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Conserved domains on  [gi|1243938431|ref|NP_001342084|]
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1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4 isoform c [Mus musculus]

Protein Classification

PLC family C2 domain-containing protein; PLC-beta family PH domain-containing protein( domain architecture ID 11598256)

PLC (phosphoinositide-specific phospholipase C) family C2 domain-containing protein similar to C2 domain region of PLCs that 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)| PLC-beta family PH (pleckstrin homology) domain-containing protein similar to PH region of phospholipase C-beta (PLC-beta) that is regulated by heterotrimeric G protein-coupled receptors

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
 312-680 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: 553.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08591      1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08591     81 IAETAFKTSEYPVILSFENHCSSKQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkgl 551
Cdd:cd08591        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQM 631
Cdd:cd08591    154 -------------------------LSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQL 208

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1243938431  632 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08591    209 SRIYPKGTRVDSSNYMPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN 257
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
 148-300 2.13e-102

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: 319.75  E-value: 2.13e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  148 KKHWMKLAFLTNTTGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFK 227
Cdd:cd16211      1 KKHWMRLCFLVNPNGKIPVRSITRTFASGKTEKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFK 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1243938431  228 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 300
Cdd:cd16211     81 KINGDKKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYLMSDE 153
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-143 9.89e-61

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: 203.19  E-value: 9.89e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431   17 LQEGAVFDRYEEESfVFEPNCLFKVDEFGFFLTWKSEGKEGQVLECSLINSIRQAAIPKDPKILAALE-AVGKSENDLEG 95
Cdd:cd13361      1 LLKGSKFDKWDEDS-SLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREvNVGGSDEDLED 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1243938431   96 RILCVCSGTDLVNIGFTYMVAENPEVTKQWVEGLRSIIHNFRANNVSP 143
Cdd:cd13361     80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 714-830 3.41e-42

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: 150.38  E-value: 3.41e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  714 TCSVQVISGQFLSD------KKIGTYVEVDMYGLPTDTiRKEFRTRMVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVY 787
Cdd:cd00275      3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADD-SAKFKTKVVKNNGFNPVWNET-FEF-DVTVPELAFLRFVVY 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1243938431  788 DDN---NKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNI 830
Cdd:cd00275     80 DEDsgdDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHI 125
DUF1154 pfam06631
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
 925-967 1.93e-17

Protein of unknown function (DUF1154); This family represents a small conserved region of unknown function within eukaryotic phospholipase C (EC:3.1.4.3). All members also contain pfam00387 and pfam00388.


:

Pssm-ID: 461969  Cd Length: 45  Bit Score: 76.91  E-value: 1.93e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1243938431  925 LIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQK 967
Cdd:pfam06631    3 KFPPITLESLRQDKAYLKLLKKQQKELESLKKKHSKERSAMQK 45
PTZ00121 super family cl31754
MAEBL; Provisional
 851-1182 2.00e-08

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 2.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  851 KKFLSITEKRADQMRAMGIETSDIADVP-SDTSKNDKKGKANPAKANVTPQSSSELRPTTTAALGSGQEAKKGIELipQV 929
Cdd:PTZ00121  1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA--KK 1398

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  930 RIEDLKQMKAYLKHLKKQQKELNSLKKKhAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGgsnclEIKKE 1009
Cdd:PTZ00121  1399 KAEEDKKKADELKKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE-----EAKKA 1472

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1010 TEIKIQTLTTDHKSKVKEIVAQHTKEWSEMINTHSAEEQ--EIRDLHLSQQCELLRKllinAHE-QQTQQLKLSHD-RES 1085
Cdd:PTZ00121  1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKK----AEEaKKADEAKKAEEkKKA 1548

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1086 KEMRAHQAKISMENSKAISQdksiKNKAERE-----RRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHL--EF 1158
Cdd:PTZ00121  1549 DELKKAEELKKAEEKKKAEE----AKKAEEDknmalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaEE 1624

                          330       340
                   ....*....|....*....|....
gi 1243938431 1159 LEKQNEQAKEMQQMVKLEAEMDRR 1182
Cdd:PTZ00121  1625 LKKAEEEKKKVEQLKKKEAEEKKK 1648
 
Name Accession Description Interval E-value
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
 312-680 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: 553.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08591      1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08591     81 IAETAFKTSEYPVILSFENHCSSKQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkgl 551
Cdd:cd08591        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQM 631
Cdd:cd08591    154 -------------------------LSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQL 208

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1243938431  632 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08591    209 SRIYPKGTRVDSSNYMPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN 257
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
 148-300 2.13e-102

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: 319.75  E-value: 2.13e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  148 KKHWMKLAFLTNTTGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFK 227
Cdd:cd16211      1 KKHWMRLCFLVNPNGKIPVRSITRTFASGKTEKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFK 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1243938431  228 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 300
Cdd:cd16211     81 KINGDKKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYLMSDE 153
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 315-462 2.15e-77

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


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 250.89  E-value: 2.15e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  315 MDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQAIKE 394
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWD--GPDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1243938431  395 TAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPlepgRPLPSPNDLKRKILIKN 462
Cdd:pfam00388   79 YAFVTSPYPVILSLENHCSPEQQKKMAEILKEIFGDMLYTPPLDDDL----TELPSPEDLKGKILIKG 142
PLN02228 PLN02228
Phosphoinositide phospholipase C
 218-819 3.02e-71

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 249.18  E-value: 3.02e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  218 PRTDIEDLFKKINGDktDYLTVDQLVSFLNEHQ--RDPRLNEILFPFYDAKRAmqiiEMYEPdeelkkKGLISSDGFCRY 295
Cdd:PLN02228    22 PPVSIKRLFEAYSRN--GKMSFDELLRFVSEVQgeRHAGLDYVQDIFHSVKHH----NVFHH------HGLVHLNAFYRY 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  296 LMSDENAPVFLDRlELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCW-DGKGEDQEpiIT 374
Cdd:PLN02228    90 LFSDTNSPLPMSG-QVHHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWpNPSGNAAE--VR 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  375 HGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEShplepGRPLPSPNDL 454
Cdd:PLN02228   167 HGRTLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHLPPNLQAQVAKMLTKTFRGMLFRCTSES-----TKHFPSPEEL 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  455 KRKILIKNKRLKPEVEKKQLEALKSMMEAGESAAPASiledDNEEEIESADQEEEAHP-EYKFGNELSAddyshkeavAN 533
Cdd:PLN02228   242 KNKILISTKPPKEYLESKTVQTTRTPTVKETSWKRVA----DAENKILEEYKDEESEAvGYRDLIAIHA---------AN 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  534 SVKKTSDDLEHENNKKGLVTVeDEQawmasykyvgattnihpYLSTMInyaqpvkfqgfhvaeernihynmssfnesvgl 613
Cdd:PLN02228   309 CKDPLKDCLSDDPEKPIRVSM-DEQ-----------------WLETMV-------------------------------- 338

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  614 gylKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFMR 693
Cdd:PLN02228   339 ---RTRGTDLVRFTQRNLVRIYPKGTRVDSSNYDPHVGWTHGAQMVAFNMQGHGKQLWIMQGMFRANGGCGYVKKPRILL 415

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  694 RPDRTFDPFSETPvdgvIAATCSVQVISGQ----------FLSDKKIGTYVEVDMYGLPTDTIrkEFRTRMVMNNGLnPV 763
Cdd:PLN02228   416 DEHTLFDPCKRLP----IKTTLKVKIYTGEgwdldfhlthFDQYSPPDFFVKIGIAGVPRDTV--SYRTETAVDQWF-PI 488

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  764 YNEESFVFrKVILPDLAVLRIAV--YDDN--NKLIGQRILPLDGLQAGYRHISLRNEGNK 819
Cdd:PLN02228   489 WGNDEFLF-QLRVPELALLWFKVqdYDNDtqNDFAGQTCLPLPELKSGVRAVRLHDRAGK 547
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 578-692 3.47e-66

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: 218.26  E-value: 3.47e-66
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431   578 STMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQ 657
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1243938431   658 MVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFM 692
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-143 9.89e-61

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: 203.19  E-value: 9.89e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431   17 LQEGAVFDRYEEESfVFEPNCLFKVDEFGFFLTWKSEGKEGQVLECSLINSIRQAAIPKDPKILAALE-AVGKSENDLEG 95
Cdd:cd13361      1 LLKGSKFDKWDEDS-SLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREvNVGGSDEDLED 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1243938431   96 RILCVCSGTDLVNIGFTYMVAENPEVTKQWVEGLRSIIHNFRANNVSP 143
Cdd:cd13361     80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-140 1.15e-57

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: 194.90  E-value: 1.15e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431   12 EVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWKSEGKEGQVLECSLINSIR---QAAIPKDPKILAALeAVGK 88
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPNVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRlgkFAKIPKDPKLREVL-SMGG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1243938431   89 SENDLEGRILCVCSGTDLVNIGFTYMVAENPEVTKQWVEGLRSIIHNFRANN 140
Cdd:pfam17787   80 SDNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 714-830 3.41e-42

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: 150.38  E-value: 3.41e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  714 TCSVQVISGQFLSD------KKIGTYVEVDMYGLPTDTiRKEFRTRMVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVY 787
Cdd:cd00275      3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADD-SAKFKTKVVKNNGFNPVWNET-FEF-DVTVPELAFLRFVVY 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1243938431  788 DDN---NKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNI 830
Cdd:cd00275     80 DEDsgdDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHI 125
DUF1154 pfam06631
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
 925-967 1.93e-17

Protein of unknown function (DUF1154); This family represents a small conserved region of unknown function within eukaryotic phospholipase C (EC:3.1.4.3). All members also contain pfam00387 and pfam00388.


Pssm-ID: 461969  Cd Length: 45  Bit Score: 76.91  E-value: 1.93e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1243938431  925 LIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQK 967
Cdd:pfam06631    3 KFPPITLESLRQDKAYLKLLKKQQKELESLKKKHSKERSAMQK 45
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 717-813 5.19e-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: 69.05  E-value: 5.19e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431   717 VQVISGQFLSDKKIGT----YVEVDMYGLPtdtiRKEFRTRMVMNNgLNPVYNEEsFVFrKVILPDLAVLRIAVYDDN-- 790
Cdd:smart00239    4 VKIISARNLPPKDKGGksdpYVKVSLDGDP----KEKKKTKVVKNT-LNPVWNET-FEF-EVPPPELAELEIEVYDKDrf 76

                            90       100
                    ....*....|....*....|....*
gi 1243938431   791 --NKLIGQRILPLDGLQAGYRHISL 813
Cdd:smart00239   77 grDDFIGQVTIPLSDLLLGGRHEKL 101
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 209-300 5.91e-14

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: 68.43  E-value: 5.91e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  209 FY-ELTQkicpRTDIEDLFKKINGDkTDYLTVDQLVSFLNEHQRDPRlneilfpfYDAKRAMQIIEMYEPDEELKKKGLI 287
Cdd:pfam09279    1 FYkMLTQ----REEIDEIFQEYSGD-GQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAM 67

                           90
                   ....*....|...
gi 1243938431  288 SSDGFCRYLMSDE 300
Cdd:pfam09279   68 TKDGFLMYLCSPD 80
C2 pfam00168
C2 domain;
716-810 2.17e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 55.79  E-value: 2.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  716 SVQVISGQFLSDKKIG----TYVEVDMYGLptdtiRKEFRTRmVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVYDDN- 790
Cdd:pfam00168    4 TVTVIEAKNLPPKDGNgtsdPYVKVYLLDG-----KQKKKTK-VVKNTLNPVWNET-FTF-SVPDPENAVLEIEVYDYDr 75

                           90       100
                   ....*....|....*....|...
gi 1243938431  791 ---NKLIGQRILPLDGLQAGYRH 810
Cdd:pfam00168   76 fgrDDFIGEVRIPLSELDSGEGL 98
PTZ00121 PTZ00121
MAEBL; Provisional
 851-1182 2.00e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 2.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  851 KKFLSITEKRADQMRAMGIETSDIADVP-SDTSKNDKKGKANPAKANVTPQSSSELRPTTTAALGSGQEAKKGIELipQV 929
Cdd:PTZ00121  1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA--KK 1398

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  930 RIEDLKQMKAYLKHLKKQQKELNSLKKKhAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGgsnclEIKKE 1009
Cdd:PTZ00121  1399 KAEEDKKKADELKKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE-----EAKKA 1472

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1010 TEIKIQTLTTDHKSKVKEIVAQHTKEWSEMINTHSAEEQ--EIRDLHLSQQCELLRKllinAHE-QQTQQLKLSHD-RES 1085
Cdd:PTZ00121  1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKK----AEEaKKADEAKKAEEkKKA 1548

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1086 KEMRAHQAKISMENSKAISQdksiKNKAERE-----RRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHL--EF 1158
Cdd:PTZ00121  1549 DELKKAEELKKAEEKKKAEE----AKKAEEDknmalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaEE 1624

