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Conserved domains on  [gi|1803860226|gb|KAF1642547|]
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1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2, partial [Eudyptes chrysocome]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 285-621 0e+00

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 2. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta2 is expressed at highest levels in cells of hematopoietic origin. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins.


:

Pssm-ID: 176561 [Multi-domain]  Cd Length: 261  Bit Score: 565.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEA 364
Cdd:cd08624      1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  365 IAESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKnqsisg 444
Cdd:cd08624     81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  445 krqnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtaYEEMSSLVNY 524
Cdd:cd08624    155 ----------------------------------------------------------------------YEEMSSLVNY 164

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  525 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 604
Cdd:cd08624    165 IQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 244

                          330
                   ....*....|....*..
gi 1803860226  605 QTMDVPMQQNMALFEFN 621
Cdd:cd08624    245 QTMDLPMQQNMALFEFN 261
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 123-273 1.87e-99

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


:

Pssm-ID: 320039  Cd Length: 151  Bit Score: 311.81  E-value: 1.87e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  123 EKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSH 202
Cdd:cd16209      1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803860226  203 HLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 273
Cdd:cd16209     81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 961-1135 1.15e-80

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


:

Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 261.54  E-value: 1.15e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  961 RVLELRERLEMDLIQLGEEHHGGIRRKKEQHATEQVTKIIELAREKQTAELKALKESSESNIKDIKKKLEAKRVDRIQTM 1040
Cdd:pfam08703    2 QVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1041 MRNTSDKAAQERLKKEINNSHIQEVVQTIKLVTEKTARYQQKLEEKQADNLRTIKEKESQLQQEALAEYEEKLKSLNMEV 1120
Cdd:pfam08703   82 KKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAEV 161

                          170
                   ....*....|....*
gi 1803860226 1121 QEMVKNYTKAGFPGQ 1135
Cdd:pfam08703  162 RESVKSCLKEGFPDE 176
PH_14 super family cl39289
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-115 2.77e-41

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


The actual alignment was detected with superfamily member pfam17787:

Pssm-ID: 465506  Cd Length: 131  Bit Score: 147.91  E-value: 2.77e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226   12 EVKEYLSKGERFIKWDD---------------------------EMEILDITSIRDTRVGRFAKIPKCQKLREVFNLDYP 64
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEestvaepnvllkvdpkgfflywksqgkEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1803860226   65 HSTFLLKTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVRNPLTYN 115
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 655-781 1.28e-33

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: 125.73  E-value: 1.28e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  655 TLSVTastshgaILSGQFLSD------RSVKTYVEVELFGLPRDTKRKYRTKlTSTANSINPVWkEEAFVFEkIMMPELA 728
Cdd:cd00275      3 TLTIK-------IISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAKFKTK-VVKNNGFNPVW-NETFEFD-VTVPELA 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1803860226  729 SLKIVAWEEGG---KFIGHRVIPVIAVHSGYHHVCLRSESNMPLTMPSLFVYLEIK 781
Cdd:cd00275     73 FLRFVVYDEDSgddDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
 
Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 285-621 0e+00

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 2. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta2 is expressed at highest levels in cells of hematopoietic origin. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins.


Pssm-ID: 176561 [Multi-domain]  Cd Length: 261  Bit Score: 565.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEA 364
Cdd:cd08624      1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  365 IAESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKnqsisg 444
Cdd:cd08624     81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  445 krqnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtaYEEMSSLVNY 524
Cdd:cd08624    155 ----------------------------------------------------------------------YEEMSSLVNY 164

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  525 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 604
Cdd:cd08624    165 IQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 244

                          330
                   ....*....|....*..
gi 1803860226  605 QTMDVPMQQNMALFEFN 621
Cdd:cd08624    245 QTMDLPMQQNMALFEFN 261
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 123-273 1.87e-99

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


Pssm-ID: 320039  Cd Length: 151  Bit Score: 311.81  E-value: 1.87e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  123 EKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSH 202
Cdd:cd16209      1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803860226  203 HLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 273
Cdd:cd16209     81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 961-1135 1.15e-80

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


Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 261.54  E-value: 1.15e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  961 RVLELRERLEMDLIQLGEEHHGGIRRKKEQHATEQVTKIIELAREKQTAELKALKESSESNIKDIKKKLEAKRVDRIQTM 1040
Cdd:pfam08703    2 QVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1041 MRNTSDKAAQERLKKEINNSHIQEVVQTIKLVTEKTARYQQKLEEKQADNLRTIKEKESQLQQEALAEYEEKLKSLNMEV 1120
Cdd:pfam08703   82 KKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAEV 161

                          170
                   ....*....|....*
gi 1803860226 1121 QEMVKNYTKAGFPGQ 1135
Cdd:pfam08703  162 RESVKSCLKEGFPDE 176
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 288-436 7.43e-77

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


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 249.34  E-value: 7.43e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  288 MTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAIAE 367
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1803860226  368 SAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEkyplKPGVPLPSPKDLLGKILIKN 436
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLD----DDLTELPSPEDLKGKILIKG 142
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 519-633 1.64e-66

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


Pssm-ID: 128454 [Multi-domain]  Cd Length: 115  Bit Score: 219.42  E-value: 1.64e-66
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226   519 SSLVNYIQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQ 598
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1803860226   599 MVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFM 633
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
PLN02222 PLN02222
phosphoinositide phospholipase C 2
 193-779 1.20e-59

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 216.05  E-value: 1.20e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  193 PEIDEIFTSHhlKAKPYMTKEHLAKFINKKQRDSRlndilfppAKPEQVQSLIEKyepSGINIQRGQLSPEGMVWFLCGP 272
Cdd:PLN02222    25 REIKTIFEKY--SENGVMTVDHLHRFLIDVQKQDK--------ATREDAQSIINS---ASSLLHRNGLHLDAFFKYLFGD 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  273 ENNVIALDKLvlYQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIItHGFTM 352
Cdd:PLN02222    92 NNPPLALHEV--HHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSDKDDIDVL-HGMTL 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  353 TTEILFKDAIEAIAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKyPLKPgvpLPSPKDLLGKI 432
Cdd:PLN02222   169 TTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHL-TPDLQSKVAEMVTEIFGEILFTPPVGE-SLKE---FPSPNSLKKRI 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  433 LIKNKKNQSI-SGKRQNSLKKGRNVEPEII---EQPTPMDAEDTVWAGDVAeeepeeedehlGNLDEEEikkmqsDEGTA 508
Cdd:PLN02222   244 IISTKPPKEYkEGKDDEVVQKGKDLGDEEVwgrEVPSFIQRNKSVDKNDSN-----------GDDDDDD------DDGED 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  509 GLEVTAYEEMSSLVNyIQPIK-----FDSFEVSAQKNRSYVISSFTELKAYDlltKFPVQFVEYNKRQMSRIYPKGTRMD 583
Cdd:PLN02222   307 KSKKNAPPQYKHLIA-IHAGKpkggiTECLKVDPDKVRRLSLSEEQLEKAAE---KYAKQIVRFTQHNLLRIYPKGTRVT 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  584 SSNYMPQMFWNVGCQMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRRPDKQFDPFSvDRIDVVVASTLSVTASTS 663
Cdd:PLN02222   383 SSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKKPDLLLKSGSDSDIFD-PKATLPVKTTLRVTIYMG 461

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  664 HGAILS---GQFLSDRSVKTYVEVELFGLPRDTKRKyRTKlTSTANSInPVWKEeafVFE-KIMMPELASLKIVAWE--- 736
Cdd:PLN02222   462 EGWYFDfrhTHFDQYSPPDFYTRVGIAGVPGDTVMK-KTK-TLEDNWI-PAWDE---VFEfPLTVPELALLRLEVHEydm 535

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 1803860226  737 -EGGKFIGHRVIPVIAVHSGYHHVCLRSESNMPLTMPSLFVYLE 779
Cdd:PLN02222   536 sEKDDFGGQTCLPVWELSQGIRAFPLHSRKGEKYKSVKLLVKVE 579
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-115 2.77e-41

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


Pssm-ID: 465506  Cd Length: 131  Bit Score: 147.91  E-value: 2.77e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226   12 EVKEYLSKGERFIKWDD---------------------------EMEILDITSIRDTRVGRFAKIPKCQKLREVFNLDYP 64
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEestvaepnvllkvdpkgfflywksqgkEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1803860226   65 HSTFLLKTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVRNPLTYN 115
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-118 4.68e-35

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


Pssm-ID: 270167  Cd Length: 127  Bit Score: 130.00  E-value: 4.68e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226   17 LSKGERFIKWDD--------------------------EMEILDITSIRDTRVGRFAKIPKCQKLREVfNLDYPHSTFLL 70
Cdd:cd13361      1 LLKGSKFDKWDEdssletpvtlkvdeygfflywksegkETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1803860226   71 KTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVRNPLTYNASR 118
Cdd:cd13361     80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 655-781 1.28e-33

