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Conserved domains on  [gi|1039738371|ref|XP_017170277|]
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1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 isoform X3 [Mus musculus]

Protein Classification

PI-PLCc_GDPD_SF and C2_PLC_like domain-containing protein( domain architecture ID 10326751)

protein containing domains PI-PLCc_GDPD_SF, C2_PLC_like, and PHA03247

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_GDPD_SF super family cl14615
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 20-314 9.05e-176

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.


The actual alignment was detected with superfamily member cd08630:

Pssm-ID: 472694 [Multi-domain]  Cd Length: 258  Bit Score: 493.00  E-value: 9.05e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08630     2 QDMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSQNPEELPSPEQLKGRILVKGKKLpaarsedgrils 179
Cdd:cd08630    82 HAFTASPYPVILSLENHCGLEQQAAMARHLQTILGDMLVTQPLDSLNPEELPSPEELKGRVLVKGKKL------------ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsrakQISPELSALAVYCCATRLRTLDPSPGPPQSCTVGSLSERKARKFTREAGTSFVR 259
Cdd:cd08630   150 --------------------------QISPELSALAVYCQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFVR 203

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039738371 260 HNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08630   204 HNARQLTRVYPLGLRMNSANYSPQEMWNSGCQLVALNFQTPGYEMDLNAGRFLVN 258
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 343-470 2.04e-53

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: 175.42  E-value: 2.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 343 TTLAIQVLTAQQLPKLNAEKpSSIVDPLVRVEIHGVPE-DCAQKETDYVLNNGFNPCWEQTLQFRLRAPELVLVRFVVED 421
Cdd:cd00275     2 LTLTIKIISGQQLPKPKGDK-GSIVDPYVEVEIHGLPAdDSAKFKTKVVKNNGFNPVWNETFEFDVTVPELAFLRFVVYD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1039738371 422 YDTTSpNDFVGQSTLPLSSLKQGYRHIHLLSKDGASLAPATLFVHIRIQ 470
Cdd:cd00275    81 EDSGD-DDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
 
Name Accession Description Interval E-value
PI-PLCc_delta3 cd08630
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily ...
 20-314 9.05e-176

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: 493.00  E-value: 9.05e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08630     2 QDMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSQNPEELPSPEQLKGRILVKGKKLpaarsedgrils 179
Cdd:cd08630    82 HAFTASPYPVILSLENHCGLEQQAAMARHLQTILGDMLVTQPLDSLNPEELPSPEELKGRVLVKGKKL------------ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsrakQISPELSALAVYCCATRLRTLDPSPGPPQSCTVGSLSERKARKFTREAGTSFVR 259
Cdd:cd08630   150 --------------------------QISPELSALAVYCQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFVR 203

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039738371 260 HNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08630   204 HNARQLTRVYPLGLRMNSANYSPQEMWNSGCQLVALNFQTPGYEMDLNAGRFLVN 258
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 22-164 6.99e-90

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: 270.15  E-value: 6.99e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  22 MGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRDHA 101
Cdd:pfam00388   1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDGPDGEPVVYHGYTLTSKIPFRDVLEAIKDYA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738371 102 FTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDsQNPEELPSPEQLKGRILVKG 164
Cdd:pfam00388  81 FVTSPYPVILSLENHCSPEQQKKMAEILKEIFGDMLYTPPLD-DDLTELPSPEDLKGKILIKG 142
PLN02952 PLN02952
phosphoinositide phospholipase C
 20-465 3.77e-81

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 263.01  E-value: 3.77e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPV-IYHGHTLTSKILFRDVIQAVR 98
Cdd:PLN02952  123 HDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGSTKDEIlVLHGRTLTTPVPLIKCLKSIR 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  99 DHAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSQnpEELPSPEQLKGRILVKGK------------- 165
Cdd:PLN02952  203 DYAFSSSPYPVIITLEDHLTPDLQAKVAEMATQIFGQMLYYPESDSL--VQFPSPESLKHRIIISTKppkeylessgpiv 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 166 -KLPAARSEDGRILSDREEEEEEEEEAEEALEAAeQRSRAKQISPELSALA--VYccaTRLRTLdpSPGPPQSCTVG--- 239
Cdd:PLN02952  281 iKKKNNVSPSGRNSSEETEEAQTLESMLFEQEAD-SRSDSDQDDNKSGELQkpAY---KRLITI--HAGKPKGTLKDamk 354

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 240 ---------SLSERKARKFTREAGTSFVRHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGR 310
Cdd:PLN02952  355 vavdkvrrlSLSEQELEKAATTNGQDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGAQMIAFNMQGYGKSLWLMHGM 434

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 311 FLINGQCGYVLKPAYLRQL---NTTFDPECPGPPRTTLAIQVLTAQ------QLPKLNAEKPSsivDPLVRVEIHGVPED 381
Cdd:PLN02952  435 FRANGGCGYLKKPDFLMKKgfhDEVFDPKKKLPVKKTLKVKVYLGDgwrldfSHTHFDSYSPP---DFYTKMYIVGVPAD 511

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 382 CAQKETDYVLNNgFNPCWEQTLQFRLRAPELVLVRFVVEDYDTTSPNDFVGQSTLPLSSLKQGYRHIHLLSKDGASLAPA 461
Cdd:PLN02952  512 NAKKKTKIIEDN-WYPAWNEEFSFPLTVPELALLRIEVREYDMSEKDDFGGQTCLPVSELRPGIRSVPLHDKKGEKLKNV 590


                  ....
gi 1039738371 462 TLFV 465
Cdd:PLN02952  591 RLLM 594
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 22-165 4.61e-75

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: 232.17  E-value: 4.61e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371   22 MGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRDHA 101
Cdd:smart00148   1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDGPDGEPVIYHGHTFTLPIKLSEVLEAIKDFA 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738371  102 FTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSqNPEELPSPEQLKGRILVKGK 165
Cdd:smart00148  81 FVTSPYPVILSLENHCSPDQQAKMAQMFKEIFGDMLYTPPLTS-SLEVLPSPEQLRGKILLKVR 143
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 343-470 2.04e-53

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: 175.42  E-value: 2.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 343 TTLAIQVLTAQQLPKLNAEKpSSIVDPLVRVEIHGVPE-DCAQKETDYVLNNGFNPCWEQTLQFRLRAPELVLVRFVVED 421
Cdd:cd00275     2 LTLTIKIISGQQLPKPKGDK-GSIVDPYVEVEIHGLPAdDSAKFKTKVVKNNGFNPVWNETFEFDVTVPELAFLRFVVYD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1039738371 422 YDTTSpNDFVGQSTLPLSSLKQGYRHIHLLSKDGASLAPATLFVHIRIQ 470
Cdd:cd00275    81 EDSGD-DDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 344-450 9.23e-19

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: 81.38  E-value: 9.23e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  344 TLAIQVLTAQQLPKLNaekPSSIVDPLVRVEIHGVPEDCAQkeTDYVLNNGfNPCWEQTLQFRLRAPELVLVRFVVEDYD 423
Cdd:smart00239   1 TLTVKIISARNLPPKD---KGGKSDPYVKVSLDGDPKEKKK--TKVVKNTL-NPVWNETFEFEVPPPELAELEIEVYDKD 74

                           90       100
                   ....*....|....*....|....*..
gi 1039738371  424 TTSPNDFVGQSTLPLSSLKQGYRHIHL 450
Cdd:smart00239  75 RFGRDDFIGQVTIPLSDLLLGGRHEKL 101
C2 pfam00168
C2 domain;
344-449 4.12e-16

