYFLLVRY-ASNKDYLTVDDLMLFLEAEQGMTGVT--------KEKCLEIINKYEP 120

                           90       100
                   ....*....|....*....|...
gi 1034590989  277 SGINAQRGQLSPEGMVWFLCGPE 299
Cdd:cd16206    121 SEEGREKGQLGIDGFTRYLLSEE 143
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 994-1151 1.64e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  994 RELKDRLELELLRQ--GEEQYECVLKRKEQHVAEQISKMMEL---AREKQAAELKALKETSENDTKEMKKKL--ETKRLE 1066
Cdd:pfam13868  195 KAQDEKAERDELRAklYQEEQERKERQKEREEAEKKARQRQElqqAREEQIELKERRLAEEAEREEEEFERMlrKQAEDE 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1067 RIqgmtkvttDKMAQERlKREINNSHIQEVVQVIKqmtenlERHQEKLEEKQAACLEQIREMEKQgsllspQFQKEALAE 1146
Cdd:pfam13868  275 EI--------EQEEAEK-RRMKRLEHRRELEKQIE------EREEQRAAEREEELEEGERLREEE------AERRERIEE 333


                   ....*
gi 1034590989 1147 YEARM 1151
Cdd:pfam13868  334 ERQKK 338
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1017-1160 2.92e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1017 KRKE-QHVAEQISKMMELAREKQAaELKALKETSEndtkEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINN--SHI 1093
Cdd:TIGR02168  675 RRREiEELEEKIEELEEKIAELEK-ALAELRKELE----ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleERI 749

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034590989 1094 QEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQGSLLspQFQKEALAEYEARMKGLEAEVKE 1160
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI--EQLKEELKALREALDELRAELTL 814
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 896-1181 3.68e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.70  E-value: 3.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  896 EPRTASLEELRELKGVVKLQ-RRHEKELRELERRGARRWEELlqrgAAQLAELGppgvggvgacklgpgkgsRKKRSLPR 974
Cdd:pfam01576  320 ELRSKREQEVTELKKALEEEtRSHEAQLQEMRQKHTQALEEL----TEQLEQAK------------------RNKANLEK 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  975 EESAgaapgegpegVDGRVRELKdrLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAELKALKETSENDT- 1053
Cdd:pfam01576  378 AKQA----------LESENAELQ--AELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESv 445

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1054 KEMKKKLETKRLERIQGMTKVT-----TDKMAQERLKREINNSHiqevvqVIKQMTENLERHQEKLEEKQaaclEQIREM 1128
Cdd:pfam01576  446 SSLLNEAEGKNIKLSKDVSSLEsqlqdTQELLQEETRQKLNLST------RLRQLEDERNSLQEQLEEEE----EAKRNV 515

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034590989 1129 EKQGSLLSPQFQ--KEALAEYEARMKGLEAEVK------ESVRACLRTcfPSEAKDKPERA 1181
Cdd:pfam01576  516 ERQLSTLQAQLSdmKKKLEEDAGTLEALEEGKKrlqrelEALTQQLEE--KAAAYDKLEKT 574
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 991-1205 4.20e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 4.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  991 GRVRELKDRLE-----LELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAA--ELKALKetSENDTKEMKKKLETK 1063
Cdd:TIGR02168  232 LRLEELREELEelqeeLKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELqkELYALA--NEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1064 RLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQ-----------------IR 1126
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesrleeleeqletlrskVA 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1127 EMEKQGSLLSPQFQkealaEYEARMKGLEAEVKEsvracLRTCFPSEAKDKPE-RACECPPELCEQDPLIAKADAQESRL 1205
Cdd:TIGR02168  390 QLELQIASLNNEIE-----RLEARLERLEDRRER-----LQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERL 459
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1007-1143 4.37e-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: 4.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1007 QGEEQYECVLKRKEqHVAEQIskmmelarekqaaeLKALKETSENDTKEMKKKLETKRLERIQGMTKVttDKMAQERLKR 1086
Cdd:cd16269    167 KAEEVLQEFLQSKE-AEAEAI--------------LQADQALTEKEKEIEAERAKAEAAEQERKLLEE--QQRELEQKLE 229