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: 125.73  E-value: 1.28e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  655 TLSVTastshgaILSGQFLSD------RSVKTYVEVELFGLPRDTKRKYRTKlTSTANSINPVWkEEAFVFEkIMMPELA 728
Cdd:cd00275      3 TLTIK-------IISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAKFKTK-VVKNNGFNPVW-NETFEFD-VTVPELA 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1803860226  729 SLKIVAWEEGG---KFIGHRVIPVIAVHSGYHHVCLRSESNMPLTMPSLFVYLEIK 781
Cdd:cd00275     73 FLRFVVYDEDSgddDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 667-761 4.76e-10

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: 57.88  E-value: 4.76e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226   667 ILSGQFLSDR----SVKTYVEVELFGlprDTKRKYRTKltSTANSINPVWKEEaFVFEkIMMPELASLKIVAWEEGG--- 739
Cdd:smart00239    6 IISARNLPPKdkggKSDPYVKVSLDG---DPKEKKKTK--VVKNTLNPVWNET-FEFE-VPPPELAELEIEVYDKDRfgr 78

                            90       100
                    ....*....|....*....|...
gi 1803860226   740 -KFIGHRVIPVIAVHSGYHHVCL 761
Cdd:smart00239   79 dDFIGQVTIPLSDLLLGGRHEKL 101
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 189-276 1.21e-07

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


Pssm-ID: 401279 [Multi-domain]  Cd Length: 85  Bit Score: 50.32  E-value: 1.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  189 LCPRPEIDEIFTSHHlKAKPYMTKEHLAKFINKKQRDSRlndilfppAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWF 268
Cdd:pfam09279    5 LTQREEIDEIFQEYS-GDGQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAMTKDGFLMY 75


                   ....*...
gi 1803860226  269 LCGPENNV 276
Cdd:pfam09279   76 LCSPDGSI 83
C2 pfam00168
C2 domain;
667-749 2.38e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 44.23  E-value: 2.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  667 ILSGQFL----SDRSVKTYVEVELfglpRDTKRKYRTKLTStaNSINPVWKEEaFVFEkIMMPELASLKIVAWEEGG--- 739
Cdd:pfam00168    7 VIEAKNLppkdGNGTSDPYVKVYL----LDGKQKKKTKVVK--NTLNPVWNET-FTFS-VPDPENAVLEIEVYDYDRfgr 78

                           90
                   ....*....|.
gi 1803860226  740 -KFIGHRVIPV 749
Cdd:pfam00168   79 dDFIGEVRIPL 89
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1003-1159 1.37e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1003 AREKQTAELKALKESSESNIKDIKKKLEAKRVDRIQTMMRNTSDKAAQERLKKEINN--SHIQEVVQTIKLVTEKTARYQ 1080
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaNEISRLEQQKQILRERLANLE 315

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1803860226 1081 QKLEEKQADNLRtiKEKESQLQQEALAEYEEKLKSLNMEVQEMvknytkagfpgqPEAQKEAVQSIPEGEQGSTAQLEE 1159
Cdd:TIGR02168  316 RQLEELEAQLEE--LESKLDELAEELAELEEKLEELKEELESL------------EAELEELEAELEELESRLEELEEQ 380
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1005-1161 5.25e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 5.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1005 EKQTAELKALKESSESNIKDIKKKLEAKRVDRIQTMMRNTSDKAAQERLKKEINNSHIQEVVQTIKLvtEKTARYQQK-- 1082
Cdd:COG3883     22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL--GERARALYRsg 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1083 -----LEE-----------KQADNLRTIKEKESQL---QQEALAEYEEKLKSLNMEVQEMVKNYTKAgfpgqpEAQKEAV 1143
Cdd:COG3883    100 gsvsyLDVllgsesfsdflDRLSALSKIADADADLleeLKADKAELEAKKAELEAKLAELEALKAEL------EAAKAEL 173

                          170
                   ....*....|....*...
gi 1803860226 1144 QSIPEGEQGSTAQLEEKI 1161
Cdd:COG3883    174 EAQQAEQEALLAQLSAEE 191
PTZ00121 PTZ00121
MAEBL; Provisional
 903-1149 1.08e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  903 KRREELLQKYSVLFSEPVCYRGKKRMIHARKTQKKRSLATGDVGTCANPVEMAESIDSRVL--ELRERLEMDLIQLGEEH 980
Cdd:PTZ00121  1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEE 1631

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  981 HGGIRRKKEQHAtEQVTKIIELAREKQTAELKALKESSESNiKDIKKKLEAKRVDRiqtmmrntSDKAAQERLKKEinns 1060
Cdd:PTZ00121  1632 KKKVEQLKKKEA-EEKKKAEELKKAEEENKIKAAEEAKKAE-EDKKKAEEAKKAEE--------DEKKAAEALKKE---- 1697

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1061 hiQEVVQTIKLVTEKTARYQQKLEE-KQADNLRTIKEKESQLQQEalaeyEEKLKSLNMEVQEMVKN----YTKAGFPGQ 1135
Cdd:PTZ00121  1698 --AEEAKKAEELKKKEAEEKKKAEElKKAEEENKIKAEEAKKEAE-----EDKKKAEEAKKDEEEKKkiahLKKEEEKKA 1770

                          250
                   ....*....|....
gi 1803860226 1136 PEAQKEAVQSIPEG 1149
Cdd:PTZ00121  1771 EEIRKEKEAVIEEE 1784
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1012-1130 9.71e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.95  E-value: 9.71e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  1012 KALKESSEsnIKDIKKKLEAKRVDRIQTMmrntsdKAAQERLKKEINNSHIQEVVQTIKLVTEKTARYQQKLEEKQadnl 1091
Cdd:smart00935    8 KILQESPA--GKAAQKQLEKEFKKRQAEL------EKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQ---- 75

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1803860226  1092 rtikEKESQLQQEALAEYEEKLKSLNMEVQEMVKNYTKA 1130
Cdd:smart00935   76 ----RKQQKLQQDLQKRQQEELQKILDKINKAIKEVAKK 110
 
Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 285-621 0e+00

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 2. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta2 is expressed at highest levels in cells of hematopoietic origin. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins.


Pssm-ID: 176561 [Multi-domain]  Cd Length: 261  Bit Score: 565.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEA 364
Cdd:cd08624      1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  365 IAESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKnqsisg 444
Cdd:cd08624     81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  445 krqnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtaYEEMSSLVNY 524
Cdd:cd08624    155 ----------------------------------------------------------------------YEEMSSLVNY 164

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  525 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 604
Cdd:cd08624    165 IQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 244

                          330
                   ....*....|....*..
gi 1803860226  605 QTMDVPMQQNMALFEFN 621
Cdd:cd08624    245 QTMDLPMQQNMALFEFN 261
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
 285-621 0e+00

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are four PLC-beta isozymes (1-4). They are activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. The beta-gamma subunits of heterotrimeric G proteins are known to activate the PLC-beta2 and -beta3 isozymes only. Aside from four PLC-beta isozymes identified in mammals, some eukaryotic PLC-beta homologs have been classified into this subfamily, such as NorpA and PLC-21 from Drosophila and PLC-beta from turkey, Xenopus, sponge, and hydra.


Pssm-ID: 176533 [Multi-domain]  Cd Length: 257  Bit Score: 550.79  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEA 364
Cdd:cd08591      1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  365 IAESAFKTSLYPVILSFENHVDSpKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKnqsisg 444
Cdd:cd08591     81 IAETAFKTSEYPVILSFENHCSS-KQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------ 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  445 krqnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNY 524
Cdd:cd08591    154 -------------------------------------------------------------------------LSSLVNY 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  525 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 604
Cdd:cd08591    161 IQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQLSRIYPKGTRVDSSNYMPQIFWNAGCQMVALNF 240

                          330
                   ....*....|....*..
gi 1803860226  605 QTMDVPMQQNMALFEFN 621
Cdd:cd08591    241 QTPDLPMQLNQGKFEYN 257
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
 287-621 7.64e-153

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 3. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta3 is widely expressed at highest levels in brain, liver, and parotid gland. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins.