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 73.89  E-value: 4.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 344 TLAIQVLTAQQLPKLNaekPSSIVDPLVRVEIHgvpeDCAQKETDYVLNNGFNPCWEQTLQFRLRAPELVLVRFVVEDYD 423
Cdd:pfam00168   2 RLTVTVIEAKNLPPKD---GNGTSDPYVKVYLL----DGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYD 74

                          90       100
                  ....*....|....*....|....*.
gi 1039738371 424 TTSPNDFVGQSTLPLSSLKQGYRHIH 449
Cdd:pfam00168  75 RFGRDDFIGEVRIPLSELDSGEGLDG 100
 
Name Accession Description Interval E-value
PI-PLCc_delta3 cd08630
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily ...
 20-314 9.05e-176

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: 493.00  E-value: 9.05e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08630     2 QDMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSQNPEELPSPEQLKGRILVKGKKLpaarsedgrils 179
Cdd:cd08630    82 HAFTASPYPVILSLENHCGLEQQAAMARHLQTILGDMLVTQPLDSLNPEELPSPEELKGRVLVKGKKL------------ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsrakQISPELSALAVYCCATRLRTLDPSPGPPQSCTVGSLSERKARKFTREAGTSFVR 259
Cdd:cd08630   150 --------------------------QISPELSALAVYCQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFVR 203

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039738371 260 HNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08630   204 HNARQLTRVYPLGLRMNSANYSPQEMWNSGCQLVALNFQTPGYEMDLNAGRFLVN 258
PI-PLCc_delta cd08593
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta; This subfamily ...
 20-314 1.68e-167

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: 471.82  E-value: 1.68e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08593     2 QDMTQPLSHYFIASSHNTYLLEDQLKGPSSTEAYIRALKKGCRCVELDCWDGPDGEPIIYHGHTLTSKILFKDVIQAIRE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSqNPEELPSPEQLKGRILVKGKKLpaarsedgrils 179
Cdd:cd08593    82 YAFKVSPYPVILSLENHCSVEQQKVMAQHLKSILGDKLLTQPLDG-VLTALPSPEELKGKILVKGKKL------------ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsrakQISPELSALAVYCCATRLRTLDPSPGPPQSCTVGSLSERKARKFTREAGTSFVR 259
Cdd:cd08593   149 --------------------------KLAKELSDLVIYCKSVHFKSFEHSKENYHFYEMSSFSESKALKLAQESGNEFVR 202

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039738371 260 HNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08593   203 HNKRQLSRIYPAGLRTDSSNYDPQEMWNVGCQIVALNFQTPGEEMDLNDGLFRQN 257
PI-PLCc_eukaryota cd08558
Catalytic domain of eukaryotic phosphoinositide-specific phospholipase C and similar proteins; ...
 20-314 2.55e-143

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: 409.15  E-value: 2.55e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08558     2 QDMTQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDGPDGEPVVYHGHTLTSKILFKDVIEAIKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSqNPEELPSPEQLKGRILVKGKKlpaarsedgrils 179
Cdd:cd08558    82 YAFVTSPYPVILSLENHCSLEQQKKMAQILKEIFGDKLLTPPLDE-NPVQLPSPEQLKGKILIKGKK------------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsrakqispelsalaVYCCatrlrtldpspgppqsctvgSLSERKARKFTREAGTSFVR 259
Cdd:cd08558   148 ------------------------------------YHMS--------------------SFSETKALKLLKESPEEFVK 171

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039738371 260 HNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08558   172 YNKRQLSRVYPKGTRVDSSNYNPQPFWNAGCQMVALNYQTPDLPMQLNQGKFEQN 226
PI-PLCc_delta4 cd08631
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4; This subfamily ...
 20-314 3.16e-130

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: 377.37  E-value: 3.16e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08631     2 QDMTQPLCHYFICSSHNTYLMEDQLRGQSSVEGYIRALKRGCRCVEVDVWDGPNGEPIVYHGHTFTSKILFKDVVAAVAQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSQNPEELPSPEQLKGRILVKGKKLpaarsedgrils 179
Cdd:cd08631    82 YAFQVSDYPVILSLENHCGVEQQQTMAQHLTEILGEKLLSTTLDGVLPTQLPSPEELRGKILLKGKKI------------ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsrakQISPELSALAVYCCATRLRTLDPSPGPPQSCTVGSLSERKARKFTREAGTSFVR 259
Cdd:cd08631   150 --------------------------RLSPELSDCVIYCKSVSFRSFTHSREHYHFYEISSFTETKARKLIREAGNEFVQ 203

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039738371 260 HNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08631   204 HNTWQLSRVYPSGLRTDSSNYNPQEMWNAGCQMVALNFQTAGLEMDLNDGLFRQN 258
PI-PLCc_delta1 cd08629
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily ...
 20-314 1.51e-129

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: 375.53  E-value: 1.51e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08629     2 QDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTFTSKILFCDVLRAIRD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSQNpEELPSPEQLKGRILVKGKKLPAARsedgrils 179
Cdd:cd08629    82 YAFKASPYPVILSLENHCSLEQQRVMARHLRAILGPILLDQPLDGVT-TSLPSPEQLKGKILLKGKKLKLVP-------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsrakqispELSALAVYCCATRLRTL-DPSPGPPQSCTVGSLSERKARKFTREAGTSFV 258
Cdd:cd08629   153 ------------------------------ELSDMIIYCKSVHFGGFsSPGTSGQAFYEMASFSESRALRLLQESGNGFV 202

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738371 259 RHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08629   203 RHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDN 258
PI-PLCc_PRIP_metazoa cd08597
Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein; This ...
 20-314 3.38e-117

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: 344.40  E-value: 3.38e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08597     2 QDMTQPLSHYFIASSHNTYLIEDQLRGPSSVEGYVRALQRGCRCVELDCWDGPNGEPVIYHGHTLTSKISFRSVIEAINE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDsQNPEELPSPEQLKGRILVKGKKLpaarsedGRIls 179
Cdd:cd08597    82 YAFVASEYPLILCIENHCSEKQQLVMAQYLKEIFGDKLYTEPPN-EGESYLPSPHDLKGKIIIKGKKL-------KRR-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsrakQISPELSALAVYCCATRLRTLDPSPGPPQSCTVGSLSERKARKFTREAGTSFVR 259
Cdd:cd08597   152 --------------------------KLCKELSDLVSLCKSVRFQDFPTSAQNQKYWEVCSFSENLARRLANEFPEDFVN 205

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039738371 260 HNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08597   206 YNKKFLSRVYPSPMRVDSSNYNPQDFWNCGCQIVAMNYQTPGLMMDLNTGKFLEN 260
PI-PLCc_gamma cd08592
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma; This family ...
 20-314 8.83e-109

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: 321.68  E-value: 8.83e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08592     2 QDMNNPLSHYWIASSHNTYLTGDQLSSESSLEAYARCLRMGCRCIELDCWDGPDGMPIIYHGHTLTSKIKFMDVLKTIKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDsQNPEELPSPEQLKGRILVKGKKLpaarsedgrils 179
Cdd:cd08592    82 HAFVTSEYPVILSIENHCSLPQQRNMAQAFKEVFGDMLLTQPVD-RNADQLPSPNQLKRKIIIKHKKL------------ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsrAKQISpelsalavyccatrlrtldpspgppqsctvgSLSERKARK-FTREAGTSFV 258
Cdd:cd08592   149 ------------------------FYEMS-------------------------------SFPETKAEKyLNRQKGKIFL 173

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738371 259 RHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08592   174 KYNRRQLSRVYPKGQRVDSSNYDPVPMWNCGSQMVALNFQTPDKPMQLNQALFMLN 229
PI-PLCc_zeta cd08595
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta; This family ...
 20-314 6.81e-107