                          330       340
                   ....*....|....*....|....
gi 1243938431 1159 LEKQNEQAKEMQQMVKLEAEMDRR 1182
Cdd:PTZ00121  1625 LKKAEEEKKKVEQLKKKEAEEKKK 1648
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 1047-1186 5.50e-07

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: 50.83  E-value: 5.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1047 EQEIRDLHLSQQCELLRKLLINAHEQQTQQLKLSHDRESKEMrahQAKISMENSKAISQ-DKSIKNKAERERRVRELNSS 1125
Cdd:pfam08703   25 EKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEM---KKKLERKRLESIQEaKKRTSDKAAQERLKKEINNS 101

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1243938431 1126 NTKKFLEERKRLAMKQSKEMDQLKKVQ---LEHLEFLEKQNEQakemQQMVKLEAEMDRRPATV 1186
Cdd:pfam08703  102 HIQEVVQSIKQLEEKQKRRQEKLEEKQaecLQQIKEEEPQLQA----ELNAEYEEKLKGLPAEV 161
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 992-1182 3.06e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 3.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  992 EKAMKKKggsnclEIKKETEIKIQTLTTDHKSKVKEIVAQHTKEWSEMINTHSAEEQEIRDLhlsqqcellrkllinahE 1071
Cdd:COG1196    210 EKAERYR------ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL-----------------E 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1072 QQTQQLKLSHDRESKEMRAHQAKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKV 1151
Cdd:COG1196    267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1243938431 1152 QLEHLEFLEKQNEQAKEMQQMVKLEAEMDRR 1182
Cdd:COG1196    347 EEAEEELEEAEAELAEAEEALLEAEAELAEA 377
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 921-1181 3.48e-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: 41.57  E-value: 3.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  921 KGIELIPQVRIEDLKQMKAYlkHLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKE----KSTHEKILEKAMK 996
Cdd:TIGR00606  186 KALETLRQVRQTQGQKVQEH--QMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENEldplKNRLKEIEHNLSK 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  997 KKGGSNCLEIKKETEIKIQTLTTDHKSKVKEIVAQHTKEWSEMINTHSAE----EQEIRDLH-----LSQQCELLR---- 1063
Cdd:TIGR00606  264 IMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTvrekERELVDCQrelekLNKERRLLNqekt 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1064 -------KLLINAHEQQTQQLKLSHDRESKEMRAHQAKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKfLEERKR 1136
Cdd:TIGR00606  344 ellveqgRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCAD-LQSKER 422

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1137 LAMKQSKEMDQLKK-----VQLEHLEFLEKQNEQAKEMQQMVKLEAEMDR 1181
Cdd:TIGR00606  423 LKQEQADEIRDEKKglgrtIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
 
Name Accession Description Interval E-value
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
 312-680 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: 553.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08591      1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08591     81 IAETAFKTSEYPVILSFENHCSSKQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkgl 551
Cdd:cd08591        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQM 631
Cdd:cd08591    154 -------------------------LSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQL 208

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1243938431  632 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08591    209 SRIYPKGTRVDSSNYMPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN 257
PI-PLCc_beta4 cd08626
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4; This subfamily ...
 312-680 6.44e-180

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: 527.80  E-value: 6.44e-180
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08626      1 YQDMDQPLAHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCIELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08626     81 IKDTAFVTSDYPVILSFENHCSKPQQYKLAKYCEEIFGDLLLTKPLESHPLEPGVPLPSPNKLKRKILIKNKR------- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkgl 551
Cdd:cd08626        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQM 631
Cdd:cd08626    154 -------------------------LSSLVNYAQPVKFQGFDVAEERNIHFNMSSFNESVGLGYLKTSAIEFVNYNKRQM 208

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1243938431  632 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08626    209 SRIYPKGTRVDSSNYMPQIFWNAGCQMVSLNFQTPDLGMQLNQGKFEYN 257
PI-PLCc_eukaryota cd08558
Catalytic domain of eukaryotic phosphoinositide-specific phospholipase C and similar proteins; ...
 312-680 3.54e-132

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: 401.83  E-value: 3.54e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08558      1 YQDMTQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDGP--DGEPVVYHGHTLTSKILFKDVIEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgrpLPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08558     79 IKEYAFVTSPYPVILSLENHCSLEQQKKMAQILKEIFGDKLLTPPLDENPVQ----LPSPEQLKGKILIKGKK------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkgl 551
Cdd:cd08558        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnihpylstminyaqpvkfqgfhvaeernihYNMSSFNESVGLGYLKTHAIEFVNYNKRQM 631
Cdd:cd08558    148 --------------------------------------------------YHMSSFSETKALKLLKESPEEFVKYNKRQL 177

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1243938431  632 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08558    178 SRVYPKGTRVDSSNYNPQPFWNAGCQMVALNYQTPDLPMQLNQGKFEQN 226
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 312-680 1.49e-115

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: 359.37  E-value: 1.49e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08624      1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  392 IKETAFVTSEYPVILSFENHC-SKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRLkpeve 470
Cdd:cd08624     81 IAESAFKTSPYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKKY----- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  471 kkqlealksmmeagesaapasileddnEEeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkg 550
Cdd:cd08624    156 ---------------------------EE--------------------------------------------------- 157

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  551 lvtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQ 630
Cdd:cd08624    158 --------------------------MSSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQ 211

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1243938431  631 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08624    212 MSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQTMDLPMQQNMALFEFN 261
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
 314-680 1.65e-112

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: 351.28  E-value: 1.65e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  314 EMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAIK 393
Cdd:cd08625      3 DMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEAIA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  394 ETAFVTSEYPVILSFENHC-SKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevekk 472
Cdd:cd08625     83 ESAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK-------- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  473 qlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkglv 552
Cdd:cd08625        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  553 tvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMS 632
Cdd:cd08625    155 ------------------------MSTLVNYIEPVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPMEFVEYNKKQLS 210

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1243938431  633 RIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08625    211 RIYPKGTRVDSSNYMPQLFWNVGCQMVALNFQTLDLAMQLNMGVFEYN 258
PI-PLCc_delta cd08593
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta; This subfamily ...
 312-680 4.07e-107

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: 336.62  E-value: 4.07e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08593      1 YQDMTQPLSHYFIASSHNTYLLEDQLKGPSSTEAYIRALKKGCRCVELDCWD--GPDGEPIIYHGHTLTSKILFKDVIQA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgrpLPSPNDLKRKILIKNKRLKpevek 471
Cdd:cd08593     79 IREYAFKVSPYPVILSLENHCSVEQQKVMAQHLKSILGDKLLTQPLDGVLTA----LPSPEELKGKILVKGKKLK----- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkgl 551
Cdd:cd08593        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQM 631
Cdd:cd08593    150 ---------------------LAKELSDLVIYCKSVHFKSFEHSKENYHFYEMSSFSESKALKLAQESGNEFVRHNKRQL 208

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1243938431  632 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08593    209 SRIYPAGLRTDSSNYDPQEMWNVGCQIVALNFQTPGEEMDLNDGLFRQN 257
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
 148-300 2.13e-102

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: 319.75  E-value: 2.13e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  148 KKHWMKLAFLTNTTGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFK 227
Cdd:cd16211      1 KKHWMRLCFLVNPNGKIPVRSITRTFASGKTEKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFK 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1243938431  228 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 300
Cdd:cd16211     81 KINGDKKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYLMSDE 153
PI-PLCc_beta1 cd08623
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1; This subfamily ...
 313-680 1.88e-97

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: 310.86  E-value: 1.88e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  313 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAI 392
Cdd:cd08623      2 EDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  393 KETAFVTSEYPVILSFENHC-SKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08623     82 AECAFKTSPFPILLSFENHVdSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKK------- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkgl 551
Cdd:cd08623        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQM 631
Cdd:cd08623    155 -------------------------MSNLVNYIQPVKFESFEASKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQL 209

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1243938431  632 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08623    210 SRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTVDLSMQINMGMYEYN 258
PI-PLCc_gamma cd08592
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma; This family ...
 313-680 3.83e-92

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: 295.10  E-value: 3.83e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  313 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGkgEDQEPIITHGKAMCTDILFKDVIQAI 392
Cdd:cd08592      2 QDMNNPLSHYWIASSHNTYLTGDQLSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPIIYHGHTLTSKIKFMDVLKTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  393 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQaleshPLEP-GRPLPSPNDLKRKILIKNKRLKpevek 471
Cdd:cd08592     80 KEHAFVTSEYPVILSIENHCSLPQQRNMAQAFKEVFGDMLLTQ-----PVDRnADQLPSPNQLKRKIIIKHKKLF----- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkgl 551
Cdd:cd08592        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnihpylstminyaqpvkfqgfhvaeernihYNMSSFNESVGLGYL-KTHAIEFVNYNKRQ 630
Cdd:cd08592    150 --------------------------------------------------YEMSSFPETKAEKYLnRQKGKIFLKYNRRQ 179

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1243938431  631 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08592    180 LSRVYPKGQRVDSSNYDPVPMWNCGSQMVALNFQTPDKPMQLNQALFMLN 229
PI-PLCc_PRIP_metazoa cd08597
Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein; This ...
 313-680 1.98e-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: 286.24  E-value: 1.98e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  313 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGkgEDQEPIITHGKAMCTDILFKDVIQAI 392
Cdd:cd08597      2 QDMTQPLSHYFIASSHNTYLIEDQLRGPSSVEGYVRALQRGCRCVELDCWDG--PNGEPVIYHGHTLTSKISFRSVIEAI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  393 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQAleshPLEPGRPLPSPNDLKRKILIKNKRLKpeveKK 472
Cdd:cd08597     80 NEYAFVASEYPLILCIENHCSEKQQLVMAQYLKEIFGDKLYTEP----PNEGESYLPSPHDLKGKIIIKGKKLK----RR 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  473 QLealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansVKKTSDdlehennkkgLV 552
Cdd:cd08597    152 KL------------------------------------------------------------CKELSD----------LV 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  553 TVedeqawmasykyvgattnihpylstminyAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMS 632
Cdd:cd08597    162 SL-----------------------------CKSVRFQDFPTSAQNQKYWEVCSFSENLARRLANEFPEDFVNYNKKFLS 212

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1243938431  633 RIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08597    213 RVYPSPMRVDSSNYNPQDFWNCGCQIVAMNYQTPGLMMDLNTGKFLEN 260
PI-PLC1c_yeast cd08598
Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This ...
 312-677 2.34e-85

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: 276.44  E-value: 2.34e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08598      1 EEDLSRPLNEYFISSSHNTYLLGRQLAGDSSVEGYIRALQRGCRCVEIDVWD--GDDGEPVVTHGYTLTSSVPFRDVCRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgrpLPSPNDLKRKILIKnkrlkpevek 471
Cdd:cd08598     79 IKKYAFVTSPYPLILSLEVHCDAEQQERMVEIMKETFGDLLVTEPLDGLEDE----LPSPEELRGKILIK---------- 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansVKKTSDDLEHennkkgl 551
Cdd:cd08598    145 ---------------------------------------------------------------VKKESKTPNH------- 154

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnihpylstminyaqpvkfqgfhvaeernihynMSSFNESVGLGYLKTHAIEFVNYNKRQM 631
Cdd:cd08598    155 ----------------------------------------------------IFSLSERSLLKLLKDKRAALDKHNRRHL 182

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1243938431  632 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKF 677
Cdd:cd08598    183 MRVYPSGTRISSSNFNPLPFWRAGVQMVALNWQTYDLGMQLNEAMF 228
PI-PLCc_delta3 cd08630
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily ...
 312-680 1.65e-82

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: 269.97  E-value: 1.65e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGedQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08630      1 FQDMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEGPG--GEPVIYHGHTLTSKILFRDVIQA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgrPLPSPNDLKRKILIKNKRLKpevek 471
Cdd:cd08630     79 VRQHAFTASPYPVILSLENHCGLEQQAAMARHLQTILGDMLVTQPLDSLNPE---ELPSPEELKGRVLVKGKKLQ----- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkgl 551
Cdd:cd08630        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQM 631
Cdd:cd08630    151 ---------------------ISPELSALAVYCQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFVRHNARQL 209

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1243938431  632 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08630    210 TRVYPLGLRMNSANYSPQEMWNSGCQLVALNFQTPGYEMDLNAGRFLVN 258
PI-PLCc_epsilon cd08596
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon; This family ...
 313-680 2.34e-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: 260.94  E-value: 2.34e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  313 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQAI 392
Cdd:cd08596      2 EDLQYPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLTGCRCVELDCWD--GDDGMPIIYHGHTLTTKIPFKDVVEAI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  393 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevekk 472
Cdd:cd08596     80 NRSAFITSDYPVILSIENHCSLQQQRKMAEIFKTVFGEKLVTKFLFESDFSDDPSLPSPLQLKNKILLKNKK-------- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  473 qlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkglv 552
Cdd:cd08596        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  553 tvedeqawmasykyvgattniHPYLSTMINYAQPVKFQGFHVAEerniHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMS 632
Cdd:cd08596    152 ---------------------APELSDLVIYCQAVKFPGLSTPK----CYHISSLNENAAKRLCRRYPQKLVQHTRCQLL 206