Pssm-ID: 176562 [Multi-domain]  Cd Length: 258  Bit Score: 457.59  E-value: 7.64e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  287 DMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEAIA 366
Cdd:cd08625      3 DMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEAIA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  367 ESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKnqsisgkr 446
Cdd:cd08625     83 ESAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK-------- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  447 qnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNYIQ 526
Cdd:cd08625    155 -----------------------------------------------------------------------MSTLVNYIE 163

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  527 PIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQT 606
Cdd:cd08625    164 PVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPMEFVEYNKKQLSRIYPKGTRVDSSNYMPQLFWNVGCQMVALNFQT 243

                          330
                   ....*....|....*
gi 1803860226  607 MDVPMQQNMALFEFN 621
Cdd:cd08625    244 LDLAMQLNMGVFEYN 258
PI-PLCc_eukaryota cd08558
Catalytic domain of eukaryotic phosphoinositide-specific phospholipase C and similar proteins; ...
 285-621 1.30e-135

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


Pssm-ID: 176501 [Multi-domain]  Cd Length: 226  Bit Score: 411.07  E-value: 1.30e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 364
Cdd:cd08558      1 YQDMTQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGHTLTSKILFKDVIEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  365 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPlkpgVPLPSPKDLLGKILIKNKKNQsisg 444
Cdd:cd08558     79 IKEYAFVTSPYPVILSLENHC-SLEQQKKMAQILKEIFGDKLLTPPLDENP----VQLPSPEQLKGKILIKGKKYH---- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  445 krqnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeemsslvny 524
Cdd:cd08558        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  525 iqpikfdsfevsaqknrsyvISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 604
Cdd:cd08558    150 --------------------MSSFSETKALKLLKESPEEFVKYNKRQLSRVYPKGTRVDSSNYNPQPFWNAGCQMVALNY 209

                          330
                   ....*....|....*..
gi 1803860226  605 QTMDVPMQQNMALFEFN 621
Cdd:cd08558    210 QTPDLPMQLNQGKFEQN 226
PI-PLCc_beta1 cd08623
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1; This subfamily ...
 286-621 2.19e-134

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 1. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta1 is expressed at highest levels in specific regions of the brain. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension.


Pssm-ID: 176560 [Multi-domain]  Cd Length: 258  Bit Score: 409.47  E-value: 2.19e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  286 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEAI 365
Cdd:cd08623      2 EDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  366 AESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKnqsisgk 445
Cdd:cd08623     82 AECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKK------- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  446 rqnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNYI 525
Cdd:cd08623    155 ------------------------------------------------------------------------MSNLVNYI 162

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  526 QPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQ 605
Cdd:cd08623    163 QPVKFESFEASKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQ 242

                          330
                   ....*....|....*.
gi 1803860226  606 TMDVPMQQNMALFEFN 621
Cdd:cd08623    243 TVDLSMQINMGMYEYN 258
PI-PLCc_beta4 cd08626
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4; This subfamily ...
 285-621 6.05e-131

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-beta isozyme 4. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-beta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-beta4 is expressed in high concentrations in cerebellar Purkinje and granule cells, the median geniculate body, and the lateral geniculate nucleus. It is activated by the heterotrimeric G protein alpha q subunits through their C2 domain and long C-terminal extension.


Pssm-ID: 176563 [Multi-domain]  Cd Length: 257  Bit Score: 400.29  E-value: 6.05e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEA 364
Cdd:cd08626      1 YQDMDQPLAHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCIELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  365 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKnqsisg 444
Cdd:cd08626     81 IKDTAFVTSDYPVILSFENHC-SKPQQYKLAKYCEEIFGDLLLTKPLESHPLEPGVPLPSPNKLKRKILIKNKR------ 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  445 krqnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNY 524
Cdd:cd08626    154 -------------------------------------------------------------------------LSSLVNY 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  525 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 604
Cdd:cd08626    161 AQPVKFQGFDVAEERNIHFNMSSFNESVGLGYLKTSAIEFVNYNKRQMSRIYPKGTRVDSSNYMPQIFWNAGCQMVSLNF 240

                          330
                   ....*....|....*..
gi 1803860226  605 QTMDVPMQQNMALFEFN 621
Cdd:cd08626    241 QTPDLGMQLNQGKFEYN 257
PI-PLCc_delta cd08593
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta; This subfamily ...
 285-621 1.03e-112

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


Pssm-ID: 176535 [Multi-domain]  Cd Length: 257  Bit Score: 351.64  E-value: 1.03e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 364
Cdd:cd08593      1 YQDMTQPLSHYFIASSHNTYLLEDQLKGPSSTEAYIRALKKGCRCVELDCWDG--PDGEPIIYHGHTLTSKILFKDVIQA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  365 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEkyplKPGVPLPSPKDLLGKILIKNKKnqsisg 444
Cdd:cd08593     79 IREYAFKVSPYPVILSLENHC-SVEQQKVMAQHLKSILGDKLLTQPLD----GVLTALPSPEELKGKILVKGKK------ 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  445 krqnsLKkgrnvepeiieqptpmdaedtvwagdVAeeepeeedehlgnldeeeikkmqsdegtaglevtayEEMSSLVNY 524
Cdd:cd08593    148 -----LK--------------------------LA------------------------------------KELSDLVIY 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  525 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 604
Cdd:cd08593    161 CKSVHFKSFEHSKENYHFYEMSSFSESKALKLAQESGNEFVRHNKRQLSRIYPAGLRTDSSNYDPQEMWNVGCQIVALNF 240

                          330
                   ....*....|....*..
gi 1803860226  605 QTMDVPMQQNMALFEFN 621
Cdd:cd08593    241 QTPGEEMDLNDGLFRQN 257
EFh_PI-PLCbeta2 cd16209
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2); PI-PLC-beta2, ...
 123-273 1.87e-99

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


Pssm-ID: 320039  Cd Length: 151  Bit Score: 311.81  E-value: 1.87e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  123 EKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSH 202
Cdd:cd16209      1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803860226  203 HLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 273
Cdd:cd16209     81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PI-PLCc_PRIP_metazoa cd08597
Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein; This ...
 286-621 8.03e-94

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


Pssm-ID: 176539 [Multi-domain]  Cd Length: 260  Bit Score: 300.88  E-value: 8.03e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  286 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAI 365
Cdd:cd08597      2 QDMTQPLSHYFIASSHNTYLIEDQLRGPSSVEGYVRALQRGCRCVELDCWDG--PNGEPVIYHGHTLTSKISFRSVIEAI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  366 AESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPlekyPLKPGVPLPSPKDLLGKILIKNKKnqsisgk 445
Cdd:cd08597     80 NEYAFVASEYPLILCIENHC-SEKQQLVMAQYLKEIFGDKLYTEP----PNEGESYLPSPHDLKGKIIIKGKK------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  446 rqnsLKKgrnvePEIIeqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayEEMSSLVNYI 525
Cdd:cd08597    148 ----LKR-----RKLC------------------------------------------------------KELSDLVSLC 164

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  526 QPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQ 605
Cdd:cd08597    165 KSVRFQDFPTSAQNQKYWEVCSFSENLARRLANEFPEDFVNYNKKFLSRVYPSPMRVDSSNYNPQDFWNCGCQIVAMNYQ 244

                          330
                   ....*....|....*.
gi 1803860226  606 TMDVPMQQNMALFEFN 621
Cdd:cd08597    245 TPGLMMDLNTGKFLEN 260
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 285-621 3.85e-93

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: 299.95  E-value: 3.85e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFS-----GISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTtEILFK 359
Cdd:cd00137      1 HHPDTQPLAHYSIPGTHDTYLTAGQFTikqvwGLTQTEMYRQQLLSGCRCVDIRCWDG--KPEEPIIYHGPTFL-DIFLK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  360 DAIEAIAESAFKTSLYPVILSFENHVDS-PKQQAKMAEYCRTIFGDMLLTeplekYPLKPGVPLPSPKDLLGKILIKNKK 438
Cdd:cd00137     78 EVIEAIAQFLKKNPPETIIMSLKNEVDSmDSFQAKMAEYCRTIFGDMLLT-----PPLKPTVPLPSLEDLRGKILLLNKK 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  439 NQsisgkrqnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaGLEVTAYEEM 518
Cdd:cd00137    153 NG--------------------------------------------------------------------FSGPTGSSND 164

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  519 SSlvnyiqpikFDSFEVSAQKNRSYVISSFTELKAYD----LLTKFPVQFVEYNKRQMSRIYPKGTR---------MDSS 585
Cdd:cd00137    165 TG---------FVSFEFSTQKNRSYNISSQDEYKAYDdekvKLIKATVQFVDYNKNQLSRNYPSGTSggtawyyyaMDSN 235

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1803860226  586 NYMPQMFWN---VGCQMVALNFQTMDVPMQQNMALFEFN 621
Cdd:cd00137    236 NYMPQMFWNanpAGCGIVILDFQTMDLPMQQYMAVIEFN 274
PI-PLCc_gamma cd08592
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma; This family ...
 286-621 3.17e-90

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


Pssm-ID: 176534 [Multi-domain]  Cd Length: 229  Bit Score: 290.10  E-value: 3.17e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  286 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAI 365
Cdd:cd08592      2 QDMNNPLSHYWIASSHNTYLTGDQLSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPIIYHGHTLTSKIKFMDVLKTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  366 AESAFKTSLYPVILSFENHVDSPkQQAKMAEYCRTIFGDMLLTEPLEkyplKPGVPLPSPKDLLGKILIKNKKnqsisgk 445
Cdd:cd08592     80 KEHAFVTSEYPVILSIENHCSLP-QQRNMAQAFKEVFGDMLLTQPVD----RNADQLPSPNQLKRKIIIKHKK------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  446 rqnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtAYEEMsslvnyi 525
Cdd:cd08592    148 --------------------------------------------------------------------LFYEM------- 152