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: 318.03  E-value: 6.81e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08595     2 QDMDHPLSDYFISSSHNTYLVSDQLVGPSDLDGYVSALRKGCRCLEIDCWDGADNEPVVYHGYTLTSKILFKEVITTVEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSQNPEELPSPEQLKGRILVKGKklpaarsedgrils 179
Cdd:cd08595    82 YAFEKSDYPVVLSLENHCSTEQQEIMAHYLVSILGEKLLRAPIDDPATGELPSPEALKFKILVKNK-------------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsraKQISPELSALAVYCCATRLRTLDPSPGPPQSCTVGSLSERKARKFTREAGTSFVR 259
Cdd:cd08595   148 -------------------------KKIAKALSDLVIYTKSEKFCSFTHSRDNQHSYENNSIGENKARKLLKSSGADFVG 202

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039738371 260 HNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08595   203 HTQRFITRIYPKGTRASSSNYNPQEFWNVGCQMVALNFQTLGAPMDLQNGKFLDN 257
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
 20-314 1.01e-105

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: 315.05  E-value: 1.01e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPG--GEPVIYHGHTLTSKILFRDVIQAV 97
Cdd:cd08591     2 QDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGedEEPIITHGKTMCTEILFKDVIEAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  98 RDHAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSqNPEE----LPSPEQLKGRILVKGKKlpaarse 173
Cdd:cd08591    82 AETAFKTSEYPVILSFENHCSSKQQAKMAEYCREIFGDLLLTEPLEK-YPLEpgvpLPSPNDLKRKILIKNKK------- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 174 dgrilsdreeeeeeeeeaeealeaaeqrsrakqispeLSALAVYCCATRLRTLDPSPGPPQSCTVGSLSERKARKFTREA 253
Cdd:cd08591   154 -------------------------------------LSSLVNYIQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKS 196

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039738371 254 GTSFVRHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08591   197 PIEFVNYNKRQLSRIYPKGTRVDSSNYMPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYN 257
PI-PLC1c_yeast cd08598
Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This ...
 20-311 1.09e-104

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: 311.10  E-value: 1.09e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08598     2 EDLSRPLNEYFISSSHNTYLLGRQLAGDSSVEGYIRALQRGCRCVEIDVWDGDDGEPVVTHGYTLTSSVPFRDVCRAIKK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSqNPEELPSPEQLKGRILVKGKKlpaarsedgrils 179
Cdd:cd08598    82 YAFVTSPYPLILSLEVHCDAEQQERMVEIMKETFGDLLVTEPLDG-LEDELPSPEELRGKILIKVKK------------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsrakqispelsalavyccatrlrtldpSPGPPQSCTvgSLSERKARKFTREAGTSFVR 259
Cdd:cd08598   148 -------------------------------------------------ESKTPNHIF--SLSERSLLKLLKDKRAALDK 176

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039738371 260 HNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRF 311
Cdd:cd08598   177 HNRRHLMRVYPSGTRISSSNFNPLPFWRAGVQMVALNWQTYDLGMQLNEAMF 228
PI-PLCc_eta cd08594
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta; This family ...
 20-314 5.90e-100

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: 299.02  E-value: 5.90e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08594     2 QDMTQPLSHYFIASSHNTYLTGDQLLSQSRVDMYARVLQAGCRCVEVDCWDGPDGEPVVHHGYTLTSKILFRDVIETINK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSQNPEELPSPEQLKGRILVKGKKlpaarsedgrils 179
Cdd:cd08594    82 YAFIKNEYPVILSIENHCSVQQQKKMAQYLKEILGDKLDLSSVISGDSKQLPSPQSLKGKILIKGKK------------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsrakqispelsalavyccatrlrtldpspgppqsCTVGSLSERKARKFTREAGTSFVR 259
Cdd:cd08594   149 --------------------------------------------------------WQVSSFSETRAHQIVQQKAAQFLR 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039738371 260 HNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08594   173 FNQRQLSRIYPSAYRIDSSNFNPQPYWNAGCQLVALNYQTEGRMLQLNRAKFRAN 227
PI-PLCc_eta1 cd08632
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily ...
 20-314 5.75e-95

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: 287.31  E-value: 5.75e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08632     2 QDMDQPLCNYFIASSHNTYLTGDQLLSQSKVDMYARVLQAGCRCVEVDCWDGPDGEPVVHHGYTLTSKITFRDVIETINK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSQNPEELPSPEQLKGRILVKGKKLpaarsedgrils 179
Cdd:cd08632    82 YAFVKNEFPVILSIENHCSIQQQKKIAQYLKEIFGDKLDLSSVLTGDPKQLPSPQLLKGKILVKGKKL------------ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsrakqiSPELSALAVYCCATRLRTL--DPSPgppqsCTVGSLSERKARKFTREAGTSF 257
Cdd:cd08632   150 ----------------------------CRDLSDLVVYTNSVAAQDIvdDGST-----GNVLSFSETRAHQLVQQKAEQF 196

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738371 258 VRHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08632   197 MTYNQKQLTRIYPSAYRIDSSNFNPLPYWNVGCQLVALNYQSEGRMMQLNRAKFMVN 253
PI-PLCc_eta2 cd08633
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily ...
 20-314 1.14e-94

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: 286.55  E-value: 1.14e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08633     2 QDMTQPLSHYFITSSHNTYLSGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDGPDGEPIVHHGYTLTSKILFKDVIETINK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSQNPEELPSPEQLKGRILVKGKKLpaarsedgrils 179
Cdd:cd08633    82 YAFIKNEYPVILSIENHCSVPQQKKMAQYLTEILGDKLDLSSVISNDCTRLPSPEILKGKILVKGKKL------------ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrSRAkqispeLSALAVYccATRLRTLDPSPGPPQSCTVGSLSERKARKFTREAGTSFVR 259
Cdd:cd08633   150 ----------------------SRA------LSDLVKY--TKSVRVHDIETEATSSWQVSSFSETKAHQILQQKPAQYLR 199

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039738371 260 HNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08633   200 FNQRQLSRIYPSSYRVDSSNYNPQPFWNAGCQMVALNYQSEGRMLQLNRAKFSAN 254
PI-PLCc_gamma2 cd08628
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2; This subfamily ...
 20-314 5.44e-94

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: 285.03  E-value: 5.44e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08628     2 QDMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRMGCRCIELDCWDGPDGKPIIYHGWTRTTKIKFDDVVQAIKD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSQnPEELPSPEQLKGRILVKGKKLpaarsedgrils 179
Cdd:cd08628    82 HAFVTSEYPVILSIEEHCSVEQQRHMAKVFKEVFGDKLLMKPLEAS-ADQLPSPTQLKEKIIIKHKKL------------ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsrakqISPELSALAVYCCATRlRTLDPSPGPPQScTVGSLSERKARKFTREAGTSFVR 259
Cdd:cd08628   149 ---------------------------IAIELSDLVVYCKPTS-KTKDNLENPDFK-EIRSFVETKAPSIIRQKPVQLLK 199

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039738371 260 HNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08628   200 YNRKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTADKYMQLNHALFSLN 254
PI-PLCc_epsilon cd08596
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon; This family ...
 20-314 5.99e-91

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: 277.12  E-value: 5.99e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08596     2 EDLQYPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLTGCRCVELDCWDGDDGMPIIYHGHTLTTKIPFKDVVEAINR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQAL---DSQNPEELPSPEQLKGRILVKGKKlpaarsedgr 176
Cdd:cd08596    82 SAFITSDYPVILSIENHCSLQQQRKMAEIFKTVFGEKLVTKFLfesDFSDDPSLPSPLQLKNKILLKNKK---------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 177 ilsdreeeeeeeeeaeealeaaeqrsrakqiSPELSALAVYCCATRLRTLDpspgPPQSCTVGSLSERKARKFTREAGTS 256
Cdd:cd08596   152 -------------------------------APELSDLVIYCQAVKFPGLS----TPKCYHISSLNENAAKRLCRRYPQK 196