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1243938431  633 RIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08596    207 RTYPAATRIDSSNPNPLIFWLHGLQLVALNYQTDDLPMHLNAAMFEAN 254
PI-PLCc_delta1 cd08629
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily ...
 312-680 8.66e-78

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: 256.88  E-value: 8.66e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08629      1 YQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDGP--NQEPIIYHGYTFTSKILFCDVLRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgrpLPSPNDLKRKILIKNKRLKPEVEk 471
Cdd:cd08629     79 IRDYAFKASPYPVILSLENHCSLEQQRVMARHLRAILGPILLDQPLDGVTTS----LPSPEQLKGKILLKGKKLKLVPE- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkgl 551
Cdd:cd08629        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFH-VAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQ 630
Cdd:cd08629    154 -------------------------LSDMIIYCKSVHFGGFSsPGTSGQAFYEMASFSESRALRLLQESGNGFVRHNVSC 208

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1243938431  631 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08629    209 LSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDN 258
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 315-462 2.15e-77

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


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 250.89  E-value: 2.15e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  315 MDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQAIKE 394
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWD--GPDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1243938431  395 TAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPlepgRPLPSPNDLKRKILIKN 462
Cdd:pfam00388   79 YAFVTSPYPVILSLENHCSPEQQKKMAEILKEIFGDMLYTPPLDDDL----TELPSPEDLKGKILIKG 142
PI-PLCc_eta cd08594
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta; This family ...
 312-680 2.81e-77

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


Pssm-ID: 176536 [Multi-domain]  Cd Length: 227  Bit Score: 253.96  E-value: 2.81e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08594      1 NQDMTQPLSHYFIASSHNTYLTGDQLLSQSRVDMYARVLQAGCRCVEVDCWDGP--DGEPVVHHGYTLTSKILFRDVIET 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLlkqALESHPLEPGRPLPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08594     79 INKYAFIKNEYPVILSIENHCSVQQQKKMAQYLKEILGDKL---DLSSVISGDSKQLPSPQSLKGKILIKGKK------- 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkgl 551
Cdd:cd08594        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnihpylstminyaqpvkfqgfhvaeernihYNMSSFNESVGLGYLKTHAIEFVNYNKRQM 631
Cdd:cd08594    149 --------------------------------------------------WQVSSFSETRAHQIVQQKAAQFLRFNQRQL 178

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1243938431  632 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08594    179 SRIYPSAYRIDSSNFNPQPYWNAGCQLVALNYQTEGRMLQLNRAKFRAN 227
PI-PLCc_delta4 cd08631
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4; This subfamily ...
 312-680 2.21e-76

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: 252.95  E-value: 2.21e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08631      1 YQDMTQPLCHYFICSSHNTYLMEDQLRGQSSVEGYIRALKRGCRCVEVDVWDGP--NGEPIVYHGHTFTSKILFKDVVAA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEShpLEPGRpLPSPNDLKRKILIKNKRLKpevek 471
Cdd:cd08631     79 VAQYAFQVSDYPVILSLENHCGVEQQQTMAQHLTEILGEKLLSTTLDG--VLPTQ-LPSPEELRGKILLKGKKIR----- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkgl 551
Cdd:cd08631        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQM 631
Cdd:cd08631    151 ---------------------LSPELSDCVIYCKSVSFRSFTHSREHYHFYEISSFTETKARKLIREAGNEFVQHNTWQL 209

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1243938431  632 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08631    210 SRVYPSGLRTDSSNYNPQEMWNAGCQMVALNFQTAGLEMDLNDGLFRQN 258
PI-PLCc_zeta cd08595
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta; This family ...
 312-680 3.37e-76

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: 252.16  E-value: 3.37e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08595      1 YQDMDHPLSDYFISSSHNTYLVSDQLVGPSDLDGYVSALRKGCRCLEIDCWDGA--DNEPVVYHGYTLTSKILFKEVITT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEsHPlePGRPLPSPNDLKRKILIKNKRlkpevek 471
Cdd:cd08595     79 VEKYAFEKSDYPVVLSLENHCSTEQQEIMAHYLVSILGEKLLRAPID-DP--ATGELPSPEALKFKILVKNKK------- 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshKEAVAnsvkktsddlehennkkgl 551
Cdd:cd08595    149 --------------------------------------------------------KIAKA------------------- 153

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnihpyLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQM 631
Cdd:cd08595    154 -------------------------LSDLVIYTKSEKFCSFTHSRDNQHSYENNSIGENKARKLLKSSGADFVGHTQRFI 208

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1243938431  632 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08595    209 TRIYPKGTRASSSNYNPQEFWNVGCQMVALNFQTLGAPMDLQNGKFLDN 257
PI-PLCc_eta2 cd08633
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily ...
 313-680 5.52e-75

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: 248.80  E-value: 5.52e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  313 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQAI 392
Cdd:cd08633      2 QDMTQPLSHYFITSSHNTYLSGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDGP--DGEPIVHHGYTLTSKILFKDVIETI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  393 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDlllKQALESHPLEPGRPLPSPNDLKRKILIKNKRLkpevekk 472
Cdd:cd08633     80 NKYAFIKNEYPVILSIENHCSVPQQKKMAQYLTEILGD---KLDLSSVISNDCTRLPSPEILKGKILVKGKKL------- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  473 qlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshKEAVANSVKKTSDDLEHEnnkkglV 552
Cdd:cd08633    150 -------------------------------------------------------SRALSDLVKYTKSVRVHD------I 168

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  553 TVEDEQAWmasykyvgattnihpylstminyaqpvkfqgfhvaeernihyNMSSFNESVGLGYLKTHAIEFVNYNKRQMS 632
Cdd:cd08633    169 ETEATSSW------------------------------------------QVSSFSETKAHQILQQKPAQYLRFNQRQLS 206

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1243938431  633 RIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08633    207 RIYPSSYRVDSSNYNPQPFWNAGCQMVALNYQSEGRMLQLNRAKFSAN 254
PI-PLCc_eta1 cd08632
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily ...
 312-680 7.37e-72

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: 239.93  E-value: 7.37e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQA 391
Cdd:cd08632      1 NQDMDQPLCNYFIASSHNTYLTGDQLLSQSKVDMYARVLQAGCRCVEVDCWDGP--DGEPVVHHGYTLTSKITFRDVIET 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLL-LKQALESHPlepgRPLPSPNDLKRKILIKNKRLkpeve 470
Cdd:cd08632     79 INKYAFVKNEFPVILSIENHCSIQQQKKIAQYLKEIFGDKLdLSSVLTGDP----KQLPSPQLLKGKILVKGKKL----- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  471 kkqLEALKSMMEAGESAAPASILEDdneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkg 550
Cdd:cd08632    150 ---CRDLSDLVVYTNSVAAQDIVDD------------------------------------------------------- 171

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  551 lvtvedeqawmasykyvGATTNIhpylstminyaqpvkfqgfhvaeernihynmSSFNESVGLGYLKTHAIEFVNYNKRQ 630
Cdd:cd08632    172 -----------------GSTGNV-------------------------------LSFSETRAHQLVQQKAEQFMTYNQKQ 203

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1243938431  631 MSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08632    204 LTRIYPSAYRIDSSNFNPLPYWNVGCQLVALNYQSEGRMMQLNRAKFMVN 253
PLN02228 PLN02228
Phosphoinositide phospholipase C
 218-819 3.02e-71

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 249.18  E-value: 3.02e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  218 PRTDIEDLFKKINGDktDYLTVDQLVSFLNEHQ--RDPRLNEILFPFYDAKRAmqiiEMYEPdeelkkKGLISSDGFCRY 295
Cdd:PLN02228    22 PPVSIKRLFEAYSRN--GKMSFDELLRFVSEVQgeRHAGLDYVQDIFHSVKHH----NVFHH------HGLVHLNAFYRY 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  296 LMSDENAPVFLDRlELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCW-DGKGEDQEpiIT 374
Cdd:PLN02228    90 LFSDTNSPLPMSG-QVHHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWpNPSGNAAE--VR 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  375 HGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEShplepGRPLPSPNDL 454
Cdd:PLN02228   167 HGRTLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHLPPNLQAQVAKMLTKTFRGMLFRCTSES-----TKHFPSPEEL 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  455 KRKILIKNKRLKPEVEKKQLEALKSMMEAGESAAPASiledDNEEEIESADQEEEAHP-EYKFGNELSAddyshkeavAN 533
Cdd:PLN02228   242 KNKILISTKPPKEYLESKTVQTTRTPTVKETSWKRVA----DAENKILEEYKDEESEAvGYRDLIAIHA---------AN 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  534 SVKKTSDDLEHENNKKGLVTVeDEQawmasykyvgattnihpYLSTMInyaqpvkfqgfhvaeernihynmssfnesvgl 613
Cdd:PLN02228   309 CKDPLKDCLSDDPEKPIRVSM-DEQ-----------------WLETMV-------------------------------- 338

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  614 gylKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFMR 693
Cdd:PLN02228   339 ---RTRGTDLVRFTQRNLVRIYPKGTRVDSSNYDPHVGWTHGAQMVAFNMQGHGKQLWIMQGMFRANGGCGYVKKPRILL 415

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  694 RPDRTFDPFSETPvdgvIAATCSVQVISGQ----------FLSDKKIGTYVEVDMYGLPTDTIrkEFRTRMVMNNGLnPV 763
Cdd:PLN02228   416 DEHTLFDPCKRLP----IKTTLKVKIYTGEgwdldfhlthFDQYSPPDFFVKIGIAGVPRDTV--SYRTETAVDQWF-PI 488

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  764 YNEESFVFrKVILPDLAVLRIAV--YDDN--NKLIGQRILPLDGLQAGYRHISLRNEGNK 819
Cdd:PLN02228   489 WGNDEFLF-QLRVPELALLWFKVqdYDNDtqNDFAGQTCLPLPELKSGVRAVRLHDRAGK 547
PI-PLCc_gamma1 cd08627
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily ...
 313-680 7.81e-71

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: 236.08  E-value: 7.81e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  313 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQAI 392
Cdd:cd08627      2 EEMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGP--DGMPVIYHGHTLTTKIKFSDVLHTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  393 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEpgrpLPSPNDLKRKILIKNKRLkpevekk 472
Cdd:cd08627     80 KEHAFVTSEYPIILSIEDHCSIVQQRNMAQHFKKVFGDMLLTKPVDINADG----LPSPNQLKRKILIKHKKL------- 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  473 qlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddlehennkkglv 552
Cdd:cd08627        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  553 tvedeqawmasykyvgattnihpylstminyaqpvkfqgfhvaeerniHYNMSSFNESVGLGYL-KTHAIEFVNYNKRQM 631
Cdd:cd08627    149 ------------------------------------------------YRDMSSFPETKAEKYVnRSKGKKFLQYNRRQL 180

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1243938431  632 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08627    181 SRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMLG 229
EFh_NorpA_like cd16212
EF-hand motif found in Drosophila melanogaster No receptor potential A protein (NorpA) and ...
 148-300 1.00e-70

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: 232.82  E-value: 1.00e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  148 KKHWMKLAFLTNTTGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFK 227
Cdd:cd16212      1 KKHWMRLGFMVDSGGKIPVKHIARTFASGKTEKLVYQCLAEMGLPSGKGDSIEKEDFTFEKFYALYHKICPRNDIEELFT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1243938431  228 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 300
Cdd:cd16212     81 SITKGKGEHISLAQLINFMNDKQRDPRLNEILYPLYDEKRCTEIIKAYEQNEENIKNKRMSKDGFIRYLMSDE 153
EFh_PI-PLCbeta cd16200
EF-hand motif found in metazoan phosphoinositide-specific phospholipase C (PI-PLC)-beta ...
 148-300 2.17e-70

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: 231.75  E-value: 2.17e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  148 KKHWMKLAFLTNTTGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFK 227
Cdd:cd16200      1 KKLYTKLKLSVNITGKIPVKNIIKCFSSDKKRKRVLKALKALGLPDGKNDEIDPEDFTFEKFFKLYNKLCPRPDIDEIFK 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1243938431  228 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 300
Cdd:cd16200     81 ELGGKRKPYLTLEQLVDFLNEEQRDPRLNEILFPFHTKEQAKKLIDKYEPNEKNKKKGQLTLEGFLRYLMSDE 153
PI-PLCc_gamma2 cd08628
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2; This subfamily ...
 313-680 3.19e-69