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  526 qpikfdsfevsaqknrsyviSSFTELKAYDLLTKF-PVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 604
Cdd:cd08592    153 --------------------SSFPETKAEKYLNRQkGKIFLKYNRRQLSRVYPKGQRVDSSNYDPVPMWNCGSQMVALNF 212

                          330
                   ....*....|....*..
gi 1803860226  605 QTMDVPMQQNMALFEFN 621
Cdd:cd08592    213 QTPDKPMQLNQALFMLN 229
PI-PLCc_delta3 cd08630
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily ...
 285-621 4.80e-85

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: 276.90  E-value: 4.80e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 364
Cdd:cd08630      1 FQDMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEG--PGGEPVIYHGHTLTSKILFRDVIQA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  365 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvPLPSPKDLLGKILIKNKKNQsisg 444
Cdd:cd08630     79 VRQHAFTASPYPVILSLENHC-GLEQQAAMARHLQTILGDMLVTQPLDSLNPE---ELPSPEELKGRVLVKGKKLQ---- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  445 krqnslkkgrnVEPeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeEMSSLVNY 524
Cdd:cd08630    151 -----------ISP----------------------------------------------------------ELSALAVY 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  525 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 604
Cdd:cd08630    162 CQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQEMWNSGCQLVALNF 241

                          330
                   ....*....|....*..
gi 1803860226  605 QTMDVPMQQNMALFEFN 621
Cdd:cd08630    242 QTPGYEMDLNAGRFLVN 258
PI-PLC1c_yeast cd08598
Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This ...
 285-618 2.26e-84

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


Pssm-ID: 176540 [Multi-domain]  Cd Length: 231  Bit Score: 274.12  E-value: 2.26e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 364
Cdd:cd08598      1 EEDLSRPLNEYFISSSHNTYLLGRQLAGDSSVEGYIRALQRGCRCVEIDVWDG--DDGEPVVTHGYTLTSSVPFRDVCRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  365 IAESAFKTSLYPVILSFENHVDsPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvpLPSPKDLLGKILIKNKKnqsisg 444
Cdd:cd08598     79 IKKYAFVTSPYPLILSLEVHCD-AEQQERMVEIMKETFGDLLVTEPLDGLEDE----LPSPEELRGKILIKVKK------ 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  445 krqnslkkgrnvepeiiEQPTPmdaedtvwagdvaeeepeeedEHLGNLDEEEIKKMQSDegtaglevtayeemsslvny 524
Cdd:cd08598    148 -----------------ESKTP---------------------NHIFSLSERSLLKLLKD-------------------- 169

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  525 iqpikfdsfevsaqknrsyvissftelKAYDLltkfpvqfVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 604
Cdd:cd08598    170 ---------------------------KRAAL--------DKHNRRHLMRVYPSGTRISSSNFNPLPFWRAGVQMVALNW 214

                          330
                   ....*....|....
gi 1803860226  605 QTMDVPMQQNMALF 618
Cdd:cd08598    215 QTYDLGMQLNEAMF 228
PI-PLCc_delta1 cd08629
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily ...
 285-621 2.78e-83

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-delta1 isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-delta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C-terminal C2 domain. This subfamily corresponds to the catalytic domain which is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1,3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Unlike PI-PLC-delta 4, PI-PLC-delta1 and 3 possess a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1and 3 from the cell nucleus. Experiments show PI-PLC-delta1 is essential for normal hair formation.


Pssm-ID: 176566 [Multi-domain]  Cd Length: 258  Bit Score: 271.91  E-value: 2.78e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 364
Cdd:cd08629      1 YQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDG--PNQEPIIYHGYTFTSKILFCDVLRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  365 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvpLPSPKDLLGKILIKNKKnqsisg 444
Cdd:cd08629     79 IRDYAFKASPYPVILSLENHC-SLEQQRVMARHLRAILGPILLDQPLDGVTTS----LPSPEQLKGKILLKGKK------ 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  445 krqnsLKKGRnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeEMSSLVNY 524
Cdd:cd08629    148 -----LKLVP--------------------------------------------------------------ELSDMIIY 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  525 IQPIKFDSFEVSAQKNRS-YVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALN 603
Cdd:cd08629    161 CKSVHFGGFSSPGTSGQAfYEMASFSESRALRLLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALN 240

                          330
                   ....*....|....*...
gi 1803860226  604 FQTMDVPMQQNMALFEFN 621
Cdd:cd08629    241 FQTPGPEMDVYLGCFQDN 258
PI-PLCc_delta4 cd08631
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4; This subfamily ...
 285-621 3.18e-81

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-delta4 isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-delta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C-terminal C2 domain. This CD corresponds to the catalytic domain which is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1,3 and 4). Unlike PI-PLC-delta 1 and 3, a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1 and 3 from the cell nucleus, is not present in PI-PLC-delta4. Experiments show PI-PLC-delta4 is required for the acrosome reaction in fertilization.


Pssm-ID: 176568 [Multi-domain]  Cd Length: 258  Bit Score: 266.43  E-value: 3.18e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 364
Cdd:cd08631      1 YQDMTQPLCHYFICSSHNTYLMEDQLRGQSSVEGYIRALKRGCRCVEVDVWDG--PNGEPIVYHGHTFTSKILFKDVVAA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  365 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLE-KYPlkpgVPLPSPKDLLGKILIKNKKnqsis 443
Cdd:cd08631     79 VAQYAFQVSDYPVILSLENHC-GVEQQQTMAQHLTEILGEKLLSTTLDgVLP----TQLPSPEELRGKILLKGKK----- 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  444 gkrqnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtagleVTAYEEMSSLVN 523
Cdd:cd08631    149 --------------------------------------------------------------------IRLSPELSDCVI 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  524 YIQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALN 603
Cdd:cd08631    161 YCKSVSFRSFTHSREHYHFYEISSFTETKARKLIREAGNEFVQHNTWQLSRVYPSGLRTDSSNYNPQEMWNAGCQMVALN 240

                          330
                   ....*....|....*...
gi 1803860226  604 FQTMDVPMQQNMALFEFN 621
Cdd:cd08631    241 FQTAGLEMDLNDGLFRQN 258
PI-PLCc_zeta cd08595
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta; This family ...
 285-621 3.63e-81

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta; This family corresponds to the catalytic domain presenting in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-zeta isozyme. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-zeta represents a class of sperm-specific PI-PLC that has an N-terminal EF-hand domain, a PLC catalytic core domain, and a C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There is one PLC-zeta isozyme (1). PLC-zeta plays a fundamental role in vertebrate fertilization by initiating intracellular calcium oscillations that trigger the embryo development. However, the mechanism of its activation still remains unclear. Aside from PI-PLC-zeta identified in mammals, its eukaryotic homologs have been classified with this family.


Pssm-ID: 176537 [Multi-domain]  Cd Length: 257  Bit Score: 266.03  E-value: 3.63e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 364
Cdd:cd08595      1 YQDMDHPLSDYFISSSHNTYLVSDQLVGPSDLDGYVSALRKGCRCLEIDCWDG--ADNEPVVYHGYTLTSKILFKEVITT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  365 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvPLPSPKDLLGKILIKNKKnqsisg 444
Cdd:cd08595     79 VEKYAFEKSDYPVVLSLENHC-STEQQEIMAHYLVSILGEKLLRAPIDDPATG---ELPSPEALKFKILVKNKK------ 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  445 krqnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeEIKKMQSDegtaglevtayeemssLVNY 524
Cdd:cd08595    149 ----------------------------------------------------KIAKALSD----------------LVIY 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  525 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 604
Cdd:cd08595    161 TKSEKFCSFTHSRDNQHSYENNSIGENKARKLLKSSGADFVGHTQRFITRIYPKGTRASSSNYNPQEFWNVGCQMVALNF 240

                          330
                   ....*....|....*..
gi 1803860226  605 QTMDVPMQQNMALFEFN 621
Cdd:cd08595    241 QTLGAPMDLQNGKFLDN 257
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 961-1135 1.15e-80

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


Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 261.54  E-value: 1.15e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  961 RVLELRERLEMDLIQLGEEHHGGIRRKKEQHATEQVTKIIELAREKQTAELKALKESSESNIKDIKKKLEAKRVDRIQTM 1040
Cdd:pfam08703    2 QVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1041 MRNTSDKAAQERLKKEINNSHIQEVVQTIKLVTEKTARYQQKLEEKQADNLRTIKEKESQLQQEALAEYEEKLKSLNMEV 1120
Cdd:pfam08703   82 KKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAEV 161

                          170
                   ....*....|....*
gi 1803860226 1121 QEMVKNYTKAGFPGQ 1135
Cdd:pfam08703  162 RESVKSCLKEGFPDE 176
PI-PLCc_epsilon cd08596
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon; This family ...
 286-621 1.09e-79

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon; This family corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-epsilon isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-epsilon represents a class of mammalian PI-PLC that has an N-terminal CDC25 homology domain with a guanyl-nucleotide exchange factor (GFF) activity, a pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and two predicted RA (Ras association) domains that are implicated in the binding of small GTPases, such as Ras or Rap, from the Ras family. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There is one PI-PLC-epsilon isozyme (1). PI-PLC-epsilon is activated by G alpha(12/13), G beta gamma, and activated members of Ras and Rho small GTPases. Aside from PI-PLC-epsilon identified in mammals, its eukaryotic homologs have been classified with this family.