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034590989 1087 EINNSHIQEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQGsllspqFQKEA 1143
Cdd:cd16269    230 DQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALLEEG------FKEQA 280
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
900-1157 4.45e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 4.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  900 ASLEELRE------LKGVVKL-QRRHEKELReleRRGARRW------EELLQRGAAQLAELGPPGVGGVGACKlgpgKGS 966
Cdd:COG4913    565 DSPEELRRhpraitRAGQVKGnGTRHEKDDR---RRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLE----ALE 637

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  967 RKKRSLPREESAGAAPGEGPE------GVDGRVRELKDRLE--------LELLRQGEEQYECVLKRKEQHVAEQISKMME 1032
Cdd:COG4913    638 AELDALQERREALQRLAEYSWdeidvaSAEREIAELEAELErldassddLAALEEQLEELEAELEELEEELDELKGEIGR 717

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1033 LAREKQAA--ELKALKEtsendtkemkkkletkRLERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVIKQMTENLERH 1110
Cdd:COG4913    718 LEKELEQAeeELDELQD----------------RLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRAR 781

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1111 QEKLEEKQAACLEQIRE---MEKQGSLLSPqfqkEALAEYEARMKGLEAE 1157
Cdd:COG4913    782 LNRAEEELERAMRAFNRewpAETADLDADL----ESLPEYLALLDRLEED 827
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
891-1157 4.69e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  891 MKEAAEPRTASLEELRELKGVVKLQR----RHEKELRELERRGAR-------RWEELLQRGAAQLAELGPPGVGGVGACK 959
Cdd:COG4717    194 LQDLAEELEELQQRLAELEEELEEAQeeleELEEELEQLENELEAaaleerlKEARLLLLIAAALLALLGLGGSLLSLIL 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  960 LGPG--------------KGSRKKRSLPREESAGAAPGEGPEGVDGRVRELKDRLELELLRQGEEQYEcvLKRKEQHVAE 1025
Cdd:COG4717    274 TIAGvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLE--LLDRIEELQE 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1026 QISKMMELAREKQAAELKA-----LKETSENDTKEMKKKLETKRlERIQGMTKVTTDKMAQERLKREINNSHIQEVVQVI 1100
Cdd:COG4717    352 LLREAEELEEELQLEELEQeiaalLAEAGVEDEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDEEEL 430

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034590989 1101 KQMTENLERHQEKLEEKQAACLE-------QIREMEKQGSLLSpqfQKEALAEYEARMKGLEAE 1157
Cdd:COG4717    431 EEELEELEEELEELEEELEELREelaeleaELEQLEEDGELAE---LLQELEELKAELRELAEE 491
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1004-1130 5.20e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 5.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1004 LLRQGEeqYECVLKRKEQHVAEQISKMMELAREKQ-AAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQE 1082
Cdd:TIGR00618  148 LLPQGE--FAQFLKAKSKEKKELLMNLFPLDQYTQlALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLE 225

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034590989 1083 RLKReinnsHIQEVVQVIKQMTENLERHQEKLEEK---QAACLEQIREMEK 1130
Cdd:TIGR00618  226 KELK-----HLREALQQTQQSHAYLTQKREAQEEQlkkQQLLKQLRARIEE 271
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1016-1160 5.45e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 5.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1016 LKRKEQHVAEQISKMMELAREKQAAEL----KALKETSENDTKEMKKKLETKRLERIqgmtkvttdkMAQERLKREinns 1091
Cdd:pfam13868   34 IKAEEKEEERRLDEMMEEERERALEEEeekeEERKEERKRYRQELEEQIEEREQKRQ----------EEYEEKLQE---- 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034590989 1092 hIQEVVQVIKQMTENLERHQEKLEEKQAACLEQI----------REMEKQGSLLSPQFQKEALAEYEARMKGLEAEVKE 1160
Cdd:pfam13868  100 -REQMDEIVERIQEEDQAEAEEKLEKQRQLREEIdefneeqaewKELEKEEEREEDERILEYLKEKAEREEEREAEREE 177
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 697-771 5.79e-03