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: 232.64  E-value: 3.19e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  313 QEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMCTDILFKDVIQAI 392
Cdd:cd08628      2 QDMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRMGCRCIELDCWDGP--DGKPIIYHGWTRTTKIKFDDVVQAI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  393 KETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQaleshPLEP-GRPLPSPNDLKRKILIKNKRLKPevek 471
Cdd:cd08628     80 KDHAFVTSEYPVILSIEEHCSVEQQRHMAKVFKEVFGDKLLMK-----PLEAsADQLPSPTQLKEKIIIKHKKLIA---- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeIESADQEEEAHPEykfgnelsaddyshkeavansvKKTSDDLEHENNKKgl 551
Cdd:cd08628    151 -----------------------------IELSDLVVYCKPT----------------------SKTKDNLENPDFKE-- 177

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnihpylstminyaqpvkfqgfhvaeernihynMSSFNESVGLGYLKTHAIEFVNYNKRQM 631
Cdd:cd08628    178 ----------------------------------------------------IRSFVETKAPSIIRQKPVQLLKYNRKGL 205

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1243938431  632 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08628    206 TRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTADKYMQLNHALFSLN 254
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 578-692 3.47e-66

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: 218.26  E-value: 3.47e-66
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431   578 STMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQ 657
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1243938431   658 MVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFM 692
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
PLN02952 PLN02952
phosphoinositide phospholipase C
 200-821 2.98e-63

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 226.80  E-value: 2.98e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  200 EPAAFTYEKFYELTQK-----ICPRTDIEDLFKKINgDKTDYLTVDQLVSFLNEHQrdprlNEILFPFYDAKRAM-QIIE 273
Cdd:PLN02952    13 DSGSYNYKMFNLFNRKfkiteAEPPDDVKDVFCKFS-VGGGHMGADQLRRFLVLHQ-----DELDCTLAEAQRIVeEVIN 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  274 MYEPDEELKKKGLISSDGFCRYLMSDENAPVFLdrlELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAG 353
Cdd:PLN02952    87 RRHHVTRYTRHGLNLDDFFHFLLYDDLNGPITP---QVHHDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRG 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  354 CRCVELDCWDGKGEDqEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLL 433
Cdd:PLN02952   164 VRVIELDLWPGSTKD-EILVLHGRTLTTPVPLIKCLKSIRDYAFSSSPYPVIITLEDHLTPDLQAKVAEMATQIFGQMLY 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  434 KQalESHPLepgRPLPSPNDLKRKILIKNKRLKpevekkqlealksmmEAGESAAPASILEDDNEEE--IESADQEEEAH 511
Cdd:PLN02952   243 YP--ESDSL---VQFPSPESLKHRIIISTKPPK---------------EYLESSGPIVIKKKNNVSPsgRNSSEETEEAQ 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  512 PEYKFGNELSADDYShkeavansvkktsdDLEHENNKKGlvtvedeQAWMASYKYVgattnihpylsTMINYAQP---VK 588
Cdd:PLN02952   303 TLESMLFEQEADSRS--------------DSDQDDNKSG-------ELQKPAYKRL-----------ITIHAGKPkgtLK 350

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  589 fQGFHVAEERnihYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDL 668
Cdd:PLN02952   351 -DAMKVAVDK---VRRLSLSEQELEKAATTNGQDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGAQMIAFNMQGYGK 426

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  669 AMQLNQGKFEYNGSCGYLLKPDFMRRP---DRTFDPFSETPVdgviAATCSVQVISG----------QFLSDKKIGTYVE 735
Cdd:PLN02952   427 SLWLMHGMFRANGGCGYLKKPDFLMKKgfhDEVFDPKKKLPV----KKTLKVKVYLGdgwrldfshtHFDSYSPPDFYTK 502

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  736 VDMYGLPTDTIRKefRTRMVMNNgLNPVYNEEsFVFrKVILPDLAVLRIAV--YD--DNNKLIGQRILPLDGLQAGYRHI 811
Cdd:PLN02952   503 MYIVGVPADNAKK--KTKIIEDN-WYPAWNEE-FSF-PLTVPELALLRIEVreYDmsEKDDFGGQTCLPVSELRPGIRSV 577

                          650
                   ....*....|
gi 1243938431  812 SLRNEGNKPL 821
Cdd:PLN02952   578 PLHDKKGEKL 587
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 315-463 3.59e-63

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: 210.99  E-value: 3.59e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431   315 MDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgkGEDQEPIITHGKAMCTDILFKDVIQAIKE 394
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWD--GPDGEPVIYHGHTFTLPIKLSEVLEAIKD 78

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1243938431   395 TAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLepgrPLPSPNDLKRKILIKNK 463
Cdd:smart00148   79 FAFVTSPYPVILSLENHCSPDQQAKMAQMFKEIFGDMLYTPPLTSSLE----VLPSPEQLRGKILLKVR 143
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 312-680 5.40e-63

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: 215.59  E-value: 5.40e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQF-----GGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHGKAMcTDILFK 386
Cdd:cd00137      1 HHPDTQPLAHYSIPGTHDTYLTAGQFtikqvWGLTQTEMYRQQLLSGCRCVDIRCWDGK--PEEPIIYHGPTF-LDIFLK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  387 DVIQAIKETAFVTSEYPVILSFENHCSKY--QQYKMSKYCEDLFGDLLLkqaleSHPLEPGRPLPSPNDLKRKILIKNKr 464
Cdd:cd00137     78 EVIEAIAQFLKKNPPETIIMSLKNEVDSMdsFQAKMAEYCRTIFGDMLL-----TPPLKPTVPLPSLEDLRGKILLLNK- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  465 lkpevekkqlealksmmeagesaapasileddneeeiesadqeeeahpeykfgnelsaddyshkeavansvkktsddleh 544
Cdd:cd00137        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  545 eNNKKGLVTVEDEQAWMASYKYvgattnihpylSTMINYAqpvkfqgfhvaeernihYNMSSFNESVGLGYLKTHAIE-- 622
Cdd:cd00137    152 -KNGFSGPTGSSNDTGFVSFEF-----------STQKNRS-----------------YNISSQDEYKAYDDEKVKLIKat 202

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1243938431  623 --FVNYNKRQMSRIYPKGGRV---------DSSNYMPQIFWN---AGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd00137    203 vqFVDYNKNQLSRNYPSGTSGgtawyyyamDSNNYMPQMFWNanpAGCGIVILDFQTMDLPMQQYMAVIEFN 274
PLN02222 PLN02222
phosphoinositide phospholipase C 2
 204-816 1.83e-62

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 224.14  E-value: 1.83e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  204 FTYEKFYELTQKICPRtDIEDLFKKINgdKTDYLTVDQLVSFLNEHQRDPRLNEilfpfydaKRAMQIIEmyEPDEELKK 283
Cdd:PLN02222    10 FCFRRRFRYTASEAPR-EIKTIFEKYS--ENGVMTVDHLHRFLIDVQKQDKATR--------EDAQSIIN--SASSLLHR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  284 KGLiSSDGFCRYLMSDENAPVFLDrlELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWD 363
Cdd:PLN02222    77 NGL-HLDAFFKYLFGDNNPPLALH--EVHHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWP 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  364 GKGEDQEPIItHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALEshplE 443
Cdd:PLN02222   154 NSDKDDIDVL-HGMTLTTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHLTPDLQSKVAEMVTEIFGEILFTPPVG----E 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  444 PGRPLPSPNDLKRKILIKNKRLKPEVEKKQLEALKSMMEAGesaapasileddnEEEIesadqeeeahpeykFGNELSAD 523
Cdd:PLN02222   229 SLKEFPSPNSLKKRIIISTKPPKEYKEGKDDEVVQKGKDLG-------------DEEV--------------WGREVPSF 281

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  524 DYSHKEAVANSVKKTSDDLEHENNKKGLVTVEDEqawmasYKYVGATTNIHPYLS-TMINYAQPVKFQGFHVAEERnihy 602
Cdd:PLN02222   282 IQRNKSVDKNDSNGDDDDDDDDGEDKSKKNAPPQ------YKHLIAIHAGKPKGGiTECLKVDPDKVRRLSLSEEQ---- 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  603 nMSSFNESvglgylktHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGS 682
Cdd:PLN02222   352 -LEKAAEK--------YAKQIVRFTQHNLLRIYPKGTRVTSSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGG 422

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  683 CGYLLKPDFMRRPD---RTFDPFSETPVDgviaATCSVQVISGQ----------FLSDKKIGTYVEVDMYGLPTDTIRKe 749
Cdd:PLN02222   423 CGYIKKPDLLLKSGsdsDIFDPKATLPVK----TTLRVTIYMGEgwyfdfrhthFDQYSPPDFYTRVGIAGVPGDTVMK- 497

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1243938431  750 fRTRMVMNNGLnPVYnEESFVFrKVILPDLAVLRIAV--YDDNNK--LIGQRILPLDGLQAGYRHISLRNE 816
Cdd:PLN02222   498 -KTKTLEDNWI-PAW-DEVFEF-PLTVPELALLRLEVheYDMSEKddFGGQTCLPVWELSQGIRAFPLHSR 564
PI-PLC-Y pfam00387
Phosphatidylinositol-specific phospholipase C, Y domain; This associates with pfam00388 to ...
 577-691 8.03e-62

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


Pssm-ID: 459794  Cd Length: 114  Bit Score: 205.77  E-value: 8.03e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  577 LSTMINYAQPVKFQGFHvAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGC 656
Cdd:pfam00387    1 LSDLVVYTQSVKFKSFS-TPESKTPNHIFSFSESKALKLIKSSSAAFVKHNRRHLMRVYPKGTRVDSSNFNPQPFWNCGV 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1243938431  657 QMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDF 691
Cdd:pfam00387   80 QMVALNWQTPDEGMQLNEGMFADNGGCGYVLKPEF 114
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-143 9.89e-61

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: 203.19  E-value: 9.89e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431   17 LQEGAVFDRYEEESfVFEPNCLFKVDEFGFFLTWKSEGKEGQVLECSLINSIRQAAIPKDPKILAALE-AVGKSENDLEG 95
Cdd:cd13361      1 LLKGSKFDKWDEDS-SLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREvNVGGSDEDLED 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1243938431   96 RILCVCSGTDLVNIGFTYMVAENPEVTKQWVEGLRSIIHNFRANNVSP 143
Cdd:cd13361     80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-140 1.15e-57

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: 194.90  E-value: 1.15e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431   12 EVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWKSEGKEGQVLECSLINSIR---QAAIPKDPKILAALeAVGK 88
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPNVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRlgkFAKIPKDPKLREVL-SMGG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1243938431   89 SENDLEGRILCVCSGTDLVNIGFTYMVAENPEVTKQWVEGLRSIIHNFRANN 140
Cdd:pfam17787   80 SDNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
PLN02230 PLN02230
phosphoinositide phospholipase C 4
 218-815 1.70e-54

phosphoinositide phospholipase C 4


Pssm-ID: 177875 [Multi-domain]  Cd Length: 598  Bit Score: 201.09  E-value: 1.70e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  218 PRTDIEDLFKKInGDKTDYLTVDQLVSFLNEHQRDPRLNEIlfpfydaKRAMQIIemyepDEELKKKGLISS-------- 289
Cdd:PLN02230    27 PVADVRDLFEKY-ADGDAHMSPEQLQKLMAEEGGGEGETSL-------EEAERIV-----DEVLRRKHHIAKftrrnltl 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  290 DGFCRYLMSDENAPVFLDrlELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDgKGEDq 369
Cdd:PLN02230    94 DDFNYYLFSTDLNPPIAD--QVHQNMDAPLSHYFIFTGHNSYLTGNQLSSNCSELPIADALRRGVRVVELDLWP-RGTD- 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  370 EPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLkqaleSHPLEPGRPLP 449
Cdd:PLN02230   170 DVCVKHGRTLTKEVKLGKCLDSIKANAFAISKYPVIITLEDHLTPKLQFKVAKMITQTFGDMLY-----YHDSEGCQEFP 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  450 SPNDLKRKILIKNKrlkpevekkqlealksmmeagesaAPASILEDDNEEEIESADQEEEAHpEYKFGNElsADDYSHKE 529
Cdd:PLN02230   245 SPEELKEKILISTK------------------------PPKEYLEANDAKEKDNGEKGKDSD-EDVWGKE--PEDLISTQ 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  530 AVANSVKKTSDDLEHENNKKGLVTVEDE-QAWMASYKYVGATTNIHPYLS-TMINYAQPVKFQGFHVAEERnIHYNMSSF 607
Cdd:PLN02230   298 SDLDKVTSSVNDLNQDDEERGSCESDTScQLQAPEYKRLIAIHAGKPKGGlRMALKVDPNKIRRLSLSEQL-LEKAVASY 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  608 NESVglgylkthaiefVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLL 687
Cdd:PLN02230   377 GADV------------IRFTQKNFLRIYPKGTRFNSSNYKPQIGWMSGAQMIAFNMQGYGRALWLMEGMFRANGGCGYVK 444