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738371 257 FVRHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08596   197 LVQHTRCQLLRTYPAATRIDSSNPNPLIFWLHGLQLVALNYQTDDLPMHLNAAMFEAN 254
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 22-164 6.99e-90

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: 270.15  E-value: 6.99e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  22 MGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRDHA 101
Cdd:pfam00388   1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDGPDGEPVVYHGYTLTSKIPFRDVLEAIKDYA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738371 102 FTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDsQNPEELPSPEQLKGRILVKG 164
Cdd:pfam00388  81 FVTSPYPVILSLENHCSPEQQKKMAEILKEIFGDMLYTPPLD-DDLTELPSPEDLKGKILIKG 142
PI-PLCc_beta4 cd08626
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4; This subfamily ...
 20-314 9.71e-90

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: 273.95  E-value: 9.71e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPG--GEPVIYHGHTLTSKILFRDVIQAV 97
Cdd:cd08626     2 QDMDQPLAHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCIELDCWDGKGedQEPIITHGKAMCTDILFKDVIQAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  98 RDHAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSQNPE---ELPSPEQLKGRILVKGKKlpaarsed 174
Cdd:cd08626    82 KDTAFVTSDYPVILSFENHCSKPQQYKLAKYCEEIFGDLLLTKPLESHPLEpgvPLPSPNKLKRKILIKNKR-------- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 175 grilsdreeeeeeeeeaeealeaaeqrsrakqispeLSALAVYCCATRLRTLDPSPGPPQSCTVGSLSERKARKFTREAG 254
Cdd:cd08626   154 ------------------------------------LSSLVNYAQPVKFQGFDVAEERNIHFNMSSFNESVGLGYLKTSA 197

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 255 TSFVRHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08626   198 IEFVNYNKRQMSRIYPKGTRVDSSNYMPQIFWNAGCQMVSLNFQTPDLGMQLNQGKFEYN 257
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 20-314 5.87e-88

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: 269.62  E-value: 5.87e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEG--PGGEPVIYHGHTLTSKILFRDVIQAV 97
Cdd:cd08624     2 QDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGkpPDEEPIITHGFTMTTEILFKDAIEAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  98 RDHAFTSSPYPVILSLENHC-GLEQQAVMARHLRSILGDMLVTQALDS---QNPEELPSPEQLKGRILVKGKKLPaarse 173
Cdd:cd08624    82 AESAFKTSPYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKyplKPGVPLPSPEDLRGKILIKNKKYE----- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 174 dgrilsdreeeeeeeeeaeealeaaeqrsrakqispELSALAVYCCATRLRTLDPSPGPPQSCTVGSLSERKARKFTREA 253
Cdd:cd08624   157 ------------------------------------EMSSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKA 200

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039738371 254 GTSFVRHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08624   201 SVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQTMDLPMQQNMALFEFN 261
PI-PLCc_gamma1 cd08627
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily ...
 20-314 8.22e-88

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: 268.05  E-value: 8.22e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08627     2 EEMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSqNPEELPSPEQLKGRILVKGKKLPAARSedgrils 179
Cdd:cd08627    82 HAFVTSEYPIILSIEDHCSIVQQRNMAQHFKKVFGDMLLTKPVDI-NADGLPSPNQLKRKILIKHKKLYRDMS------- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsrakqispelsalavyccatrlrtldpspgppqsctvgSLSERKARKF-TREAGTSFV 258
Cdd:cd08627   154 ------------------------------------------------------------SFPETKAEKYvNRSKGKKFL 173

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738371 259 RHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08627   174 QYNRRQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMLG 229
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
 21-314 2.22e-82

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: 255.36  E-value: 2.22e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  21 DMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEG--PGGEPVIYHGHTLTSKILFRDVIQAVR 98
Cdd:cd08625     3 DMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGrpPEEEPFITHGFTMTTEIPFKDVIEAIA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  99 DHAFTSSPYPVILSLENHC-GLEQQAVMARHLRSILGDMLVTQALDS---QNPEELPSPEQLKGRILVKGKKlpaarsed 174
Cdd:cd08625    83 ESAFKTSPYPVILSFENHVdSAKQQAKMAEYCRSIFGDALLIDPLDKyplVPGVQLPSPQELMGKILVKNKK-------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 175 grilsdreeeeeeeeeaeealeaaeqrsrakqispeLSALAVYCCATRLRTLDPSPGPPQSCTVGSLSERKARKFTREAG 254
Cdd:cd08625   155 ------------------------------------MSTLVNYIEPVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSP 198

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 255 TSFVRHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08625   199 MEFVEYNKKQLSRIYPKGTRVDSSNYMPQLFWNVGCQMVALNFQTLDLAMQLNMGVFEYN 258
PLN02952 PLN02952
phosphoinositide phospholipase C
 20-465 3.77e-81

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 263.01  E-value: 3.77e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPV-IYHGHTLTSKILFRDVIQAVR 98
Cdd:PLN02952  123 HDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGSTKDEIlVLHGRTLTTPVPLIKCLKSIR 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  99 DHAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSQnpEELPSPEQLKGRILVKGK------------- 165
Cdd:PLN02952  203 DYAFSSSPYPVIITLEDHLTPDLQAKVAEMATQIFGQMLYYPESDSL--VQFPSPESLKHRIIISTKppkeylessgpiv 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 166 -KLPAARSEDGRILSDREEEEEEEEEAEEALEAAeQRSRAKQISPELSALA--VYccaTRLRTLdpSPGPPQSCTVG--- 239
Cdd:PLN02952  281 iKKKNNVSPSGRNSSEETEEAQTLESMLFEQEAD-SRSDSDQDDNKSGELQkpAY---KRLITI--HAGKPKGTLKDamk 354

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 240 ---------SLSERKARKFTREAGTSFVRHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGR 310
Cdd:PLN02952  355 vavdkvrrlSLSEQELEKAATTNGQDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGAQMIAFNMQGYGKSLWLMHGM 434

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 311 FLINGQCGYVLKPAYLRQL---NTTFDPECPGPPRTTLAIQVLTAQ------QLPKLNAEKPSsivDPLVRVEIHGVPED 381
Cdd:PLN02952  435 FRANGGCGYLKKPDFLMKKgfhDEVFDPKKKLPVKKTLKVKVYLGDgwrldfSHTHFDSYSPP---DFYTKMYIVGVPAD 511

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 382 CAQKETDYVLNNgFNPCWEQTLQFRLRAPELVLVRFVVEDYDTTSPNDFVGQSTLPLSSLKQGYRHIHLLSKDGASLAPA 461
Cdd:PLN02952  512 NAKKKTKIIEDN-WYPAWNEEFSFPLTVPELALLRIEVREYDMSEKDDFGGQTCLPVSELRPGIRSVPLHDKKGEKLKNV 590


                  ....
gi 1039738371 462 TLFV 465
Cdd:PLN02952  591 RLLM 594
PLN02228 PLN02228
Phosphoinositide phospholipase C
 20-465 1.86e-80