Pssm-ID: 176538 [Multi-domain]  Cd Length: 254  Bit Score: 262.09  E-value: 1.09e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  286 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRppDEEPIITHGFTMTTEILFKDAIEAI 365
Cdd:cd08596      2 EDLQYPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLTGCRCVELDCWDGD--DGMPIIYHGHTLTTKIPFKDVVEAI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  366 AESAFKTSLYPVILSFENHVDSPkQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKNQsisgk 445
Cdd:cd08596     80 NRSAFITSDYPVILSIENHCSLQ-QQRKMAEIFKTVFGEKLVTKFLFESDFSDDPSLPSPLQLKNKILLKNKKAP----- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  446 rqnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeEMSSLVNYI 525
Cdd:cd08596    154 -----------------------------------------------------------------------ELSDLVIYC 162

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  526 QPIKFDSFEVSaqknRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQ 605
Cdd:cd08596    163 QAVKFPGLSTP----KCYHISSLNENAAKRLCRRYPQKLVQHTRCQLLRTYPAATRIDSSNPNPLIFWLHGLQLVALNYQ 238

                          330
                   ....*....|....*.
gi 1803860226  606 TMDVPMQQNMALFEFN 621
Cdd:cd08596    239 TDDLPMHLNAAMFEAN 254
PI-PLCc_eta cd08594
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta; This family ...
 285-621 2.51e-77

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


Pssm-ID: 176536 [Multi-domain]  Cd Length: 227  Bit Score: 254.34  E-value: 2.51e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 364
Cdd:cd08594      1 NQDMTQPLSHYFIASSHNTYLTGDQLLSQSRVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKILFRDVIET 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  365 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLtepLEKYPLKPGVPLPSPKDLLGKILIKNKKNQsisg 444
Cdd:cd08594     79 INKYAFIKNEYPVILSIENHC-SVQQQKKMAQYLKEILGDKLD---LSSVISGDSKQLPSPQSLKGKILIKGKKWQ---- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  445 krqnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeemsslvny 524
Cdd:cd08594        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  525 iqpikfdsfevsaqknrsyvISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 604
Cdd:cd08594    151 --------------------VSSFSETRAHQIVQQKAAQFLRFNQRQLSRIYPSAYRIDSSNFNPQPYWNAGCQLVALNY 210

                          330
                   ....*....|....*..
gi 1803860226  605 QTMDVPMQQNMALFEFN 621
Cdd:cd08594    211 QTEGRMLQLNRAKFRAN 227
PI-PLCc_gamma2 cd08628
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2; This subfamily ...
 286-621 2.75e-77

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-gamma isozyme 2. PI-PLC is a signaling enzyme that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-gamma represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unique to PI-PLC-gamma2, a second PH domain, two SH2 (Src homology 2) regions, and one SH3 (Src homology 3) region is present within this linker region. PI-PLC-gamma2 is highly expressed in cells of hematopoietic origin. It is activated by receptor and non-receptor tyrosine kinases due to the presence of two SH2 and a single SH3 domain within the linker region. Unlike PI-PLC-gamma1, the activation of PI-PLC-gamma2 may require concurrent stimulation of PI 3-kinase.


Pssm-ID: 176565 [Multi-domain]  Cd Length: 254  Bit Score: 255.36  E-value: 2.75e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  286 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAI 365
Cdd:cd08628      2 QDMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRMGCRCIELDCWDG--PDGKPIIYHGWTRTTKIKFDDVVQAI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  366 AESAFKTSLYPVILSFENHVDSpKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvpLPSPKDLLGKILIKNKKNQSIsgk 445
Cdd:cd08628     80 KDHAFVTSEYPVILSIEEHCSV-EQQRHMAKVFKEVFGDKLLMKPLEASADQ----LPSPTQLKEKIIIKHKKLIAI--- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  446 rqnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeEMSSLVNYI 525
Cdd:cd08628    152 -----------------------------------------------------------------------ELSDLVVYC 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  526 QPI--KFDSFEVSAQKNrsyvISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALN 603
Cdd:cd08628    161 KPTskTKDNLENPDFKE----IRSFVETKAPSIIRQKPVQLLKYNRKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALN 236

                          330
                   ....*....|....*...
gi 1803860226  604 FQTMDVPMQQNMALFEFN 621
Cdd:cd08628    237 FQTADKYMQLNHALFSLN 254
PI-PLCc_eta2 cd08633
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily ...
 286-621 3.10e-77

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-eta isozyme 2. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-eta represents a class of neuron-speific PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-eta2 is a neuron-specific enzyme and expressed in the brain. It may in part function downstream of G-protein-coupled receptors and play an important role in the formation and maintenance of the neuronal network in the postnatal brain.


Pssm-ID: 176570 [Multi-domain]  Cd Length: 254  Bit Score: 254.96  E-value: 3.10e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  286 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAI 365
Cdd:cd08633      2 QDMTQPLSHYFITSSHNTYLSGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDG--PDGEPIVHHGYTLTSKILFKDVIETI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  366 AESAFKTSLYPVILSFENHVDSPkQQAKMAEYCRTIFGDMLltePLEKYPLKPGVPLPSPKDLLGKILIKNKKnqsisgk 445
Cdd:cd08633     80 NKYAFIKNEYPVILSIENHCSVP-QQKKMAQYLTEILGDKL---DLSSVISNDCTRLPSPEILKGKILVKGKK------- 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  446 rqnsLKKGrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNYI 525
Cdd:cd08633    149 ----LSRA----------------------------------------------------------------LSDLVKYT 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  526 QPIKFDSFEVSAQKnrSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQ 605
Cdd:cd08633    161 KSVRVHDIETEATS--SWQVSSFSETKAHQILQQKPAQYLRFNQRQLSRIYPSSYRVDSSNYNPQPFWNAGCQMVALNYQ 238

                          330
                   ....*....|....*.
gi 1803860226  606 TMDVPMQQNMALFEFN 621
Cdd:cd08633    239 SEGRMLQLNRAKFSAN 254
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 288-436 7.43e-77

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


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 249.34  E-value: 7.43e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  288 MTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAIAE 367
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1803860226  368 SAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEkyplKPGVPLPSPKDLLGKILIKN 436
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLD----DDLTELPSPEDLKGKILIKG 142
PI-PLCc_eta1 cd08632
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily ...
 285-621 1.63e-69

Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-eta isozyme 1. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PI-PLC-eta represents a class of neuron-speific PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-eta1 is a neuron-specific enzyme and expressed in only nerve tissues such as the brain and spinal cord. It may perform a fundamental role in the brain.


Pssm-ID: 176569 [Multi-domain]  Cd Length: 253  Bit Score: 233.38  E-value: 1.63e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 364
Cdd:cd08632      1 NQDMDQPLCNYFIASSHNTYLTGDQLLSQSKVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKITFRDVIET 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  365 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDML-LTEPLEKYPLKpgvpLPSPKDLLGKILIKNKK-NQSI 442
Cdd:cd08632     79 INKYAFVKNEFPVILSIENHC-SIQQQKKIAQYLKEIFGDKLdLSSVLTGDPKQ----LPSPQLLKGKILVKGKKlCRDL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  443 SgkrqnslkkgrnvepEIIEQPTPMDAEDTVwagdvaeeepeeedehlgnldeeeikkmqsDEGTAGlevtayeemsslv 522
Cdd:cd08632    154 S---------------DLVVYTNSVAAQDIV------------------------------DDGSTG------------- 175

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  523 nyiqpikfdsfevsaqknrsyVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVAL 602
Cdd:cd08632    176 ---------------------NVLSFSETRAHQLVQQKAEQFMTYNQKQLTRIYPSAYRIDSSNFNPLPYWNVGCQLVAL 234

                          330
                   ....*....|....*....
gi 1803860226  603 NFQTMDVPMQQNMALFEFN 621
Cdd:cd08632    235 NYQSEGRMMQLNRAKFMVN 253
PI-PLCc_gamma1 cd08627
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily ...
 286-621 3.95e-69

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


Pssm-ID: 176564 [Multi-domain]  Cd Length: 229  Bit Score: 231.46  E-value: 3.95e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  286 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAI 365
Cdd:cd08627      2 EEMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPVIYHGHTLTTKIKFSDVLHTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  366 AESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEkyplKPGVPLPSPKDLLGKILIKNKKnqsisgk 445
Cdd:cd08627     80 KEHAFVTSEYPIILSIEDHC-SIVQQRNMAQHFKKVFGDMLLTKPVD----INADGLPSPNQLKRKILIKHKK------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  446 rqnslkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtAYEEMsslvnyi 525
Cdd:cd08627    148 --------------------------------------------------------------------LYRDM------- 152