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  688 KPDFMRRPDRTFDPFseTPVDGVI-AATCSVQVISG----------QFLSDKKIGTYVEVDMYGLPTDTIRKEFRtrmVM 756
Cdd:PLN02230   445 KPDFLMDAGPNGQDF--YPKDNSCpKKTLKVKVCMGdgwlldfkktHFDSYSPPDFFVRVGIAGAPVDEVMEKTK---IE 519

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1243938431  757 NNGLNPVYNEEsFVFrKVILPDLAVLRIAVYD----DNNKLIGQRILPLDGLQAGYRHISLRN 815
Cdd:PLN02230   520 YDTWTPIWNKE-FIF-PLAVPELALLRVEVHEhdinEKDDFGGQTCLPVSEIRQGIHAVPLFN 580
EFh_PI-PLC21 cd16213
EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family ...
 148-300 1.44e-53

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: 184.04  E-value: 1.44e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  148 KKHWMKLAFLTNTTGKIPVRSITRTFASGKTE-KVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLF 226
Cdd:cd16213      1 EKAYTKLTLQTDKEGKIPVKNIVKMFAQHKDDrKRVEKALEAIGLPSGKNDAIDPKKFTFEDFFNFYRRLTGRQEVEKIF 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1243938431  227 KKINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 300
Cdd:cd16213     81 DELGAKKKPYLTTEQFVDFLNKTQRDPRLNEILYPYANPKRARDLINQYEPNKSFAKKGHLSVEGFLRYLMSED 154
PI-PLCc_plant cd08599
Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family ...
 312-680 9.01e-52

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: 181.80  E-value: 9.01e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  312 YQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDqePIITHGKAMCTDILFKDVIQA 391
Cdd:cd08599      1 HHDMTAPLSHYFIFSSHNSYLTGNQLSSRSSTAPIIEALLRGCRVIELDLWPGGRGD--ICVLHGGTLTKPVKFEDCIKA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  392 IKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQalesHPLEPGRPLPSPNDLKRKILIknkRLKPEVek 471
Cdd:cd08599     79 IKENAFTASEYPVIITLENHLSPELQAKAAQILRETLGDKLFYP----DSEDLPEEFPSPEELKGKILI---SDKPPV-- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  472 kqlealksmmeagesaapasileddneeeiesadqeeeahpeykFGNELSaddyshkeavansvkktsddlEHENNKKgl 551
Cdd:cd08599    150 --------------------------------------------IRNSLS---------------------ETQLKKV-- 162

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  552 vtvedeqawmasykyvgattnihpylstminyaqpvkfqgfhvaeernihynmssfnesVGLGYlKTHAIEFvnyNKRQM 631
Cdd:cd08599    163 -----------------------------------------------------------IEGEH-PTDLIEF---TQKNL 179

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1243938431  632 SRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:cd08599    180 LRVYPAGLRITSSNYDPMLAWMHGAQMVALNMQGYDRPLWLNRGKFRAN 228
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 714-830 3.41e-42

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: 150.38  E-value: 3.41e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  714 TCSVQVISGQFLSD------KKIGTYVEVDMYGLPTDTiRKEFRTRMVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVY 787
Cdd:cd00275      3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADD-SAKFKTKVVKNNGFNPVWNET-FEF-DVTVPELAFLRFVVY 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1243938431  788 DDN---NKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNI 830
Cdd:cd00275     80 DEDsgdDDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHI 125
EFh_PI-PLCbeta1 cd16208
EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1); PI-PLC-beta1, ...
 149-300 1.88e-36

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: 135.01  E-value: 1.88e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  149 KHWMKLAFLTNTTGKIPVRSITRTFASGKteKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFKK 228
Cdd:cd16208      2 KAYTKLKLQVNPEGRIPVKNIYRLFSADR--KRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDHIFSE 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1243938431  229 INGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 300
Cdd:cd16208     80 FGAKSKPYLSVDQMTEFINSKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSTLAKKGQISVDGFMRYLSGEE 151
PLN02223 PLN02223
phosphoinositide phospholipase C
 295-822 2.40e-35

phosphoinositide phospholipase C


Pssm-ID: 165867 [Multi-domain]  Cd Length: 537  Bit Score: 142.47  E-value: 2.40e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  295 YLMSDENAPVFLDRLElYQEMDHPLAHYFISSSHNTYLTGRQ-FGGKSSVEMYRQVLLAGCRCVELDCW-DGKGedqepi 372
Cdd:PLN02223    89 FLFSTELNPPIGDQVR-HHDMHAPLSHYFIHTSLKSYFTGNNvFGKLYSIEPIIDALEQGVRVVELDLLpDGKD------ 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  373 ithgkAMCT--------DILFKDVIQAIKETAFV-TSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQAlESHPLE 443
Cdd:PLN02223   162 -----GICVrpkwnfekPLELQECLDAIKEHAFTkCRSYPLIITFKDGLKPDLQSKATQMIDQTFGDMVYHED-PQHSLE 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  444 PgrpLPSPNDLKRKILIknkrlkpevekkqlealksmmeageSAAPASILeddneeeiesadqeeeahpeykfgneLSAD 523
Cdd:PLN02223   236 E---FPSPAELQNKILI-------------------------SRRPPKEL--------------------------LYAK 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  524 DYSHKEAVANSVKKTsddlEHENNKkglvtvedeqawmasykyvgattnihpylstmiNYAQPVkfqGFHVAEERNIHYN 603
Cdd:PLN02223   262 ADDGGVGVRNELEIQ----EGPADK---------------------------------NYQSLV---GFHAVEPRGMLQK 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  604 M--SSFNESVGLGYLKTHAIEFVnynKRQMSRIYPKGGRVDS-SNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYN 680
Cdd:PLN02223   302 AltGKADDIQQPGWYERDIISFT---QKKFLRTRPKKKNLLInAPYKPQRAWMHGAQLIALSRKDDKEKLWLMQGMFRAN 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  681 GSCGYLLKPDFMRR--PDRTFDPfSETPvdgVIAATCSVQVISGQ-FLSD--KKIGT------YVEVDMYGLPTDtirKE 749
Cdd:PLN02223   379 GGCGYVKKPDFLLNagPSGVFYP-TENP---VVVKILKVKIYMGDgWIVDfkKRIGRlskpdlYVRISIAGVPHD---EK 451

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1243938431  750 FRTRMVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVYD----DNNKLIGQRILPLDGLQAGYRHISLRNEGNKPLS 822
Cdd:PLN02223   452 IMKTTVKNNEWKPTWGEE-FTF-PLTYPDLALISFEVYDyevsTADAFCGQTCLPVSELIEGIRAVPLYDERGKACS 526
EFh_PI-PLCbeta3 cd16210
EF-hand motif found in phosphoinositide phospholipase C beta 3 (PI-PLC-beta3); PI-PLC-beta3, ...
 148-300 2.91e-32

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: 123.10  E-value: 2.91e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  148 KKHWMKLAFLTNTTGKIPVRSITRTFASGKteKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFK 227
Cdd:cd16210      1 RKAYTKLKLQVNQDGRIPVKNILKMFSADK--KRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILL 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1243938431  228 KINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 300
Cdd:cd16210     79 EIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQVRQLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 151
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 149-300 1.97e-27

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: 109.20  E-value: 1.97e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  149 KHWMKLAFLTNTTGKIPVRSITRTFASGKteKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFKK 228
Cdd:cd16209      2 KIYVKLKMQLNSEGKIPVKNFFQMFPADR--KRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTS 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1243938431  229 INGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 300
Cdd:cd16209     80 YHAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
DUF1154 pfam06631
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
 925-967 1.93e-17

Protein of unknown function (DUF1154); This family represents a small conserved region of unknown function within eukaryotic phospholipase C (EC:3.1.4.3). All members also contain pfam00387 and pfam00388.


Pssm-ID: 461969  Cd Length: 45  Bit Score: 76.91  E-value: 1.93e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1243938431  925 LIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQK 967
Cdd:pfam06631    3 KFPPITLESLRQDKAYLKLLKKQQKELESLKKKHSKERSAMQK 45
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 326-434 4.46e-17

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: 80.17  E-value: 4.46e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  326 SSHNTYLtgrQFGGKSSVEMYRQVLLAGCRCVELDCWDGKgeDQEPIITHG------KAMCTDILFKDVIQAIKETAFvT 399
Cdd:cd08555      2 LSHRGYS---QNGQENTLEAFYRALDAGARGLELDVRLTK--DGELVVYHGptldrtTAGILPPTLEEVLELIADYLK-N 75

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1243938431  400 SEYPVILSFENHCS----KYQQYKMSKYCEDLFGDLLLK 434
Cdd:cd08555     76 PDYTIILSLEIKQDspeyDEFLAKVLKELRVYFDYDLRG 114
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 177-300 1.78e-15

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: 74.57  E-value: 1.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  177 KTEKVIFQALKELGlpsgkNDEIEPAAFTyeKFYE-LTQkicpRTDIEDLFKKINGDKtDYLTVDQLVSFLNEHQRDPRL 255
Cdd:cd16202     36 DYAKKLFQEADTSG-----EDVLDEEEFV--QFYNrLTK----RPEIEELFKKYSGDD-EALTVEELRRFLQEEQKVKDV 103

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1243938431  256 neilfpfyDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 300
Cdd:cd16202    104 --------TLEWAEQLIETYEPSEDLKAQGLMSLDGFTLFLLSPD 140
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 717-813 5.19e-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: 69.05  E-value: 5.19e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431   717 VQVISGQFLSDKKIGT----YVEVDMYGLPtdtiRKEFRTRMVMNNgLNPVYNEEsFVFrKVILPDLAVLRIAVYDDN-- 790
Cdd:smart00239    4 VKIISARNLPPKDKGGksdpYVKVSLDGDP----KEKKKTKVVKNT-LNPVWNET-FEF-EVPPPELAELEIEVYDKDrf 76

                            90       100
                    ....*....|....*....|....*
gi 1243938431   791 --NKLIGQRILPLDGLQAGYRHISL 813
Cdd:smart00239   77 grDDFIGQVTIPLSDLLLGGRHEKL 101
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 209-300 5.91e-14

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: 68.43  E-value: 5.91e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  209 FY-ELTQkicpRTDIEDLFKKINGDkTDYLTVDQLVSFLNEHQRDPRlneilfpfYDAKRAMQIIEMYEPDEELKKKGLI 287
Cdd:pfam09279    1 FYkMLTQ----REEIDEIFQEYSGD-GQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAM 67

                           90
                   ....*....|...
gi 1243938431  288 SSDGFCRYLMSDE 300
Cdd:pfam09279   68 TKDGFLMYLCSPD 80
EFh_PRIP cd16206
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ...
 151-300 7.24e-12

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: 64.15  E-value: 7.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  151 WMKLAFL---TNTTGKIP---VRSITRTFASGKTEKVIFQALKELglpSGKNDEiEPAAFTYEKFYELTQKICPRTDIED 224
Cdd:cd16206      1 WLESVFEeadTNKSGFLDeeeAVQLIKQLNPGLSTSRIKQKLKEL---QKKKDG-ARGRVSSDEFVELFKELATRPEIYF 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1243938431  225 LFKKINGDKtDYLTVDQLVSFLNEHQRDPRLNEilfpfydaKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 300
Cdd:cd16206     77 LLVRYASNK-DYLTVDDLMLFLEAEQGMTGVTK--------EKCLEIINKYEPSEEGREKGQLGIDGFTRYLLSEE 143
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
 205-298 2.97e-10

EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes represent a class of neuron-specific metazoan PI-PLCs that are most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. They are phosphatidylinositol 4,5-bisphosphate-hydrolyzing enzymes that are more sensitive to Ca2+ than other PI-PLC isozymes. They function as calcium sensors activated by small increases in intracellular calcium concentrations. They are also activated through G-protein-coupled receptor (GPCR) stimulation, and further mediate GPCR signalling pathways. PI-PLC-eta isozymes contain an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases. There are two PI-PLC-eta isozymes (1-2). Aside from the PI-PLC-eta isozymes identified in mammals, their eukaryotic homologs are also present in this family.