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 259.97  E-value: 1.86e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGG-EPVIYHGHTLTSKILFRDVIQAVR 98
Cdd:PLN02228  106 HDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWPNPSGnAAEVRHGRTLTSHEDLQKCLNAIK 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  99 DHAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTqaLDSQNPEELPSPEQLKGRILVKGKK----LPAARSED 174
Cdd:PLN02228  186 DNAFQVSDYPVVITLEDHLPPNLQAQVAKMLTKTFRGMLFR--CTSESTKHFPSPEELKNKILISTKPpkeyLESKTVQT 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 175 GRilSDREEEEEEEEEAEEALEAAEQRSRAKQISPELSALAVYCCATRLRTL-DPSPGPPQSCTVGSLSERKARKFTREA 253
Cdd:PLN02228  264 TR--TPTVKETSWKRVADAENKILEEYKDEESEAVGYRDLIAIHAANCKDPLkDCLSDDPEKPIRVSMDEQWLETMVRTR 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 254 GTSFVRHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLINGQCGYVLKPAYLRQLNTTF 333
Cdd:PLN02228  342 GTDLVRFTQRNLVRIYPKGTRVDSSNYDPHVGWTHGAQMVAFNMQGHGKQLWIMQGMFRANGGCGYVKKPRILLDEHTLF 421

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 334 DPECPGPPRTTLAIQVLTAQ----QLPKLNAEKPSSiVDPLVRVEIHGVPEDCAQKETDYVLNNGFnPCW-EQTLQFRLR 408
Cdd:PLN02228  422 DPCKRLPIKTTLKVKIYTGEgwdlDFHLTHFDQYSP-PDFFVKIGIAGVPRDTVSYRTETAVDQWF-PIWgNDEFLFQLR 499

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738371 409 APELVLVRFVVEDYDTTSPNDFVGQSTLPLSSLKQGYRHIHLLSKDGASLAPATLFV 465
Cdd:PLN02228  500 VPELALLWFKVQDYDNDTQNDFAGQTCLPLPELKSGVRAVRLHDRAGKAYKNTRLLV 556
PI-PLCc_plant cd08599
Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family ...
 20-314 8.24e-76

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: 237.27  E-value: 8.24e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:cd08599     2 HDMTAPLSHYFIFSSHNSYLTGNQLSSRSSTAPIIEALLRGCRVIELDLWPGGRGDICVLHGGTLTKPVKFEDCIKAIKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQaLDSQNPEELPSPEQLKGRILVKgKKLPAARSedgrils 179
Cdd:cd08599    82 NAFTASEYPVIITLENHLSPELQAKAAQILRETLGDKLFYP-DSEDLPEEFPSPEELKGKILIS-DKPPVIRN------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 180 dreeeeeeeeeaeealeaaeqrsrakqispelsalavyccatrlrtldpspgppqsctvgSLSERKARKFTR-EAGTSFV 258
Cdd:cd08599   153 ------------------------------------------------------------SLSETQLKKVIEgEHPTDLI 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738371 259 RHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08599   173 EFTQKNLLRVYPAGLRITSSNYDPMLAWMHGAQMVALNMQGYDRPLWLNRGKFRAN 228
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 22-165 4.61e-75

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: 232.17  E-value: 4.61e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371   22 MGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRDHA 101
Cdd:smart00148   1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDGPDGEPVIYHGHTFTLPIKLSEVLEAIKDFA 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738371  102 FTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSqNPEELPSPEQLKGRILVKGK 165
Cdd:smart00148  81 FVTSPYPVILSLENHCSPDQQAKMAQMFKEIFGDMLYTPPLTS-SLEVLPSPEQLRGKILLKVR 143
PLN02222 PLN02222
phosphoinositide phospholipase C 2
 20-467 5.45e-73

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 241.09  E-value: 5.45e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPV-IYHGHTLTSKILFRDVIQAVR 98
Cdd:PLN02222  103 HDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSDKDDIdVLHGMTLTTPVGLIKCLKAIR 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  99 DHAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALdSQNPEELPSPEQLKGRILVKGK---KLPAARSED- 174
Cdd:PLN02222  183 AHAFDVSDYPVVVTLEDHLTPDLQSKVAEMVTEIFGEILFTPPV-GESLKEFPSPNSLKKRIIISTKppkEYKEGKDDEv 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 175 -------------GR-----ILSDREEEEEEEEEAEEALEAAEQRSRAKQISPELSAL-AVYCCATRLRTLDPSPGPPQS 235
Cdd:PLN02222  262 vqkgkdlgdeevwGRevpsfIQRNKSVDKNDSNGDDDDDDDDGEDKSKKNAPPQYKHLiAIHAGKPKGGITECLKVDPDK 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 236 CTVGSLSERKARKFTREAGTSFVRHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLING 315
Cdd:PLN02222  342 VRRLSLSEEQLEKAAEKYAKQIVRFTQHNLLRIYPKGTRVTSSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANG 421

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 316 QCGYVLKPAYLRQLNTT---FDPECPGPPRTTLAIQVLTAQ----QLPKLNAEKPSSiVDPLVRVEIHGVPEDCAQKETD 388
Cdd:PLN02222  422 GCGYIKKPDLLLKSGSDsdiFDPKATLPVKTTLRVTIYMGEgwyfDFRHTHFDQYSP-PDFYTRVGIAGVPGDTVMKKTK 500

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738371 389 yVLNNGFNPCWEQTLQFRLRAPELVLVRFVVEDYDTTSPNDFVGQSTLPLSSLKQGYRHIHLLSKDGASLAPATLFVHI 467
Cdd:PLN02222  501 -TLEDNWIPAWDEVFEFPLTVPELALLRLEVHEYDMSEKDDFGGQTCLPVWELSQGIRAFPLHSRKGEKYKSVKLLVKV 578
PI-PLCc_beta1 cd08623
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1; This subfamily ...
 20-314 1.40e-72

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: 229.97  E-value: 1.40e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGG--EPVIYHGHTLTSKILFRDVIQAV 97
Cdd:cd08623     2 EDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAeeEPVITHGFTMTTEISFKEVIEAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  98 RDHAFTSSPYPVILSLENHC-GLEQQAVMARHLRSILGDMLVTQALDSQNPEE---LPSPEQLKGRILVKGKKlpaarse 173
Cdd:cd08623    82 AECAFKTSPFPILLSFENHVdSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESgvpLPSPMDLMYKILVKNKK------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 174 dgrilsdreeeeeeeeeaeealeaaeqrsrakqispeLSALAVYCCATRLRTLDPSPGPPQSCTVGSLSERKARKFTREA 253
Cdd:cd08623   155 -------------------------------------MSNLVNYIQPVKFESFEASKKRNKSFEMSSFVETKGLEQLTKS 197

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039738371 254 GTSFVRHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd08623   198 PVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTVDLSMQINMGMYEYN 258
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 20-314 7.65e-70

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: 223.30  E-value: 7.65e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQI-----GGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTsKILFRDVI 94
Cdd:cd00137     2 HPDTQPLAHYSIPGTHDTYLTAGQFtikqvWGLTQTEMYRQQLLSGCRCVDIRCWDGKPEEPIIYHGPTFL-DIFLKEVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  95 QAVRDHAFTSSPYPVILSLENHCGL--EQQAVMARHLRSILGDMLVTQALDSQNPeeLPSPEQLKGRILVKGKKL----P 168
Cdd:cd00137    81 EAIAQFLKKNPPETIIMSLKNEVDSmdSFQAKMAEYCRTIFGDMLLTPPLKPTVP--LPSLEDLRGKILLLNKKNgfsgP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 169 AARSEDGRILSDREeeeeeeeeaeealeaaeqrSRAKQISPELSalavyccatrlrTLDPSPGPpqsctvgslseRKARK 248
Cdd:cd00137   159 TGSSNDTGFVSFEF-------------------STQKNRSYNIS------------SQDEYKAY-----------DDEKV 196