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


Pssm-ID: 176001 [Multi-domain]  Cd Length: 119  Bit Score: 38.01  E-value: 5.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  697 LSITVISGQFLSERSVRT----YVEVELfglPGDPKRRYRTKLSPstNSINPVWKEEpfvFEKILMPELAS-LRVAVMEE 771
Cdd:cd04036      2 LTVRVLRATNITKGDLLStpdcYVELWL---PTASDEKKRTKTIK--NSINPVWNET---FEFRIQSQVKNvLELTVMDE 73
PTZ00121 PTZ00121
MAEBL; Provisional
 891-1204 6.39e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 6.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  891 MKEAAEPRTASLEELR----ELKGVVKLQRRHE--KELRELERRG--ARRWEELLQRGA-AQLAELGPPGVGGVGACKLG 961
Cdd:PTZ00121  1396 AKKKAEEDKKKADELKkaaaAKKKADEAKKKAEekKKADEAKKKAeeAKKADEAKKKAEeAKKAEEAKKKAEEAKKADEA 1475

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  962 PGKGSRKKRSlpreESAGAAPGEGPEGVDGRVRELKDRLELELLRQGEEQYecvlKRKEQHVAEQISKMMELAREKQAAE 1041
Cdd:PTZ00121  1476 KKKAEEAKKA----DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK----KADEAKKAEEAKKADEAKKAEEKKK 1547

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1042 LKALKETSENDTKEMKKKLETKRLE---RIQGMTKVTTDKMAQERLKREINNSHIQEVV----QVIKQMTENLERHQEKL 1114
Cdd:PTZ00121  1548 ADELKKAEELKKAEEKKKAEEAKKAeedKNMALRKAEEAKKAEEARIEEVMKLYEEEKKmkaeEAKKAEEAKIKAEELKK 1627

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1115 EEKQAACLEQIREMEKQGSLLSPQFQKEAlAEYEARMKGLEAEVKESVRACLRTCFPSEAKDKPERACECPPELCEQDPL 1194
Cdd:PTZ00121  1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAE-EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706

                          330
                   ....*....|
gi 1034590989 1195 IAKADAQESR 1204
Cdd:PTZ00121  1707 LKKKEAEEKK 1716
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
892-1160 7.23e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 7.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  892 KEAAEPRTAsLEELRELKGVVKLQRR-----HEKELRELERRGARRWEELLQRGAAQLAELGPPGVGGVGACKlgpgkgs 966
Cdd:PRK03918   419 KEIKELKKA-IEELKKAKGKCPVCGRelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK------- 490

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  967 rKKRSLPREESagaapgegpegVDGRVRELKDRLE---LELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKqaaELK 1043
Cdd:PRK03918   491 -KESELIKLKE-----------LAEQLKELEEKLKkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE---ELK 555

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1044 ALKETSENDTKEMKKKLetKRLERIQGMTKVTTDKMAQERLK--REINNSHIQEV-----VQVIKQMTENLERHQEKLEE 1116
Cdd:PRK03918   556 KKLAELEKKLDELEEEL--AELLKELEELGFESVEELEERLKelEPFYNEYLELKdaekeLEREEKELKKLEEELDKAFE 633

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034590989 1117 KQAACLEQIREMEKQGSLLSPQFQKEALAEYEARM-------KGLEAEVKE 1160
Cdd:PRK03918   634 ELAETEKRLEELRKELEELEKKYSEEEYEELREEYlelsrelAGLRAELEE 684
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 997-1160 7.58e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 7.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  997 KDRLELELLRQgEEQYECVLKRKEQHVAEQISKMMEL-AREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVT 1075
Cdd:TIGR02168  332 LDELAEELAEL-EEKLEELKEELESLEAELEELEAELeELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1076 TDKMAQERLKREIN--------------NSHIQEVVQVIKQMTENLERHQEKLEEKQAAcLEQIREMEKQ--GSLLSPQF 1139
Cdd:TIGR02168  411 RLEDRRERLQQEIEellkkleeaelkelQAELEELEEELEELQEELERLEEALEELREE-LEEAEQALDAaeRELAQLQA 489

                          170       180
                   ....*....|....*....|.
gi 1034590989 1140 QKEALAEYEARMKGLEAEVKE 1160
Cdd:TIGR02168  490 RLDSLERLQENLEGFSEGVKA 510
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
983-1160 7.62e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 7.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  983 GEGPEGVDGRVRELkdRLELELLRQGEEQYECVLKRKEQhvaeqiskmmelaREKQAAELKALKETSENDTKEMKKKLET 1062
Cdd:COG4717     63 GRKPELNLKELKEL--EEELKEAEEKEEEYAELQEELEE-------------LEEELEELEAELEELREELEKLEKLLQL 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1063 KRLERiqgmtkvttdKMAQERLKREINNSHIQEVVQVIKQMtENLERHQEKLEEKQAACLEQIREMEKQGSLLSPQFQKE 1142
Cdd:COG4717    128 LPLYQ----------ELEALEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEELEELLEQLSLATEEELQD 196