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  526 qpikfdsfevsaqknrsyviSSFTELKAYDLLTKFP-VQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 604
Cdd:cd08627    153 --------------------SSFPETKAEKYVNRSKgKKFLQYNRRQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNF 212

                          330
                   ....*....|....*..
gi 1803860226  605 QTMDVPMQQNMALFEFN 621
Cdd:cd08627    213 QTPDKPMQMNQALFMLG 229
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 519-633 1.64e-66

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


Pssm-ID: 128454 [Multi-domain]  Cd Length: 115  Bit Score: 219.42  E-value: 1.64e-66
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226   519 SSLVNYIQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQ 598
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1803860226   599 MVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFM 633
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
EFh_PI-PLCbeta cd16200
EF-hand motif found in metazoan phosphoinositide-specific phospholipase C (PI-PLC)-beta ...
 123-273 1.55e-63

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


Pssm-ID: 320030 [Multi-domain]  Cd Length: 153  Bit Score: 212.49  E-value: 1.55e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  123 EKILVKLKMQLNAEGKIPVRNIFQMFPAD--RKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFT 200
Cdd:cd16200      1 KKLYTKLKLSVNITGKIPVKNIIKCFSSDkkRKRVLKALKALGLPDGKNDEIDPEDFTFEKFFKLYNKLCPRPDIDEIFK 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1803860226  201 SHHLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 273
Cdd:cd16200     81 ELGGKRKPYLTLEQLVDFLNEEQRDPRLNEILFPFHTKEQAKKLIDKYEPNEKNKKKGQLTLEGFLRYLMSDE 153
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 288-437 9.44e-62

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


Pssm-ID: 197543 [Multi-domain]  Cd Length: 143  Bit Score: 206.75  E-value: 9.44e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226   288 MTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAIAE 367
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDG--PDGEPVIYHGHTFTLPIKLSEVLEAIKD 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226   368 SAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvpLPSPKDLLGKILIKNK 437
Cdd:smart00148   79 FAFVTSPYPVILSLENHC-SPDQQAKMAQMFKEIFGDMLYTPPLTSSLEV----LPSPEQLRGKILLKVR 143
EFh_PI-PLCbeta1 cd16208
EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1); PI-PLC-beta1, ...
 123-273 1.95e-60

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


Pssm-ID: 320038  Cd Length: 151  Bit Score: 203.57  E-value: 1.95e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  123 EKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSH 202
Cdd:cd16208      1 EKAYTKLKLQVNPEGRIPVKNIYRLFSADRKRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDHIFSEF 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803860226  203 HLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 273
Cdd:cd16208     81 GAKSKPYLSVDQMTEFINSKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSTLAKKGQISVDGFMRYLSGEE 151
PLN02222 PLN02222
phosphoinositide phospholipase C 2
 193-779 1.20e-59

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 216.05  E-value: 1.20e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  193 PEIDEIFTSHhlKAKPYMTKEHLAKFINKKQRDSRlndilfppAKPEQVQSLIEKyepSGINIQRGQLSPEGMVWFLCGP 272
Cdd:PLN02222    25 REIKTIFEKY--SENGVMTVDHLHRFLIDVQKQDK--------ATREDAQSIINS---ASSLLHRNGLHLDAFFKYLFGD 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  273 ENNVIALDKLvlYQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIItHGFTM 352
Cdd:PLN02222    92 NNPPLALHEV--HHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSDKDDIDVL-HGMTL 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  353 TTEILFKDAIEAIAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKyPLKPgvpLPSPKDLLGKI 432
Cdd:PLN02222   169 TTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHL-TPDLQSKVAEMVTEIFGEILFTPPVGE-SLKE---FPSPNSLKKRI 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  433 LIKNKKNQSI-SGKRQNSLKKGRNVEPEII---EQPTPMDAEDTVWAGDVAeeepeeedehlGNLDEEEikkmqsDEGTA 508
Cdd:PLN02222   244 IISTKPPKEYkEGKDDEVVQKGKDLGDEEVwgrEVPSFIQRNKSVDKNDSN-----------GDDDDDD------DDGED 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  509 GLEVTAYEEMSSLVNyIQPIK-----FDSFEVSAQKNRSYVISSFTELKAYDlltKFPVQFVEYNKRQMSRIYPKGTRMD 583
Cdd:PLN02222   307 KSKKNAPPQYKHLIA-IHAGKpkggiTECLKVDPDKVRRLSLSEEQLEKAAE---KYAKQIVRFTQHNLLRIYPKGTRVT 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  584 SSNYMPQMFWNVGCQMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRRPDKQFDPFSvDRIDVVVASTLSVTASTS 663
Cdd:PLN02222   383 SSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKKPDLLLKSGSDSDIFD-PKATLPVKTTLRVTIYMG 461

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  664 HGAILS---GQFLSDRSVKTYVEVELFGLPRDTKRKyRTKlTSTANSInPVWKEeafVFE-KIMMPELASLKIVAWE--- 736
Cdd:PLN02222   462 EGWYFDfrhTHFDQYSPPDFYTRVGIAGVPGDTVMK-KTK-TLEDNWI-PAWDE---VFEfPLTVPELALLRLEVHEydm 535

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 1803860226  737 -EGGKFIGHRVIPVIAVHSGYHHVCLRSESNMPLTMPSLFVYLE 779
Cdd:PLN02222   536 sEKDDFGGQTCLPVWELSQGIRAFPLHSRKGEKYKSVKLLVKVE 579
PI-PLC-Y pfam00387
Phosphatidylinositol-specific phospholipase C, Y domain; This associates with pfam00388 to ...
 518-632 2.14e-58

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


Pssm-ID: 459794  Cd Length: 114  Bit Score: 196.14  E-value: 2.14e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  518 MSSLVNYIQPIKFDSFEvSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGC 597
Cdd:pfam00387    1 LSDLVVYTQSVKFKSFS-TPESKTPNHIFSFSESKALKLIKSSSAAFVKHNRRHLMRVYPKGTRVDSSNFNPQPFWNCGV 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1803860226  598 QMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEF 632
Cdd:pfam00387   80 QMVALNWQTPDEGMQLNEGMFADNGGCGYVLKPEF 114
PI-PLCc_plant cd08599
Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family ...
 285-621 6.55e-58

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


Pssm-ID: 176541 [Multi-domain]  Cd Length: 228  Bit Score: 199.52  E-value: 6.55e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  285 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDeePIITHGFTMTTEILFKDAIEA 364
Cdd:cd08599      1 HHDMTAPLSHYFIFSSHNSYLTGNQLSSRSSTAPIIEALLRGCRVIELDLWPGGRGD--ICVLHGGTLTKPVKFEDCIKA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  365 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPlekyPLKPGVPLPSPKDLLGKILIKNKknqsisg 444
Cdd:cd08599     79 IKENAFTASEYPVIITLENHL-SPELQAKAAQILRETLGDKLFYPD----SEDLPEEFPSPEELKGKILISDK------- 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  445 krqnslkkgrnvePEIIEqptpmdaedtvwagdvaeeepeeedehlGNLDEEEIKKMQSDEgtaglevtayeemsslvny 524
Cdd:cd08599    147 -------------PPVIR----------------------------NSLSETQLKKVIEGE------------------- 166

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  525 iqpikfdsfevsaqknrsyvissftelkaydlltkFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 604
Cdd:cd08599    167 -----------------------------------HPTDLIEFTQKNLLRVYPAGLRITSSNYDPMLAWMHGAQMVALNM 211

                          330
                   ....*....|....*..
gi 1803860226  605 QTMDVPMQQNMALFEFN 621
Cdd:cd08599    212 QGYDRPLWLNRGKFRAN 228
PLN02952 PLN02952
phosphoinositide phospholipase C
 284-776 1.18e-57

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 210.62  E-value: 1.18e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  284 LYQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDeEPIITHGFTMTTEILFKDAIE 363
Cdd:PLN02952   121 VHHDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGSTKD-EILVLHGRTLTTPVPLIKCLK 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  364 AIAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLteplekYPLKPG-VPLPSPKDLLGKILIKNK-KNQS 441
Cdd:PLN02952   200 SIRDYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLY------YPESDSlVQFPSPESLKHRIIISTKpPKEY 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  442 ISGKRQNSLKKGRNVEPEiIEQPTPMDAEdtvwagdvaeeePEEEDEHLGNLD-EEEIKKMQSDEGTAGLEVTAYEEMSS 520
Cdd:PLN02952   273 LESSGPIVIKKKNNVSPS-GRNSSEETEE------------AQTLESMLFEQEaDSRSDSDQDDNKSGELQKPAYKRLIT 339

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  521 lVNYIQP---IKfDSFEVSAQKNRSYvisSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGC 597
Cdd:PLN02952   340 -IHAGKPkgtLK-DAMKVAVDKVRRL---SLSEQELEKAATTNGQDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGA 414