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738371 249 FTREAGTSFVRHNTQQLTRVYPLGLR---------MNSANYNPQEMWN---SGCQLVALNFQTPGYEMDLNTGRFLIN 314
Cdd:cd00137   197 KLIKATVQFVDYNKNQLSRNYPSGTSggtawyyyaMDSNNYMPQMFWNanpAGCGIVILDFQTMDLPMQQYMAVIEFN 274
PLN02230 PLN02230
phosphoinositide phospholipase C 4
 20-465 9.06e-64

phosphoinositide phospholipase C 4


Pssm-ID: 177875 [Multi-domain]  Cd Length: 598  Bit Score: 216.88  E-value: 9.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRD 99
Cdd:PLN02230  115 QNMDAPLSHYFIFTGHNSYLTGNQLSSNCSELPIADALRRGVRVVELDLWPRGTDDVCVKHGRTLTKEVKLGKCLDSIKA 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 100 HAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQalDSQNPEELPSPEQLKGRILVKGKK----LPA--ARSE 173
Cdd:PLN02230  195 NAFAISKYPVIITLEDHLTPKLQFKVAKMITQTFGDMLYYH--DSEGCQEFPSPEELKEKILISTKPpkeyLEAndAKEK 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 174 DG-----------------RILSDREEEEEEEEEAEEALEAAEQRSRAKQ-ISPELSAlAVYCCATRLRTLDPSPG---- 231
Cdd:PLN02230  273 DNgekgkdsdedvwgkepeDLISTQSDLDKVTSSVNDLNQDDEERGSCESdTSCQLQA-PEYKRLIAIHAGKPKGGlrma 351

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 232 ---PPQSCTVGSLSERKARKFTREAGTSFVRHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNT 308
Cdd:PLN02230  352 lkvDPNKIRRLSLSEQLLEKAVASYGADVIRFTQKNFLRIYPKGTRFNSSNYKPQIGWMSGAQMIAFNMQGYGRALWLME 431

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 309 GRFLINGQCGYVLKPAYLRQLNTT---FDPECPGPPRTTLAIQVLTAQ------QLPKLNAEKPSsivDPLVRVEIHGVP 379
Cdd:PLN02230  432 GMFRANGGCGYVKKPDFLMDAGPNgqdFYPKDNSCPKKTLKVKVCMGDgwlldfKKTHFDSYSPP---DFFVRVGIAGAP 508

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 380 EDCAQKETDyVLNNGFNPCWEQTLQFRLRAPELVLVRFVVEDYDTTSPNDFVGQSTLPLSSLKQGYRHIHLLSKDGASLA 459
Cdd:PLN02230  509 VDEVMEKTK-IEYDTWTPIWNKEFIFPLAVPELALLRVEVHEHDINEKDDFGGQTCLPVSEIRQGIHAVPLFNRKGVKYS 587


                  ....*.
gi 1039738371 460 PATLFV 465
Cdd:PLN02230  588 STRLLM 593
PI-PLC-Y pfam00387
Phosphatidylinositol-specific phospholipase C, Y domain; This associates with pfam00388 to ...
 211-325 1.33e-54

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


Pssm-ID: 459794  Cd Length: 114  Bit Score: 178.04  E-value: 1.33e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 211 LSALAVYCCATRLRTLD-PSPGPPQSCTvgSLSERKARKFTREAGTSFVRHNTQQLTRVYPLGLRMNSANYNPQEMWNSG 289
Cdd:pfam00387   1 LSDLVVYTQSVKFKSFStPESKTPNHIF--SFSESKALKLIKSSSAAFVKHNRRHLMRVYPKGTRVDSSNFNPQPFWNCG 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039738371 290 CQLVALNFQTPGYEMDLNTGRFLINGQCGYVLKPAY 325
Cdd:pfam00387  79 VQMVALNWQTPDEGMQLNEGMFADNGGCGYVLKPEF 114
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 343-470 2.04e-53

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: 175.42  E-value: 2.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 343 TTLAIQVLTAQQLPKLNAEKpSSIVDPLVRVEIHGVPE-DCAQKETDYVLNNGFNPCWEQTLQFRLRAPELVLVRFVVED 421
Cdd:cd00275     2 LTLTIKIISGQQLPKPKGDK-GSIVDPYVEVEIHGLPAdDSAKFKTKVVKNNGFNPVWNETFEFDVTVPELAFLRFVVYD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1039738371 422 YDTTSpNDFVGQSTLPLSSLKQGYRHIHLLSKDGASLAPATLFVHIRIQ 470
Cdd:cd00275    81 EDSGD-DDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
PLN02223 PLN02223
phosphoinositide phospholipase C
 20-468 2.03e-46

phosphoinositide phospholipase C


Pssm-ID: 165867 [Multi-domain]  Cd Length: 537  Bit Score: 168.66  E-value: 2.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  20 QDMGQPLAHYFISSSHNTYLTDSQI-GGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVR 98
Cdd:PLN02223  106 HDMHAPLSHYFIHTSLKSYFTGNNVfGKLYSIEPIIDALEQGVRVVELDLLPDGKDGICVRPKWNFEKPLELQECLDAIK 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  99 DHAFTSSP-YPVILSLENHCGLEQQAVMARHLRSILGDMlVTQALDSQNPEELPSPEQLKGRILVK---GKKLPAARSED 174
Cdd:PLN02223  186 EHAFTKCRsYPLIITFKDGLKPDLQSKATQMIDQTFGDM-VYHEDPQHSLEEFPSPAELQNKILISrrpPKELLYAKADD 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 175 GRIlsdreeeeeeeeeAEEALEAAEQRSRAKQISpelSALAVYCCATRLRTLDPSPGPPQSCTVGSLSERKARKFTREag 254
Cdd:PLN02223  265 GGV-------------GVRNELEIQEGPADKNYQ---SLVGFHAVEPRGMLQKALTGKADDIQQPGWYERDIISFTQK-- 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 255 tSFVRhntqqlTRVYPLGLRMNsANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLINGQCGYVLKPAYLRQLNTT-- 332
Cdd:PLN02223  327 -KFLR------TRPKKKNLLIN-APYKPQRAWMHGAQLIALSRKDDKEKLWLMQGMFRANGGCGYVKKPDFLLNAGPSgv 398

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 333 FDPECPGPPRTTLAIQVLTA--------QQLPKLNaeKPssivDPLVRVEIHGVPEDCAQKETDyVLNNGFNPCWEQTLQ 404
Cdd:PLN02223  399 FYPTENPVVVKILKVKIYMGdgwivdfkKRIGRLS--KP----DLYVRISIAGVPHDEKIMKTT-VKNNEWKPTWGEEFT 471

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738371 405 FRLRAPELVLVRFVVEDYDTTSPNDFVGQSTLPLSSLKQGYRHIHLLSKDGASLAPATLFVHIR 468
Cdd:PLN02223  472 FPLTYPDLALISFEVYDYEVSTADAFCGQTCLPVSELIEGIRAVPLYDERGKACSSTMLLTRFK 535
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 240-326 5.63e-46

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: 155.47  E-value: 5.63e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  240 SLSERKARKFTREAGTSFVRHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLINGQCGY 319
Cdd:smart00149  29 SFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQMVALNFQTPDKPMQLNQGMFRANGGCGY 108


                   ....*..
gi 1039738371  320 VLKPAYL 326
Cdd:smart00149 109 VLKPDFL 115
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 33-137 8.23e-25

Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases superfamily; The PI-PLC-like phosphodiesterases superfamily represents the catalytic domains of bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11), glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.41) from spider venom, SMases D-like proteins, and phospholipase D (PLD) from several pathogenic bacteria, as well as their uncharacterized homologs found in organisms ranging from bacteria and archaea to metazoans, plants, and fungi. PI-PLCs are ubiquitous enzymes hydrolyzing the membrane lipid phosphoinositides to yield two important second messengers, inositol phosphates and diacylglycerol (DAG). GP-GDEs play essential roles in glycerol metabolism and catalyze the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols that are major sources of carbon and phosphate. Both, PI-PLCs and GP-GDEs, can hydrolyze the 3'-5' phosphodiester bonds in different substrates, and utilize a similar mechanism of general base and acid catalysis with conserved histidine residues, which consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This superfamily also includes Neurospora crassa ankyrin repeat protein NUC-2 and its Saccharomyces cerevisiae counterpart, Phosphate system positive regulatory protein PHO81, glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs). The residues essential for enzyme activities and metal binding are not conserved in these sequence homologs, which might suggest that the function of catalytic domains in these proteins might be distinct from those in typical PLC-like phosphodiesterases.