                          170       180
                   ....*....|....*....|.
gi 1034590989 1143 ALAEYE---ARMKGLEAEVKE 1160
Cdd:COG4717    197 LAEELEelqQRLAELEEELEE 217
PRK12704 PRK12704
phosphodiesterase; Provisional
 1033-1160 8.79e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 8.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1033 LAREKQAAELKALKETSENDTKEMKKKLETKRLERI-QGMTKVTTDKMAQERLKREINNsHIQEVVQVIKQMTENLERHQ 1111
Cdd:PRK12704    24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALlEAKEEIHKLRNEFEKELRERRN-ELQKLEKRLLQKEENLDRKL 102

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1034590989 1112 EKLEEKQAACLEQIREMEKqgsllspqfQKEALAEYEARMKGLEAEVKE 1160
Cdd:PRK12704   103 ELLEKREEELEKKEKELEQ---------KQQELEKKEEELEELIEEQLQ 142
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
989-1159 9.19e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.04  E-value: 9.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989  989 VDGRVRELKDRLE--LELLRQGEEQYECVLKRKEQHVAEQISKMMELAREKQAAE----------LKALKETSENDTKEM 1056
Cdd:COG1842     10 IRANINALLDKAEdpEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEaeaekweekaRLALEKGREDLAREA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1057 kkkletkrLERIQGMTKvttdkmAQERLKREINN--SHIQEVVQVIKQMTENLERHQEKLE-----EKQAACLEQIREME 1129
Cdd:COG1842     90 --------LERKAELEA------QAEALEAQLAQleEQVEKLKEALRQLESKLEELKAKKDtlkarAKAAKAQEKVNEAL 155

                          170       180       190
                   ....*....|....*....|....*....|
gi 1034590989 1130 KQGSLLSPQfqkEALAEYEARMKGLEAEVK 1159
Cdd:COG1842    156 SGIDSDDAT---SALERMEEKIEEMEARAE 182
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 1007-1164 9.28e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.42  E-value: 9.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1007 QGEEQYECVLKRKEQHVAEQISkmmelAREKQAAELKALKETSENDTKEMKKKLE------TKRLERIQGMTKVTTDKMA 1080
Cdd:TIGR00606  206 QMELKYLKQYKEKACEIRDQIT-----SKEAQLESSREIVKSYENELDPLKNRLKeiehnlSKIMKLDNEIKALKSRKKQ 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1081 QERLKREINNSHI---QEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQGSLLSpqfQKEALAEYEARMKGLEAE 1157
Cdd:TIGR00606  281 MEKDNSELELKMEkvfQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLN---QEKTELLVEQGRLQLQAD 357


                   ....*...
gi 1034590989 1158 V-KESVRA 1164
Cdd:TIGR00606  358 RhQEHIRA 365
APP_E2 pfam12925
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ...
 1042-1191 9.82e-03

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


Pssm-ID: 463752  Cd Length: 190  Bit Score: 38.48  E-value: 9.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1042 LKALKETSENDT-KEMKKKLETKRLERiqgMTKVTTD-KMAQERLKrEINNSHIQEVVQVIKQMTENLERHQEKLEEKQA 1119
Cdd:pfam12925   14 FEHPDPRNEHESfKKAKKRLEEKHRER---MTKVMKEwEEAEERYQ-NLPKADPKAAEKFKKAMTARFQETVEALEEEAA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590989 1120 ACLEQIREMEKQGSL-LSPQFQKEALAEYearMKGLEAEVK--ESVRACLRTCFPSEAKDKP------ERACECPPELCE 1190
Cdd:pfam12925   90 AERQQLVETHQQRVEaHLNDRRRDALECY---LQALQENPPnpHRILKALKKLLRAEQKDRRhtlrhyRHLLASDPEKAE 166


                   .
gi 1034590989 1191 Q 1191
Cdd:pfam12925  167 Q 167
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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