Pssm-ID: 320035 [Multi-domain]  Cd Length: 141  Bit Score: 59.70  E-value: 2.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  205 TYEKFYELTQKICPRTDIEDLFKKInGDKTDYLTVDQLVSFLNEHQRdprLNEIlfpfyDAKRAMQIIEMYEPDEELKKK 284
Cdd:cd16205     55 DFEEFCAFYKMMSTRRELYLLLLSY-SNKKDYLTLEDLARFLEVEQK---MTNV-----TLEYCLDIIEKFEPSEENKKN 125

                           90
                   ....*....|....
gi 1243938431  285 GLISSDGFCRYLMS 298
Cdd:cd16205    126 GLLGIDGFTNYMRS 139
C2 pfam00168
C2 domain;
716-810 2.17e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 55.79  E-value: 2.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  716 SVQVISGQFLSDKKIG----TYVEVDMYGLptdtiRKEFRTRmVMNNGLNPVYNEEsFVFrKVILPDLAVLRIAVYDDN- 790
Cdd:pfam00168    4 TVTVIEAKNLPPKDGNgtsdPYVKVYLLDG-----KQKKKTK-VVKNTLNPVWNET-FTF-SVPDPENAVLEIEVYDYDr 75

                           90       100
                   ....*....|....*....|...
gi 1243938431  791 ---NKLIGQRILPLDGLQAGYRH 810
Cdd:pfam00168   76 fgrDDFIGEVRIPLSELDSGEGL 98
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 205-300 3.46e-09

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: 56.52  E-value: 3.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  205 TYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVDQLVSFLNEHQRDPrlneilfpfYDAKRAMQIIEMYEPDEElkkK 284
Cdd:cd15898     54 TFDEFEELYKSLTERPELEPIFKKYAGTNRDYMTLEEFIRFLREEQGEN---------VSEEECEELIEKYEPERE---N 121

                           90
                   ....*....|....*.
gi 1243938431  285 GLISSDGFCRYLMSDE 300
Cdd:cd15898    122 RQLSFEGFTNFLLSPE 137
EFh_PRIP2 cd16223
EF-hand motif found in phospholipase C-related but catalytically inactive protein 2 (PRIP-2); ...
 158-300 1.69e-08

EF-hand motif found in phospholipase C-related but catalytically inactive protein 2 (PRIP-2); PRIP-2, also termed phospholipase C-L2, or phospholipase C-epsilon-2 (PLC-epsilon-2), or inactive phospholipase C-like protein 2 (PLC-L2), is a novel inositol 1,4,5-trisphosphate (InsP3) binding protein that exhibits a relatively ubiquitous expression. It functions as a novel negative regulator of B-cell receptor (BCR) signaling and immune responses. PRIP-2 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-2 does not have PLC enzymatic activity.


Pssm-ID: 320053 [Multi-domain]  Cd Length: 144  Bit Score: 54.53  E-value: 1.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  158 TNTTGKIP----VRSITRTFASGKTEKVIFQaLKELGlpsgKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFKKINGDK 233
Cdd:cd16223     11 TDNVGHITlcraVQFIKNLNPGLKTSKIELK-FKELH----KSKEKGGTEVTKEEFIEVFHELCTRPEIYFLLVQFSSNK 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1243938431  234 tDYLTVDQLVSFLNEHQRDPRLNEilfpfydaKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDE 300
Cdd:cd16223     86 -EFLDTKDLMMFLEAEQGMAHVTE--------EISLDIIHKYEPSKEGQEKGWLSLDGFTNYLMSPE 143
PTZ00121 PTZ00121
MAEBL; Provisional
 851-1182 2.00e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 2.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  851 KKFLSITEKRADQMRAMGIETSDIADVP-SDTSKNDKKGKANPAKANVTPQSSSELRPTTTAALGSGQEAKKGIELipQV 929
Cdd:PTZ00121  1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA--KK 1398

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  930 RIEDLKQMKAYLKHLKKQQKELNSLKKKhAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGgsnclEIKKE 1009
Cdd:PTZ00121  1399 KAEEDKKKADELKKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE-----EAKKA 1472

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1010 TEIKIQTLTTDHKSKVKEIVAQHTKEWSEMINTHSAEEQ--EIRDLHLSQQCELLRKllinAHE-QQTQQLKLSHD-RES 1085
Cdd:PTZ00121  1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKK----AEEaKKADEAKKAEEkKKA 1548

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1086 KEMRAHQAKISMENSKAISQdksiKNKAERE-----RRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHL--EF 1158
Cdd:PTZ00121  1549 DELKKAEELKKAEEKKKAEE----AKKAEEDknmalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaEE 1624

                          330       340
                   ....*....|....*....|....
gi 1243938431 1159 LEKQNEQAKEMQQMVKLEAEMDRR 1182
Cdd:PTZ00121  1625 LKKAEEEKKKVEQLKKKEAEEKKK 1648
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
 207-300 2.34e-08

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: 53.97  E-value: 2.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  207 EKFY-ELTQkicpRTDIEDLFKKINGdKTDYLTVDQLVSFLNEHQRDPRLNEIlfpfydakrAMQIIEMYEPDEELKKKG 285
Cdd:cd16217     59 EEFYkLLTK----REEIDVIFGEYAK-SDGTMSRNNLLNFLQEEQREEVAPAY---------ALSLIEKYEPDETAKAQR 124

                           90
                   ....*....|....*
gi 1243938431  286 LISSDGFCRYLMSDE 300
Cdd:cd16217    125 QMTKDGFLMYLLSPE 139
PTZ00121 PTZ00121
MAEBL; Provisional
 848-1182 1.03e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 1.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  848 SDPKKFLSITEKRADQMRAMGiETSDIADVPSDTSKNDKKGKANPAKANVTPQSSSELRPTTTAAlGSGQEAKKGIELip 927
Cdd:PTZ00121  1374 EEAKKKADAAKKKAEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK-KKAEEAKKADEA-- 1449

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  928 QVRIEDLKQMKAyLKHLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGGSNCLEIK 1007
Cdd:PTZ00121  1450 KKKAEEAKKAEE-AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1008 KETEIKI--QTLTTDHKSKVKEI-VAQHTKEWSEMINTHSAEEQEIRDLHLSQQCELLRKL------LINAHEQQTQQLK 1078
Cdd:PTZ00121  1529 KAEEAKKadEAKKAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeearieEVMKLYEEEKKMK 1608

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1079 LSHDRESKEMR--AHQAKISMENSKAISQDKSI----KNKAERERRVRELN---SSNTKKFLEERKRLAMKQSKEMDQLK 1149
Cdd:PTZ00121  1609 AEEAKKAEEAKikAEELKKAEEEKKKVEQLKKKeaeeKKKAEELKKAEEENkikAAEEAKKAEEDKKKAEEAKKAEEDEK 1688

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1243938431 1150 KVQlehlEFLEKQNEQAKEMQQMVKLEAEMDRR 1182
Cdd:PTZ00121  1689 KAA----EALKKEAEEAKKAEELKKKEAEEKKK 1717
PTZ00121 PTZ00121
MAEBL; Provisional
 859-1176 1.14e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  859 KRADQMRAMGIETSDIADvpSDTSKNDKKGKANPAKANVTPQSSSELRPTTTA----ALGSGQEAKKGIELipqVRIEDL 934
Cdd:PTZ00121  1483 KKADEAKKKAEEAKKKAD--EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkadEAKKAEEKKKADEL---KKAEEL 1557

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  935 KQMKAYLK-HLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGgsnclEIKKETEIK 1013
Cdd:PTZ00121  1558 KKAEEKKKaEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-----ELKKAEEEK 1632

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1014 IQTLTTDHKSKVKEIVAQHTKEwseminthSAEEQEIRDLHLSQQCELLRKlliNAHEQQTQQLKLSHDRESKEMRAHQA 1093
Cdd:PTZ00121  1633 KKVEQLKKKEAEEKKKAEELKK--------AEEENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKKAAEALKKEAEEA 1701

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1094 KISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHLEFLEKQNEQAKEMQQMV 1173
Cdd:PTZ00121  1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781


                   ...
gi 1243938431 1174 KLE 1176
Cdd:PTZ00121  1782 EEE 1784
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 716-796 1.79e-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: 50.53  E-value: 1.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  716 SVQVISGQFLSDKKIG----TYVEVDMYGlptdtiRKEFRTRMVMNNgLNPVYNEEsFVFrKVILPDLAVLRIAVYDDN- 790
Cdd:cd00030      2 RVTVIEARNLPAKDLNgksdPYVKVSLGG------KQKFKTKVVKNT-LNPVWNET-FEF-PVLDPESDTLTVEVWDKDr 72


                   ....*....
gi 1243938431  791 ---NKLIGQ 796
Cdd:cd00030     73 fskDDFLGE 81
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 1047-1186 5.50e-07

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: 50.83  E-value: 5.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1047 EQEIRDLHLSQQCELLRKLLINAHEQQTQQLKLSHDRESKEMrahQAKISMENSKAISQ-DKSIKNKAERERRVRELNSS 1125
Cdd:pfam08703   25 EKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEM---KKKLERKRLESIQEaKKRTSDKAAQERLKKEINNS 101

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1243938431 1126 NTKKFLEERKRLAMKQSKEMDQLKKVQ---LEHLEFLEKQNEQakemQQMVKLEAEMDRRPATV 1186
Cdd:pfam08703  102 HIQEVVQSIKQLEEKQKRRQEKLEEKQaecLQQIKEEEPQLQA----ELNAEYEEKLKGLPAEV 161
EFh_PRIP1 cd16222
EF-hand motif found in phospholipase C-related but catalytically inactive protein 1 (PRIP-1); ...
 205-300 9.66e-07

EF-hand motif found in phospholipase C-related but catalytically inactive protein 1 (PRIP-1); PRIP-1, also termed phospholipase C-deleted in lung carcinoma, or inactive phospholipase C-like protein 1 (PLC-L1), or p130, is a novel inositol 1,4,5-trisphosphate (InsP3) binding protein that is predominantly expressed in the brain. It is involved in InsP3-mediated calcium signaling pathway and GABA(A)receptor-mediated signaling pathway. It interacts with the catalytic subunits of protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A), and functions as a scaffold to regulate the activities and subcellular localizations of both PP1 and PP2A in phospho-dependent cellular signaling. It also promotes the translocation of phosphatases to lipid droplets to trigger the dephosphorylation of hormone-sensitive lipase (HSL) and perilipin A, thus reducing protein kinase A (PKA)-mediated lipolysis. Moreover, PRIP-1 plays an important role in insulin granule exocytosis through the association with GABAA-receptor-associated protein (GABARAP) to form a complex to regulate KIF5B-mediated insulin secretion. It also inhibits regulated exocytosis through direct interactions with syntaxin 1 and synaptosomal-associated protein 25 (SNAP-25) via its C2 domain. Furthermore, PRIP-1 has been implicated in the negative regulation of bone formation. PRIP-1 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-1 does not have PLC enzymatic activity.


Pssm-ID: 320052 [Multi-domain]  Cd Length: 143  Bit Score: 49.48  E-value: 9.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  205 TYEKFYELTQKICPRTDIEDLFKKINGDKtDYLTVDQLVSFLNEHQRDPRLNEilfpfydaKRAMQIIEMYEPDEELKKK 284
Cdd:cd16222     57 TEEEFCEAYSELCTRPEVYFLLVQISKNK-EYLDAKDLMLFLEAEQGMTHITE--------EMCLDIIRRYEPSQEGRLK 127

                           90
                   ....*....|....*.
gi 1243938431  285 GLISSDGFCRYLMSDE 300
Cdd:cd16222    128 GFLGIDGFTQYLLSSE 143
EFh_PI-PLCdelta4 cd16219
EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, ...
 207-300 4.62e-06

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: 47.53  E-value: 4.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  207 EKFYELTQKICPRTDIEDLFKKINGDKTDyLTVDQLVSFLNEHQRDPRLNEILfpfydakrAMQIIEMYEPDEELKKKGL 286
Cdd:cd16219     56 EEFVLFYKALTQREDVLKIFQDFSADGQK-LTLLEFVDFLQQEQLERENTEEL--------AMELIDRYEPSDTAKKLHA 126

                           90
                   ....*....|....
gi 1243938431  287 ISSDGFCRYLMSDE 300
Cdd:cd16219    127 LSIDGFLMYLCSPE 140
PH_PLC_ELMO1 cd01248
Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain; The ...
 17-133 4.99e-06

Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain; The C-terminal region of ELMO1, the PH domain and Pro-rich sequences, binds the SH3-containing region of DOCK2 forming a intermolecular five-helix bundle allowing for DOCK mediated Rac1 activation. ELMO1, a mammalian homolog of C. elegans CED-12, contains an N-terminal RhoG-binding region, a ELMO domain, a PH domain, and a C-terminal sequence with three PxxP motifs. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). All PLCs, except for PLCzeta, have a PH domain which is for most part N-terminally located, though lipid binding specificity is not conserved between them. In addition PLC gamma contains a split PH domain within its catalytic domain that is separated by 2 SH2 domains and a single SH3 domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269952  Cd Length: 108  Bit Score: 46.55  E-value: 4.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431   17 LQEGAVFDRYEEESFVFEpnCLFKVDEFGFFLTWKSEGK--EGQVLECSLINSIRQAAIPKDPKilaaleAVGKSENDLE 94
Cdd:cd01248      1 LQQGTLLLKYREGSKPKE--RTFYLDPDGTRITWESSKKksEKKSIDISDIKEIRPGKDTDGFK------RKKKSNKPKE 72