Pssm-ID: 176498 [Multi-domain]  Cd Length: 179  Bit Score: 100.59  E-value: 8.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  33 SSHNTYltdSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLT------SKILFRDVIQAVRDHAFTsSP 106
Cdd:cd08555     2 LSHRGY---SQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDrttagiLPPTLEEVLELIADYLKN-PD 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039738371 107 YPVILSLENHCG----LEQQAVMARHLRSILGDML 137
Cdd:cd08555    78 YTIILSLEIKQDspeyDEFLAKVLKELRVYFDYDL 112
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 344-450 9.23e-19

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: 81.38  E-value: 9.23e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  344 TLAIQVLTAQQLPKLNaekPSSIVDPLVRVEIHGVPEDCAQkeTDYVLNNGfNPCWEQTLQFRLRAPELVLVRFVVEDYD 423
Cdd:smart00239   1 TLTVKIISARNLPPKD---KGGKSDPYVKVSLDGDPKEKKK--TKVVKNTL-NPVWNETFEFEVPPPELAELEIEVYDKD 74

                           90       100
                   ....*....|....*....|....*..
gi 1039738371  424 TTSPNDFVGQSTLPLSSLKQGYRHIHL 450
Cdd:smart00239  75 RFGRDDFIGQVTIPLSDLLLGGRHEKL 101
C2 pfam00168
C2 domain;
344-449 4.12e-16

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 73.89  E-value: 4.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 344 TLAIQVLTAQQLPKLNaekPSSIVDPLVRVEIHgvpeDCAQKETDYVLNNGFNPCWEQTLQFRLRAPELVLVRFVVEDYD 423
Cdd:pfam00168   2 RLTVTVIEAKNLPPKD---GNGTSDPYVKVYLL----DGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYD 74

                          90       100
                  ....*....|....*....|....*.
gi 1039738371 424 TTSPNDFVGQSTLPLSSLKQGYRHIH 449
Cdd:pfam00168  75 RFGRDDFIGEVRIPLSELDSGEGLDG 100
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 345-443 3.62e-11

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: 59.77  E-value: 3.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 345 LAIQVLTAQQLPKLNAEKPSsivDPLVRVEIHGVPedcaQKETDYVLNNgFNPCWEQTLQFRLRAPELVLVRFVVEDYDT 424
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKS---DPYVKVSLGGKQ----KFKTKVVKNT-LNPVWNETFEFPVLDPESDTLTVEVWDKDR 72

                          90
                  ....*....|....*....
gi 1039738371 425 TSPNDFVGQSTLPLSSLKQ 443
Cdd:cd00030    73 FSKDDFLGEVEIPLSELLD 91
C2B_Munc13-like cd04009
C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
 340-441 3.64e-07

C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. 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 third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175976 [Multi-domain]  Cd Length: 133  Bit Score: 49.16  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 340 PPRTTLAIQVLTAQQLPKLnaeKPSSIVDPLVRVEI--HGVPEDCAQKETDyVLNNGFNPCWEQTLQFRL----RAPELV 413
Cdd:cd04009    13 ASEQSLRVEILNARNLLPL---DSNGSSDPFVKVELlpRHLFPDVPTPKTQ-VKKKTLFPLFDESFEFNVppeqCSVEGA 88

                          90       100
                  ....*....|....*....|....*...
gi 1039738371 414 LVRFVVEDYDTTSPNDFVGQSTLPLSSL 441
Cdd:cd04009    89 LLLFTVKDYDLLGSNDFEGEAFLPLNDI 116
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
 345-441 5.51e-07

C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha and gamma. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1(alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. 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-I topology.


Pssm-ID: 175992 [Multi-domain]  Cd Length: 131  Bit Score: 48.41  E-value: 5.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 345 LAIQVLTAQQLPKLNaekPSSIVDPLVRVEIHGVPEDCAQKETDYVLNNgFNPCWEQTLQFRLRaPELVLVRFVVE--DY 422
Cdd:cd04026    15 LTVEVREAKNLIPMD---PNGLSDPYVKLKLIPDPKNETKQKTKTIKKT-LNPVWNETFTFDLK-PADKDRRLSIEvwDW 89

                          90
                  ....*....|....*....
gi 1039738371 423 DTTSPNDFVGQSTLPLSSL 441
Cdd:cd04026    90 DRTTRNDFMGSLSFGVSEL 108
C2A_Synaptotagmin-7 cd08386
C2A domain first repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 328-442 6.33e-07

C2A domain first repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 7, a member of class 2 synaptotagmins, is located in presynaptic plasma membranes in neurons, dense-core vesicles in endocrine cells, and lysosomes in fibroblasts. It has been shown to play a role in regulation of Ca2+-dependent lysosomal exocytosis in fibroblasts and may also function as a vesicular Ca2+-sensor. It is distinguished from the other synaptotagmins by having over 12 splice forms. 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: 176032 [Multi-domain]  Cd Length: 125  Bit Score: 48.09  E-value: 6.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 328 QLNTTFDPECpgpprTTLAIQVLTAQQLPklnAEKPSSIVDPLVRVEIhgVPeDCAQKETDYVLNNGFNPCWEQTLQFRL 407
Cdd:cd08386     6 QFSVSYDFQE-----STLTLKILKAVELP---AKDFSGTSDPFVKIYL--LP-DKKHKLETKVKRKNLNPHWNETFLFEG 74

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1039738371 408 RAPELVLVRFV---VEDYDTTSPNDFVGQSTLPLSSLK 442
Cdd:cd08386    75 FPYEKLQQRVLylqVLDYDRFSRNDPIGEVSLPLNKVD 112
C2B_RasA1_RasA4 cd04025
C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase ...
 344-443 1.39e-06

C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase activating protein 1s ), Ras-specific GAP members, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. Both proteins contain two C2 domains, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding 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. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175991 [Multi-domain]  Cd Length: 123  Bit Score: 47.09  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 344 TLAIQVLTAQQLPKLNAEKPSsivDPLVRVEIHGvpedcAQKETDYVLNNGFnPCWEQTLQFRLRAPELVLVRFVVEDYD 423
Cdd:cd04025     1 RLRCHVLEARDLAPKDRNGTS---DPFVRVFYNG-----QTLETSVVKKSCY-PRWNEVFEFELMEGADSPLSVEVWDWD 71

                          90       100
                  ....*....|....*....|
gi 1039738371 424 TTSPNDFVGQSTLPLSSLKQ 443
Cdd:cd04025    72 LVSKNDFLGKVVFSIQTLQQ 91
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 25-162 1.04e-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: 47.09  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371  25 PLAHYFISSSHNTYltdSQIGGTSSTEAYIRAFAQ----------GCRCVELDCWEGP-GGEPVIYHGHTLTSKILFRDV 93
Cdd:cd08557     8 PLSQLSIPGTHNSY---AYTIDGNSPIVSKWSKTQdlsitdqldaGVRYLDLRVAYDPdDGDLYVCHGLFLLNGQTLEDV 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738371  94 IQAVRDhaFTSS-PY-PVILSLENHCGLEQ----QAVMARhLRSILGDMLV-TQALDSQNP--EELpspeqLKGRILV 162
Cdd:cd08557    85 LNEVKD--FLDAhPSeVVILDLEHEYGGDNgedhDELDAL-LRDVLGDPLYrPPVRAGGWPtlGEL-----RAGKRVL 154
C2B_Synaptotagmin-4 cd08404
C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking ...
 337-447 1.16e-05