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  598 QMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFM--RRPDKQ-FDPfsvdRIDVVVASTLSVTASTSHGAILS---GQ 671
Cdd:PLN02952   415 QMIAFNMQGYGKSLWLMHGMFRANGGCGYLKKPDFLmkKGFHDEvFDP----KKKLPVKKTLKVKVYLGDGWRLDfshTH 490

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  672 FLSDRSVKTYVEVELFGLPRDTKRKyRTKLTStaNSINPVWKEEaFVFeKIMMPELASLKIVAWE----EGGKFIGHRVI 747
Cdd:PLN02952   491 FDSYSPPDFYTKMYIVGVPADNAKK-KTKIIE--DNWYPAWNEE-FSF-PLTVPELALLRIEVREydmsEKDDFGGQTCL 565

                          490       500       510
                   ....*....|....*....|....*....|....
gi 1803860226  748 PVIAVHSGYHHVCLRSE-----SNMPLTMPSLFV 776
Cdd:PLN02952   566 PVSELRPGIRSVPLHDKkgeklKNVRLLMRFIFV 599
PLN02228 PLN02228
Phosphoinositide phospholipase C
 191-761 1.40e-54

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 200.65  E-value: 1.40e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  191 PRPEIDEIFTSHHLKAKpyMTKEHLAKFINKKQRDSRlndilfppAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLC 270
Cdd:PLN02228    22 PPVSIKRLFEAYSRNGK--MSFDELLRFVSEVQGERH--------AGLDYVQDIFHSVKHHNVFHHHGLVHLNAFYRYLF 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  271 GPENNVIALDKLVlYQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrPPDEEPIITHGF 350
Cdd:PLN02228    92 SDTNSPLPMSGQV-HHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWPN-PSGNAAEVRHGR 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  351 TMTTEILFKDAIEAIAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLkpgvpLPSPKDLLG 430
Cdd:PLN02228   170 TLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHL-PPNLQAQVAKMLTKTFRGMLFRCTSESTKH-----FPSPEELKN 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  431 KILIKNKKNQSIsgkrqnslkkgrnVEPEIIEQPTPMDAEDTVWAgDVAEEepeeedehlgnldEEEIKKMQSDEGTAGL 510
Cdd:PLN02228   244 KILISTKPPKEY-------------LESKTVQTTRTPTVKETSWK-RVADA-------------ENKILEEYKDEESEAV 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  511 EvtaYEEMSSL--VNYIQPIKfDSFEVSAQKNRSYvisSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYM 588
Cdd:PLN02228   297 G---YRDLIAIhaANCKDPLK-DCLSDDPEKPIRV---SMDEQWLETMVRTRGTDLVRFTQRNLVRIYPKGTRVDSSNYD 369

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  589 PQMFWNVGCQMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRRPDKQFDPFSvdriDVVVASTLSVTASTSHGAIL 668
Cdd:PLN02228   370 PHVGWTHGAQMVAFNMQGHGKQLWIMQGMFRANGGCGYVKKPRILLDEHTLFDPCK----RLPIKTTLKVKIYTGEGWDL 445

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  669 S---GQFLSDRSVKTYVEVELFGLPRDTKrKYRTKLtsTANSINPVWKEEAFVFEkIMMPELASL--KIVAWEEGGK--F 741
Cdd:PLN02228   446 DfhlTHFDQYSPPDFFVKIGIAGVPRDTV-SYRTET--AVDQWFPIWGNDEFLFQ-LRVPELALLwfKVQDYDNDTQndF 521

                          570       580
                   ....*....|....*....|
gi 1803860226  742 IGHRVIPVIAVHSGYHHVCL 761
Cdd:PLN02228   522 AGQTCLPLPELKSGVRAVRL 541
EFh_PI-PLCbeta3 cd16210
EF-hand motif found in phosphoinositide phospholipase C beta 3 (PI-PLC-beta3); PI-PLC-beta3, ...
 123-273 3.67e-49

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


Pssm-ID: 320040  Cd Length: 151  Bit Score: 171.25  E-value: 3.67e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  123 EKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSH 202
Cdd:cd16210      1 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILLEI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803860226  203 HLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 273
Cdd:cd16210     81 GAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQVRQLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 151
EFh_PI-PLC21 cd16213
EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family ...
 123-269 2.14e-48

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


Pssm-ID: 320043  Cd Length: 154  Bit Score: 169.40  E-value: 2.14e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  123 EKILVKLKMQLNAEGKIPVRNIFQMFPA---DRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIF 199
Cdd:cd16213      1 EKAYTKLTLQTDKEGKIPVKNIVKMFAQhkdDRKRVEKALEAIGLPSGKNDAIDPKKFTFEDFFNFYRRLTGRQEVEKIF 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  200 TSHHLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFL 269
Cdd:cd16213     81 DELGAKKKPYLTTEQFVDFLNKTQRDPRLNEILYPYANPKRARDLINQYEPNKSFAKKGHLSVEGFLRYL 150
PLN02230 PLN02230
phosphoinositide phospholipase C 4
 284-779 5.23e-46

phosphoinositide phospholipase C 4


Pssm-ID: 177875 [Multi-domain]  Cd Length: 598  Bit Score: 176.05  E-value: 5.23e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  284 LYQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKgRPPDEePIITHGFTMTTEILFKDAIE 363
Cdd:PLN02230   113 VHQNMDAPLSHYFIFTGHNSYLTGNQLSSNCSELPIADALRRGVRVVELDLWP-RGTDD-VCVKHGRTLTKEVKLGKCLD 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  364 AIAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPlkpgvPLPSPKDLLGKILIKNKKNQSI- 442
Cdd:PLN02230   191 SIKANAFAISKYPVIITLEDHL-TPKLQFKVAKMITQTFGDMLYYHDSEGCQ-----EFPSPEELKEKILISTKPPKEYl 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  443 ---SGKRQNSLKKGRnvepeiieqptpmDAEDTVWAGD-----VAEEEPEEEDEHLGNL--DEEEIKKMQSDEgTAGLEV 512
Cdd:PLN02230   265 eanDAKEKDNGEKGK-------------DSDEDVWGKEpedliSTQSDLDKVTSSVNDLnqDDEERGSCESDT-SCQLQA 330

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  513 TAYEEMSSlVNYIQP---IKFdSFEVSAQKNRSYVISSFTELKAydlLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMP 589
Cdd:PLN02230   331 PEYKRLIA-IHAGKPkggLRM-ALKVDPNKIRRLSLSEQLLEKA---VASYGADVIRFTQKNFLRIYPKGTRFNSSNYKP 405

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  590 QMFWNVGCQMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRRPDKQFDPFsVDRIDVVVASTLSVTASTSHGAIL- 668
Cdd:PLN02230   406 QIGWMSGAQMIAFNMQGYGRALWLMEGMFRANGGCGYVKKPDFLMDAGPNGQDF-YPKDNSCPKKTLKVKVCMGDGWLLd 484

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  669 --SGQFLSDRSVKTYVEVELFGLPRDTKRKyRTKLTStaNSINPVWKEEaFVFeKIMMPELASLKIVAWE----EGGKFI 742
Cdd:PLN02230   485 fkKTHFDSYSPPDFFVRVGIAGAPVDEVME-KTKIEY--DTWTPIWNKE-FIF-PLAVPELALLRVEVHEhdinEKDDFG 559

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1803860226  743 GHRVIPVIAVHSGYHHVCLRSESNMPLTMPSLFVYLE 779
Cdd:PLN02230   560 GQTCLPVSEIRQGIHAVPLFNRKGVKYSSTRLLMRFE 596
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-115 2.77e-41

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


Pssm-ID: 465506  Cd Length: 131  Bit Score: 147.91  E-value: 2.77e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226   12 EVKEYLSKGERFIKWDD---------------------------EMEILDITSIRDTRVGRFAKIPKCQKLREVFNLDYP 64
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEestvaepnvllkvdpkgfflywksqgkEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1803860226   65 HSTFLLKTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVRNPLTYN 115
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-118 4.68e-35

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


Pssm-ID: 270167  Cd Length: 127  Bit Score: 130.00  E-value: 4.68e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226   17 LSKGERFIKWDD--------------------------EMEILDITSIRDTRVGRFAKIPKCQKLREVfNLDYPHSTFLL 70
Cdd:cd13361      1 LLKGSKFDKWDEdssletpvtlkvdeygfflywksegkETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1803860226   71 KTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVRNPLTYNASR 118
Cdd:cd13361     80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 655-781 1.28e-33

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: 125.73  E-value: 1.28e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  655 TLSVTastshgaILSGQFLSD------RSVKTYVEVELFGLPRDTKRKYRTKlTSTANSINPVWkEEAFVFEkIMMPELA 728
Cdd:cd00275      3 TLTIK-------IISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAKFKTK-VVKNNGFNPVW-NETFEFD-VTVPELA 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1803860226  729 SLKIVAWEEGG---KFIGHRVIPVIAVHSGYHHVCLRSESNMPLTMPSLFVYLEIK 781
Cdd:cd00275     73 FLRFVVYDEDSgddDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
 128-269 2.84e-31