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1243938431   95 GRILCVCSGTDLVNIGFtymVAENPEVTKQWVEGLRSII 133
Cdd:cd01248     73 ERCFSIIYGSNNKTLDL---VAPSEDEANLWVEGLRALL 108
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 897-1181 5.85e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 50.89  E-value: 5.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  897 VTPQSSSELRPTTTAALgsgQEAKKGIEL----IPQVR------IEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQ 966
Cdd:pfam15921  489 MTLESSERTVSDLTASL---QEKERAIEAtnaeITKLRsrvdlkLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIE 565

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  967 KLHcTQVD---KIVAQYDKEKSTHEkiLEKA-MKKKGGSNCLEIKketEIKIqtLTTDHKSKVKEIVAQHTK---EWSEM 1039
Cdd:pfam15921  566 ILR-QQIEnmtQLVGQHGRTAGAMQ--VEKAqLEKEINDRRLELQ---EFKI--LKDKKDAKIRELEARVSDlelEKVKL 637

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1040 INTHSAEEQEIRDL-------------------HLSQQCELLRKLLINAHEQQ---TQQLKL---SHDRESKEMR----- 1089
Cdd:pfam15921  638 VNAGSERLRAVKDIkqerdqllnevktsrnelnSLSEDYEVLKRNFRNKSEEMettTNKLKMqlkSAQSELEQTRntlks 717

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1090 -----AHQAKISMENSKAISQDKSIKNKAERERRVRE---LNSSNTKKFL-EERKRLAMKQSKEMDQLKKVQLEhLEFLE 1160
Cdd:pfam15921  718 megsdGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEeamTNANKEKHFLkEEKNKLSQELSTVATEKNKMAGE-LEVLR 796

                          330       340
                   ....*....|....*....|.
gi 1243938431 1161 KQNEQAKEmqQMVKLEAEMDR 1181
Cdd:pfam15921  797 SQERRLKE--KVANMEVALDK 815
EFh_PI-PLCzeta cd16204
EF-hand motif found in phosphoinositide phospholipase C zeta 1 (PI-PLC-zeta1); PI-PLC-zeta1, ...
 195-300 2.61e-05

EF-hand motif found in phosphoinositide phospholipase C zeta 1 (PI-PLC-zeta1); PI-PLC-zeta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1, or phospholipase C-zeta-1 (PLC-zeta-1), or testis-development protein NYD-SP27, is only found in the testis. The sperm-specific PI-PLC 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. PI-PLC-zeta1 contains an N-terminal 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 other PI-PLCs, PI-PLC-zeta is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. There is only one PLC-zeta isozyme. Aside from PI-PLC-zeta identified in mammals, its eukaryotic homologs have been classified with this family.


Pssm-ID: 320034 [Multi-domain]  Cd Length: 142  Bit Score: 45.19  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  195 KNDEIEPAAFTYEKFYELTQKICPRTDIEDLFKkINGDKTDYLTVDQLVSFLNEHQRDPRLNEilfpfydaKRAMQIIEM 274
Cdd:cd16204     46 KNDSFKAGNITIEDFRAIYRAIAHRCEIHEIFN-TYSENRKILSAPNLVGFLKKEQFQDEADE--------TIASELIAK 116

                           90       100
                   ....*....|....*....|....*.
gi 1243938431  275 YEPDEELKKKGLISSDGFCRYLMSDE 300
Cdd:cd16204    117 YEPIEEVRKRKQMSFEGFIRYMTSED 142
EFh_PI-PLCepsilon cd16203
EF-hand motif found in phosphoinositide phospholipase C epsilon 1 (PI-PLC-epsilon1); ...
 237-297 3.11e-05

EF-hand motif found in phosphoinositide phospholipase C epsilon 1 (PI-PLC-epsilon1); PI-PLC-epsilon1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1, or pancreas-enriched phospholipase C, or phospholipase C-epsilon-1 (PLC-epsilon-1), is dominant in connective tissues and brain. It has been implicated in carcinogenesis, such as in bladder and intestinal tumor, oesophageal squamous cell carcinoma, gastric adenocarcinoma, murine skin cancer, head and neck cancer. PI-PLC-epsilon1 contains an N-terminal CDC25 homology domain with a guanyl-nucleotide exchange factor (GFF) activity, a pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and at least one and perhaps two C-terminal 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 only one PI-PLC-epsilon isozyme. It is directly activated by G alpha(12/13), G beta gamma, and activated members of Ras and Rho small GTPases.


Pssm-ID: 320033  Cd Length: 174  Bit Score: 45.78  E-value: 3.11e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1243938431  237 LTVDQLVSFLNEHQRDPrlneilfpfYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLM 297
Cdd:cd16203    120 LTISQLKDFLENHQMEH---------ITEEEAIKIIQRHEPDPILRSKNCLSFEGFARYLM 171
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 944-1185 3.13e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.20  E-value: 3.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  944 LKKQQKELNSLKKKH-AKEHSTMQKLHCTQVDKivaQYDKEKSTHEkiLEKAMKKKggsnCLEIKKETEIKIQTLTTDHK 1022
Cdd:pfam17380  355 QEERKRELERIRQEEiAMEISRMRELERLQMER---QQKNERVRQE--LEAARKVK----ILEEERQRKIQQQKVEMEQI 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1023 SKVKEIVAQHTKEWSEMINTHSAEEQEIRDLHLSQQCELLRKllinaHEQQTQQLKLSHDRESKEmrahQAKISMENSKA 1102
Cdd:pfam17380  426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQ-----QEEERKRKKLELEKEKRD----RKRAEEQRRKI 496

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1103 ISQDKSIKNKA----ERERRV--RELNSSNTKKFLEERKR---------LAMKQSKEM-DQLKKVQLE--HLEFLEKQNE 1164
Cdd:pfam17380  497 LEKELEERKQAmieeERKRKLleKEMEERQKAIYEEERRReaeeerrkqQEMEERRRIqEQMRKATEErsRLEAMERERE 576

                          250       260
                   ....*....|....*....|.
gi 1243938431 1165 QakeMQQMVKLEAEMDRRPAT 1185
Cdd:pfam17380  577 M---MRQIVESEKARAEYEAT 594
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 316-465 5.05e-05

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: 46.32  E-value: 5.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  316 DHPLAHYFISSSHNTY---LTGRQFGGKSSVE-----MYRQvLLAGCRCVELDCWDgKGEDQEPIITHGKAMCTDILFKD 387
Cdd:cd08557      6 DLPLSQLSIPGTHNSYaytIDGNSPIVSKWSKtqdlsITDQ-LDAGVRYLDLRVAY-DPDDGDLYVCHGLFLLNGQTLED 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  388 VIQAIKetAFVT---SEyPVILSFENHcskyqqYKMSKYCEDLFGDLLLKQALESHPLEPgrPLPSPNDLKRKILIKNKR 464
Cdd:cd08557     84 VLNEVK--DFLDahpSE-VVILDLEHE------YGGDNGEDHDELDALLRDVLGDPLYRP--PVRAGGWPTLGELRAGKR 152


                   .
gi 1243938431  465 L 465
Cdd:cd08557    153 V 153
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 917-1168 7.57e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 47.12  E-value: 7.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  917 QEAKKGIELIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHcTQVDKIVAQYDKEKSTHEKILEKAMK 996
Cdd:pfam10174  257 QMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQ-TKLETLTNQNSDCKQHIEVLKESLTA 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  997 KKGGSNCLEikkeTEIKIQTLTTDHKskvKEIVAQHTKEWSEMINTHSAEEQEIRDLhlsqqcellrKLLINAHEQQTQQ 1076
Cdd:pfam10174  336 KEQRAAILQ----TEVDALRLRLEEK---ESFLNKKTKQLQDLTEEKSTLAGEIRDL----------KDMLDVKERKINV 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1077 LklshdreskemrahQAKIsmENSKAISQDKSiKNKAERERRVREL--NSSNT-------KKFLEERKRLAMKQSKEMDQ 1147
Cdd:pfam10174  399 L--------------QKKI--ENLQEQLRDKD-KQLAGLKERVKSLqtDSSNTdtalttlEEALSEKERIIERLKEQRER 461

                          250       260
                   ....*....|....*....|.
gi 1243938431 1148 LKKVQLEHLEFLEKQNEQAKE 1168
Cdd:pfam10174  462 EDRERLEELESLKKENKDLKE 482
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 1060-1181 7.99e-05

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 43.70  E-value: 7.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1060 ELLRKLLINAHEQQTQQLKLSHDRESKEM-RAHQAKIS-MENSKAISQDKSIKN-KAERERRvrelnssnTKKFLEERKR 1136
Cdd:pfam12474    2 QLQKEQQKDRFEQERQQLKKRYEKELEQLeRQQKQQIEkLEQRQTQELRRLPKRiRAEQKKR--------LKMFRESLKQ 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1243938431 1137 LAMKQSKEMDQLKKVQL--------EHLEFLEKQNEQAKEMQQMVKLEAEMDR 1181
Cdd:pfam12474   74 EKKELKQEVEKLPKFQRkeakrqrkEELELEQKHEELEFLQAQSEALERELQQ 126
EFh_PI-PLCeta1 cd16220
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ...
 204-298 2.58e-04

EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1, or phospholipase C-eta-1 (PLC-eta-1), or phospholipase C-like protein 3 (PLC-L3), is a neuron-specific PI-PLC that is most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. It is also expressed in the zona incerta and in the spinal cord. PI-PLC-eta1 may perform a fundamental role in the brain. It may also act in synergy with other PLC subtypes. For instance, it is activated via intracellular Ca2+ mobilization and then plays a role in the amplification of GPCR (G-protein-coupled receptor)-mediated PLC-beta signals. In addition, its activity can be stimulated by ionomycin. PI-PLC-eta1 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases.


Pssm-ID: 320050 [Multi-domain]  Cd Length: 141  Bit Score: 42.32  E-value: 2.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  204 FTYEKFYELTQKICPRTDIEDLFKKINgDKTDYLTVDQLVSFLNEHQrdpRLNEILFPFydakrAMQIIEMYEPDEELKK 283
Cdd:cd16220     54 LTFEEFCVFYKMMSLRRDLYLLLLSYS-DKKDHLTVEELAQFLKVEQ---KMNNVTTEY-----CLDIIKKFEVSEENKE 124

                           90
                   ....*....|....*
gi 1243938431  284 KGLISSDGFCRYLMS 298
Cdd:cd16220    125 QNVLGIEGFTNFMRS 139
EFh_PI-PLCdelta3 cd16218
EF-hand motif found in phosphoinositide phospholipase C delta 3 (PI-PLC-delta3); PI-PLC-delta3, ...
 211-300 2.80e-04

EF-hand motif found in phosphoinositide phospholipase C delta 3 (PI-PLC-delta3); PI-PLC-delta3, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 (PLCD3), phospholipase C-delta-3 (PLC-delta-3), is expressed abundantly in brain, skeletal muscle and heart. PI-PLC-delta3 gene expression is down-regulation by cAMP and calcium. PI-PLC-delta3 acts as anchoring of myosin VI on plasma membrane, and further modulates Myosin IV expression and microvilli formation in enterocytes. It negatively regulates RhoA expression, inhibits RhoA/Rho kinase signaling, and plays an essential role in normal neuronal migration by promoting neuronal outgrowth in the developing brain. Moreover, PI-PLC-delta3 is essential in trophoblasts for placental development. Simultaneous loss of PI-PLC-delta3 may cause placental vascular defects, leading to embryonic lethality. PI-PLC-delta3 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. In addition, PI-PLC-delta3 possesses a classical leucine-rich nuclear export sequence (NES) located in the EF hand motifs, which may be responsible transporting PI-PLC-delta3 from the cell nucleus.