C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. 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: 176049 [Multi-domain]  Cd Length: 136  Bit Score: 44.73  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 337 CPGPPRTTLAIQVLTAQQLPKLNAEKPSsivDPLVRVEIHGVPEDCAQKETdYVLNNGFNPCWEQTLQFRLRAPEL--VL 414
Cdd:cd08404     9 CYQPTTNRLTVVVLKARHLPKMDVSGLA---DPYVKVNLYYGKKRISKKKT-HVKKCTLNPVFNESFVFDIPSEELedIS 84

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1039738371 415 VRFVVEDYDTTSPNDFVGQSTLPLSSLKQGYRH 447
Cdd:cd08404    85 VEFLVLDSDRVTKNEVIGRLVLGPKASGSGGHH 117
C2B_Synaptotagmin-17 cd08410
C2 domain second repeat present in Synaptotagmin 17; Synaptotagmin is a membrane-trafficking ...
 340-433 4.66e-04

C2 domain second repeat present in Synaptotagmin 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. 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: 176055 [Multi-domain]  Cd Length: 135  Bit Score: 40.26  E-value: 4.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 340 PPRTTLAIQVLTAQQLPKLNAEKPSsivDPLVRVE-IHGVPEDCAQKETdyVLNNGFNPCWEQTLQFRLRAPEL--VLVR 416
Cdd:cd08410    11 PSAGRLNVDIIRAKQLLQTDMSQGS---DPFVKIQlVHGLKLIKTKKTS--CMRGTIDPFYNESFSFKVPQEELenVSLV 85

                          90
                  ....*....|....*..
gi 1039738371 417 FVVEDYDTTSPNDFVGQ 433
Cdd:cd08410    86 FTVYGHNVKSSNDFIGR 102
C2A_Copine cd04048
C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 368-457 7.54e-04

C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. 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: 176013 [Multi-domain]  Cd Length: 120  Bit Score: 39.47  E-value: 7.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 368 DPLVRVEIHGVPEdcaQKETDY----VLNNGFNPCWEQTLQFRLRAPELVLVRFVVEDYD----TTSPNDFVGQSTLPLS 439
Cdd:cd04048    22 DPFVVVYVKTGGS---GQWVEIgrteVIKNNLNPDFVTTFTVDYYFEEVQKLRFEVYDVDskskDLSDHDFLGEAECTLG 98

                          90       100
                  ....*....|....*....|
gi 1039738371 440 SL--KQGYRhIHLLSKDGAS 457
Cdd:cd04048    99 EIvsSPGQK-LTLPLKGGKG 117
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
 368-450 1.17e-03

C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating protein which regulates the ADP ribosylation factor Arf, a member of the Ras superfamily of GTP-binding proteins. The GTP-bound form of Arf is involved in Golgi morphology and is involved in recruiting coat proteins. ArfGAP is responsible for the GDP-bound form of Arf which is necessary for uncoating the membrane and allowing the Golgi to fuse with an acceptor compartment. These proteins contain an N-terminal ArfGAP domain containing the characteristic zinc finger motif (Cys-x2-Cys-x(16,17)-x2-Cys) and C-terminal C2 domain. C2 domains were first identified in Protein Kinase C (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: 176003 [Multi-domain]  Cd Length: 145  Bit Score: 39.23  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 368 DPLVrVEIHGvpedcAQKETDYVLNNGFNPCWEQTLQFRLRAPELVLvRFVVEDYDTTSPNDFVGQSTL---PLSSLKQG 444
Cdd:cd04038    23 DPYV-VLTLG-----NQKVKTRVIKKNLNPVWNEELTLSVPNPMAPL-KLEVFDKDTFSKDDSMGEAEIdlePLVEAAKL 95


                  ....*.
gi 1039738371 445 YRHIHL 450
Cdd:cd04038    96 DHLRDT 101
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 51-84 1.45e-03

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE4-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE4 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 1 (GDPD1)) and similar proteins. Mammalian GDE4 is a transmembrane protein whose cellular function is not elucidated. It is expressed widely, including in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocytes. It is also expressed in the growth cones in neuroblastoma Neuro2a cells, which suggests mammalian GDE4 may play some distinct role from other members of mammalian GDEs family. Also included in this subfamily are uncharacterized mammalian glycerophosphodiester phosphodiesterase domain-containing protein 3 (GDPD3) and similar proteins which display very high sequence homology to mammalian GDE4.


Pssm-ID: 176517 [Multi-domain]  Cd Length: 264  Bit Score: 40.28  E-value: 1.45e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1039738371  51 EAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTL 84
Cdd:cd08575    19 AAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDL 52
C2_Intersectin cd08375
C2 domain present in Intersectin; A single instance of the C2 domain is located C terminally ...
 384-443 6.85e-03

C2 domain present in Intersectin; A single instance of the C2 domain is located C terminally in the intersectin protein. Intersectin functions as a scaffolding protein, providing a link between the actin cytoskeleton and the components of endocytosis and plays a role in signal transduction. In addition to C2, intersectin contains several additional domains including: Eps15 homology domains, SH3 domains, a RhoGEF domain, and a PH 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. The members here have topology I.


Pssm-ID: 176021 [Multi-domain]  Cd Length: 136  Bit Score: 36.98  E-value: 6.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 384 QKETDYVLNNGFNPCWEQTLQFRLRAPELVLVRFVVEDYDTTSPNDFVGQSTLPLSSLKQ 443
Cdd:cd08375    47 QEHKTKVVSDTLNPKWNSSMQFFVKDLEQDVLCITVFDRDFFSPDDFLGRTEIRVADILK 106
C2A_Synaptotagmin-15-17 cd08390
C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a ...
 342-439 7.28e-03

C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. 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: 176036 [Multi-domain]  Cd Length: 123  Bit Score: 36.47  E-value: 7.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 342 RTTLAIQVLTAQQLPKLNAEKPSSivDPLVRVeiHGVPEDCAQKETdYVLNNGFNPCWEQTLQFRL---RAPELVLvRFV 418
Cdd:cd08390    13 EEQLTVSLIKARNLPPRTKDVAHC--DPFVKV--CLLPDERRSLQS-KVKRKTQNPNFDETFVFQVsfkELQRRTL-RLS 86

                          90       100
                  ....*....|....*....|.
gi 1039738371 419 VEDYDTTSPNDFVGQSTLPLS 439
Cdd:cd08390    87 VYDVDRFSRHCIIGHVLFPLK 107
C2B_Synaptotagmin-1 cd08402
C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking ...
 340-447 8.27e-03

C2 domain second repeat present in Synaptotagmin 1; 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 the 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. It, like synaptotagmin-2, has an N-glycosylated N-terminus. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. 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: 176047 [Multi-domain]  Cd Length: 136  Bit Score: 36.61  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738371 340 PPRTTLAIQVLTAQQLPKLNAEKPSsivDPLVRVEIHGVPEDCAQKETDyVLNNGFNPCWEQTLQFRLRAPELVLVRFVV 419
Cdd:cd08402    12 PTAGKLTVVILEAKNLKKMDVGGLS---DPYVKIHLMQNGKRLKKKKTT-IKKRTLNPYYNESFSFEVPFEQIQKVHLIV 87

                          90       100       110
                  ....*....|....*....|....*....|
gi 1039738371 420 E--DYDTTSPNDFVGQSTLPLSSLKQGYRH 447
Cdd:cd08402    88 TvlDYDRIGKNDPIGKVVLGCNATGAELRH 117
 
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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