Pssm-ID: 320048 [Multi-domain]  Cd Length: 138  Bit Score: 42.43  E-value: 2.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  211 ELTQKICPRTDIEDLFKKINGdKTDYLTVDQLVSFLNEHQRDPRLneilfpfydaKRAMQIIEMYEPDEELKKKGLISSD 290
Cdd:cd16218     60 EFCRRLMQRPELEEIFHQYSG-EDCVLSAEELREFLKDQGEDASL----------VHAKELIQTYELNEKAKQHQLMTLD 128

                           90
                   ....*....|
gi 1243938431  291 GFCRYLMSDE 300
Cdd:cd16218    129 GFTMYMLSKD 138
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 992-1182 3.06e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 3.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  992 EKAMKKKggsnclEIKKETEIKIQTLTTDHKSKVKEIVAQHTKEWSEMINTHSAEEQEIRDLhlsqqcellrkllinahE 1071
Cdd:COG1196    210 EKAERYR------ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL-----------------E 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1072 QQTQQLKLSHDRESKEMRAHQAKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKV 1151
Cdd:COG1196    267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1243938431 1152 QLEHLEFLEKQNEQAKEMQQMVKLEAEMDRR 1182
Cdd:COG1196    347 EEAEEELEEAEAELAEAEEALLEAEAELAEA 377
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 843-1173 5.83e-04

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


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 43.98  E-value: 5.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  843 IVDALSDPKKFLSITEKRADQmramgiETSDIADVPSDTSKNDKKGKANPAKANVTPQSSSELRP----------TTTAA 912
Cdd:pfam09731  158 AVKAHTDSLKEASDTAEISRE------KATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAapetppklpeHLDNV 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  913 LGSGQEAKKGIELIPQV-------RIEDLKQMKAYLKHLKKQQKELNSLKKkhAKEHSTMQKLHcTQVDKIVAQYDKEKS 985
Cdd:pfam09731  232 EEKVEKAQSLAKLVDQYkelvaseRIVFQQELVSIFPDIIPVLKEDNLLSN--DDLNSLIAHAH-REIDQLSKKLAELKK 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  986 THEKILEKAMKKKggsncleiKKETEIKIQTLTTDHKSKVKEIVAQHTKEW-SEMINTHSAEEQEIRdLHLSQQCELLRK 1064
Cdd:pfam09731  309 REEKHIERALEKQ--------KEELDKLAEELSARLEEVRAADEAQLRLEFeREREEIRESYEEKLR-TELERQAEAHEE 379

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1065 LLINAHEQQTQQLKLSHDREskemrahqakismenskaisqdksIKNKAERERRVRelnssnTKKFLEERKRLAmkqske 1144
Cdd:pfam09731  380 HLKDVLVEQEIELQREFLQD------------------------IKEKVEEERAGR------LLKLNELLANLK------ 423

                          330       340
                   ....*....|....*....|....*....
gi 1243938431 1145 mdQLKKVQLEHLEfLEKQNEQAKEMQQMV 1173
Cdd:pfam09731  424 --GLEKATSSHSE-VEDENRKAQQLWLAV 449
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 716-790 1.03e-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: 40.32  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  716 SVQVISGQFLSDKKIGT----YVEVDmygLPTDTIRKeFRTRmVMNNGLNPVYNeESFVFRkvILPDLA-VLRIAVYDDN 790
Cdd:cd04036      3 TVRVLRATNITKGDLLStpdcYVELW---LPTASDEK-KRTK-TIKNSINPVWN-ETFEFR--IQSQVKnVLELTVMDED 74
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
 733-801 1.48e-03

C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis as do synaptotagmins 5, 6, and 10. It is distinguished from the other synaptotagmins by having an N-glycosylated N-terminus. Synaptotagmins 5, 6, and 10, members of class 3 synaptotagmins, are located primarily in the brain and localized to the active zone and plasma membrane. They is distinguished from the other synaptotagmins by having disulfide bonds at its N-terminus. Synaptotagmin 6 also regulates the acrosome reaction, a unique Ca2+-regulated exocytosis, in sperm. Synaptotagmin 9, a class 5 synaptotagmins, is located in the brain and localized to the synaptic vesicles. It is thought to be a Ca2+-sensor for dense-core vesicle exocytosis. 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 first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176031 [Multi-domain]  Cd Length: 124  Bit Score: 39.94  E-value: 1.48e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243938431  733 YVEVdmYGLPtDTiRKEFRTRmVMNNGLNPVYNeESFVFrKVILPDLA--VLRIAVYDDN----NKLIGQRILPL 801
Cdd:cd08385     40 YVKV--YLLP-DK-KKKFETK-VHRKTLNPVFN-ETFTF-KVPYSELGnkTLVFSVYDFDrfskHDLIGEVRVPL 107
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
 219-298 1.57e-03

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


Pssm-ID: 320037 [Multi-domain]  Cd Length: 142  Bit Score: 40.31  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  219 RTDIEDLFKKINGDKTDYLTVDQLVSFLNEHQRDPrlneilfpfYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMS 298
Cdd:cd16207     70 RKDIKAIFKQLTKPGSDGLTLEEFLKFLRDVQKED---------VDRETWEKIFEKFARRIDDSDSLTMTLEGFTSFLLS 140
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 921-1181 3.48e-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: 41.57  E-value: 3.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  921 KGIELIPQVRIEDLKQMKAYlkHLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKE----KSTHEKILEKAMK 996
Cdd:TIGR00606  186 KALETLRQVRQTQGQKVQEH--QMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENEldplKNRLKEIEHNLSK 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  997 KKGGSNCLEIKKETEIKIQTLTTDHKSKVKEIVAQHTKEWSEMINTHSAE----EQEIRDLH-----LSQQCELLR---- 1063
Cdd:TIGR00606  264 IMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTvrekERELVDCQrelekLNKERRLLNqekt 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1064 -------KLLINAHEQQTQQLKLSHDRESKEMRAHQAKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKfLEERKR 1136
Cdd:TIGR00606  344 ellveqgRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCAD-LQSKER 422

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1137 LAMKQSKEMDQLKK-----VQLEHLEFLEKQNEQAKEMQQMVKLEAEMDR 1181
Cdd:TIGR00606  423 LKQEQADEIRDEKKglgrtIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 935-1107 4.50e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 41.25  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  935 KQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKlhctqvdkivaQYDKEKSTHEKILEKAMKKKGGSN-CLEIKKETEIK 1013
Cdd:pfam05483  629 KQLNAYEIKVNKLELELASAKQKFEEIIDNYQK-----------EIEDKKISEEKLLEEVEKAKAIADeAVKLQKEIDKR 697

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1014 IQ-------TLTTDHKSKVKEIVAQHTKEwsemINTHSAEEQEIRDLHLSQQCEL--LRKLLINAHEQqtqqlkLSHDRE 1084
Cdd:pfam05483  698 CQhkiaemvALMEKHKHQYDKIIEERDSE----LGLYKNKEQEQSSAKAALEIELsnIKAELLSLKKQ------LEIEKE 767

                          170       180
                   ....*....|....*....|...
gi 1243938431 1085 SKEMRAHQAKismENSKAISQDK 1107
Cdd:pfam05483  768 EKEKLKMEAK---ENTAILKDKK 787
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 716-810 5.71e-03

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


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 38.33  E-value: 5.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  716 SVQVISGQFLSDKKIG----TYVEVDMYGlpTDTIRKEFRTRMVMNNgLNPVYNeESFVFrKVILPDL--AVLRIAVYDD 789
Cdd:cd00276     17 TVVVLKARNLPPSDGKglsdPYVKVSLLQ--GGKKLKKKKTSVKKGT-LNPVFN-EAFSF-DVPAEQLeeVSLVITVVDK 91

                           90       100
                   ....*....|....*....|....*
gi 1243938431  790 ----NNKLIGQRILPLDGLQAGYRH 810
Cdd:cd00276     92 dsvgRNEVIGQVVLGPDSGGEELEH 116
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
917-1181 6.31e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 6.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  917 QEAKKGIELIPQVRiEDLKQMKAYLKHLKKQQKELNSLKKKhAKEHSTMQKLHCTQVDKI------VAQYDKEKSTHEKI 990
Cdd:PRK03918   252 GSKRKLEEKIRELE-ERIEELKKEIEELEEKVKELKELKEK-AEEYIKLSEFYEEYLDELreiekrLSRLEEEINGIEER 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  991 LEKAMKKKGGSNCLEIK-KETEIKIQTLTTDHK--SKVKEIVAQhtkewsemINTHSAEEQEIRDLHLSQQCELLRKlli 1067
Cdd:PRK03918   330 IKELEEKEERLEELKKKlKELEKRLEELEERHElyEEAKAKKEE--------LERLKKRLTGLTPEKLEKELEELEK--- 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1068 nAHEQQTQQLKlshdrESKEMRAHQAKISMENSKAISQDKSIKNKAERERrvRELNSsntkkflEERKRLAMKQSKEMDQ 1147
Cdd:PRK03918   399 -AKEEIEEEIS-----KITARIGELKKEIKELKKAIEELKKAKGKCPVCG--RELTE-------EHRKELLEEYTAELKR 463

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1243938431 1148 LKKVQLEHLEFLEKQNEQAKEMQQMVKLEAEMDR 1181
Cdd:PRK03918   464 IEKELKEIEEKERKLRKELRELEKVLKKESELIK 497
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 945-1167 6.55e-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: 40.93  E-value: 6.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  945 KKQQKELNSLKKKHAKEHSTMQKLhctQVDKIVAQyDKEKSTHEKIL-----------EKAMKKKGGSNCLEIKKETEIK 1013
Cdd:pfam01576   99 KKMQQHIQDLEEQLDEEEAARQKL---QLEKVTTE-AKIKKLEEDILlledqnsklskERKLLEERISEFTSNLAEEEEK 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1014 IQTLT---TDHKSKVKEIVAQHTKE---WSEMINTHSAEEQEIRDLH-----LSQQ-CELLRKLLINAHEQQTQQLKLsh 1081
Cdd:pfam01576  175 AKSLSklkNKHEAMISDLEERLKKEekgRQELEKAKRKLEGESTDLQeqiaeLQAQiAELRAQLAKKEEELQAALARL-- 252

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1082 DRES-------KEMRAHQAKISmENSKAISQDKSIKNKAERERR----------------------------VRELNSSN 1126
Cdd:pfam01576  253 EEETaqknnalKKIRELEAQIS-ELQEDLESERAARNKAEKQRRdlgeelealkteledtldttaaqqelrsKREQEVTE 331

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1243938431 1127 TKKFLEERKRLAMKQSKEMDQLKKVQLEHlefLEKQNEQAK 1167
Cdd:pfam01576  332 LKKALEEETRSHEAQLQEMRQKHTQALEE---LTEQLEQAK 369
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 927-1177 8.00e-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: 40.34  E-value: 8.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  927 PQVRIEDLKQMKAYLKHLKKQQKELNSLKKKH---AKEHSTMQKLHCTQVDKIVAQYD-KEKSTHEKILEKAMKKKGGSN 1002
Cdd:TIGR00618  364 ATSIREISCQQHTLTQHIHTLQQQKTTLTQKLqslCKELDILQREQATIDTRTSAFRDlQGQLAHAKKQQELQQRYAELC 443

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1003 CLEIKKETEIKIQTLTTDHKS----KVKEIVAQHTKEWSEMINTHSAEEQEIRDLHLSQQCELLRKLL-INAHEQQTQQL 1077
Cdd:TIGR00618  444 AAAITCTAQCEKLEKIHLQESaqslKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhPNPARQDIDNP 523

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1078 KLSHDR-ESKEMRAHQAKISMENSKAI-----SQDKSIKNKAERERRVRELNSS----------NTKKFLEERKRLAMKQ 1141
Cdd:TIGR00618  524 GPLTRRmQRGEQTYAQLETSEEDVYHQltserKQRASLKEQMQEIQQSFSILTQcdnrskedipNLQNITVRLQDLTEKL 603

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1243938431 1142 SKEMDQLKKVQLEHLEFLE-KQNEQ--AKEMQQMVKLEA 1177
Cdd:TIGR00618  604 SEAEDMLACEQHALLRKLQpEQDLQdvRLHLQQCSQELA 642
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 917-1176 8.19e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.34  E-value: 8.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  917 QEAKKGIELIPQVriedLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMK 996
Cdd:pfam02463  258 QEIEKEEEKLAQV----LKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  997 KKGGSNCLEIKKETEIKIQTLTTDHKSKVKEIVAQHTKEWSEMINTHSAEEQEIRDLHLSQQCELLRKLLINAheqQTQQ 1076
Cdd:pfam02463  334 KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE---AQLL 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1077 LKLSHDRESKEMRAHQAKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKemdQLKKVQLEHL 1156
Cdd:pfam02463  411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET---QLVKLQEQLE 487

                          250       260
                   ....*....|....*....|
gi 1243938431 1157 EFLEKQNEQAKEMQQMVKLE 1176
Cdd:pfam02463  488 LLLSRQKLEERSQKESKARS 507
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 930-1181 9.63e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 9.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  930 RIEDL-KQMKAYLKHLKKQ----------QKELNSLKKKHAKehstmqkLHCTQVDKIVAQYDKEKSTHEKILEKAMKKK 998
Cdd:COG1196    190 RLEDIlGELERQLEPLERQaekaeryrelKEELKELEAELLL-------LKLRELEAELEELEAELEELEAELEELEAEL 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431  999 ggsncleikKETEIKIQTLTTDHKSKVKEI------VAQHTKEWSEMINTHSAEEQEIRDLH-----LSQQCELLRKLLI 1067
Cdd:COG1196    263 ---------AELEAELEELRLELEELELELeeaqaeEYELLAELARLEQDIARLEERRRELEerleeLEEELAELEEELE 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938431 1068 nAHEQQTQQLKLSHDRESKEMRAHQAKISMENSKAISQDKSIknkAERERRVRELNssntKKFLEERKRLAMKQSKEMDQ 1147
Cdd:COG1196    334 -ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELA----EELLEALRAAAELAAQLEEL 405

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1243938431 1148 LKKVQLEHLEFLEKQNEQAKEMQQMVKLEAEMDR 1181
Cdd:COG1196    406 EEAEEALLERLERLEEELEELEEALAELEEEEEE 439
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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