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


Pssm-ID: 320041  Cd Length: 153  Bit Score: 120.22  E-value: 2.84e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  128 KLKMQLNAEGKIPVRNIFQMFPADR--KRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSHHLK 205
Cdd:cd16211      6 RLCFLVNPNGKIPVRSITRTFASGKteKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFKKINGD 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1803860226  206 AKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFL 269
Cdd:cd16211     86 KKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYL 149
PLN02223 PLN02223
phosphoinositide phospholipase C
 283-770 4.05e-27

phosphoinositide phospholipase C


Pssm-ID: 165867 [Multi-domain]  Cd Length: 537  Bit Score: 117.43  E-value: 4.05e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  283 VLYQDMTQPLSHYFINSSHNTYLTAGQ-FSGISSPEMYRQTLLAGCRCVELDCWkgrPPDEEPI-ITHGFTMTTEILFKD 360
Cdd:PLN02223   103 VRHHDMHAPLSHYFIHTSLKSYFTGNNvFGKLYSIEPIIDALEQGVRVVELDLL---PDGKDGIcVRPKWNFEKPLELQE 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  361 AIEAIAESAF-KTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPlekyPLKPGVPLPSPKDLLGKILIKNKKN 439
Cdd:PLN02223   180 CLDAIKEHAFtKCRSYPLIITFKDGL-KPDLQSKATQMIDQTFGDMVYHED----PQHSLEEFPSPAELQNKILISRRPP 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  440 QSISGKRQNSLKKGRNVEPEIIEQPTPMDAEDTVwagdvaeeepeeedehlgnldeeeikkmqsdegtaGLEVTayeEMS 519
Cdd:PLN02223   255 KELLYAKADDGGVGVRNELEIQEGPADKNYQSLV-----------------------------------GFHAV---EPR 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  520 SLVNYIQPIKFDSFEVSAQKNRSyvISSFTELKaydLLTKFPvqfveynKRQMSRIYPKgtrmdssnYMPQMFWNVGCQM 599
Cdd:PLN02223   297 GMLQKALTGKADDIQQPGWYERD--IISFTQKK---FLRTRP-------KKKNLLINAP--------YKPQRAWMHGAQL 356

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  600 VALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRR--PDKQFDPfsvdRIDVVVASTLSVTASTSHGAILSGQFLSDRS 677
Cdd:PLN02223   357 IALSRKDDKEKLWLMQGMFRANGGCGYVKKPDFLLNagPSGVFYP----TENPVVVKILKVKIYMGDGWIVDFKKRIGRL 432

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  678 VKT--YVEVELFGLPRDTKrkyRTKLTSTANSINPVWKEEaFVFeKIMMPELA--SLKIVAWE--EGGKFIGHRVIPVIA 751
Cdd:PLN02223   433 SKPdlYVRISIAGVPHDEK---IMKTTVKNNEWKPTWGEE-FTF-PLTYPDLAliSFEVYDYEvsTADAFCGQTCLPVSE 507

                          490       500
                   ....*....|....*....|....*
gi 1803860226  752 VHSGYHHVCLRSE------SNMPLT 770
Cdd:PLN02223   508 LIEGIRAVPLYDErgkacsSTMLLT 532
EFh_NorpA_like cd16212
EF-hand motif found in Drosophila melanogaster No receptor potential A protein (NorpA) and ...
 127-273 5.29e-25

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


Pssm-ID: 320042 [Multi-domain]  Cd Length: 153  Bit Score: 102.24  E-value: 5.29e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  127 VKLKMQLNAEGKIPVRNIFQMFPADR--KRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSHHL 204
Cdd:cd16212      5 MRLGFMVDSGGKIPVKHIARTFASGKteKLVYQCLAEMGLPSGKGDSIEKEDFTFEKFYALYHKICPRNDIEELFTSITK 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1803860226  205 KAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 273
Cdd:cd16212     85 GKGEHISLAQLINFMNDKQRDPRLNEILYPLYDEKRCTEIIKAYEQNEENIKNKRMSKDGFIRYLMSDE 153
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 298-604 1.48e-23

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


Pssm-ID: 176498 [Multi-domain]  Cd Length: 179  Bit Score: 99.05  E-value: 1.48e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  298 NSSHNTYLTAGQfsgISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMT------TEILFKDAIEAIAESAFK 371
Cdd:cd08555      1 VLSHRGYSQNGQ---ENTLEAFYRALDAGARGLELDVRLT--KDGELVVYHGPTLDrttagiLPPTLEEVLELIADYLKN 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  372 TSlYPVILSFENHVDS---PKQQAKMAEYCRTIFGDmllteplekyplkpgvplpspkDLLGKILIKnkknqsisgkrqn 448
Cdd:cd08555     76 PD-YTIILSLEIKQDSpeyDEFLAKVLKELRVYFDY----------------------DLRGKVVLS------------- 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  449 slkkgrnvepeiieqptpmdaedtvwagdvaeeepeeedehlgnldeeeikkmqsdegtaglevtayeemsslvnyiqpi 528
Cdd:cd08555        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1803860226  529 kfdsfevsaqknrSYVISSFTELKAYDLLTKFPVQFVEYNK-RQMSRIYPKGTrmdsSNYMPQMFWNVGCQMVALNF 604
Cdd:cd08555    120 -------------SFNALGVDYYNFSSKLIKDTELIASANKlGLLSRIWTVND----NNEIINKFLNLGVDGLITDF 179
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 169-273 1.34e-13

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


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 69.18  E-value: 1.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  169 NDAINPEDFpetvyKTFLMNLCPRPEIDEIFTSHHlKAKPYMTKEHLAKFINKKQRdsrlndilFPPAKPEQVQSLIEKY 248
Cdd:cd16202     50 EDVLDEEEF-----VQFYNRLTKRPEIEELFKKYS-GDDEALTVEELRRFLQEEQK--------VKDVTLEWAEQLIETY 115

                           90       100
                   ....*....|....*....|....*
gi 1803860226  249 EPSGINIQRGQLSPEGMVWFLCGPE 273
Cdd:cd16202    116 EPSEDLKAQGLMSLDGFTLFLLSPD 140
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 129-273 1.42e-10

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 60.37  E-value: 1.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  129 LKMQLNAEGKIPVRNIFQM-----FPADRKRVEAALSACHlpKGKNDAINPEDFpetvyKTFLMNLCPRPEIDEIFTSHH 203
Cdd:cd15898      7 IKADKDGDGKLSLKEIKKLlkrlnIRVSEKELKKLFKEVD--TNGDGTLTFDEF-----EELYKSLTERPELEPIFKKYA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  204 LKAKPYMTKEHLAKFINKKQRDSRlndilfppaKPEQVQSLIEKYEPSGiniQRGQLSPEGMVWFLCGPE 273
Cdd:cd15898     80 GTNRDYMTLEEFIRFLREEQGENV---------SEEECEELIEKYEPER---ENRQLSFEGFTNFLLSPE 137
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 667-761 4.76e-10

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: 57.88  E-value: 4.76e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226   667 ILSGQFLSDR----SVKTYVEVELFGlprDTKRKYRTKltSTANSINPVWKEEaFVFEkIMMPELASLKIVAWEEGG--- 739
Cdd:smart00239    6 IISARNLPPKdkggKSDPYVKVSLDG---DPKEKKKTK--VVKNTLNPVWNET-FEFE-VPPPELAELEIEVYDKDRfgr 78

                            90       100
                    ....*....|....*....|...
gi 1803860226   740 -KFIGHRVIPVIAVHSGYHHVCL 761
Cdd:smart00239   79 dDFIGQVTIPLSDLLLGGRHEKL 101
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 189-276 1.21e-07

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


Pssm-ID: 401279 [Multi-domain]  Cd Length: 85  Bit Score: 50.32  E-value: 1.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  189 LCPRPEIDEIFTSHHlKAKPYMTKEHLAKFINKKQRDSRlndilfppAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWF 268
Cdd:pfam09279    5 LTQREEIDEIFQEYS-GDGQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAMTKDGFLMY 75


                   ....*...
gi 1803860226  269 LCGPENNV 276
Cdd:pfam09279   76 LCSPDGSI 83
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
 183-273 2.04e-06

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


Pssm-ID: 320047 [Multi-domain]  Cd Length: 139  Bit Score: 48.58  E-value: 2.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  183 KTFLMNLCPRPEIDEIFTSHHlKAKPYMTKEHLAKFINKKQRDsrlndilfpPAKPEQVQSLIEKYEPSGINIQRGQLSP 262
Cdd:cd16217     59 EEFYKLLTKREEIDVIFGEYA-KSDGTMSRNNLLNFLQEEQRE---------EVAPAYALSLIEKYEPDETAKAQRQMTK 128

                           90
                   ....*....|.
gi 1803860226  263 EGMVWFLCGPE 273
Cdd:cd16217    129 DGFLMYLLSPE 139
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 895-1103 2.20e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 52.05  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  895 RELER-------KGHKRREEL--LQKYSVLFSEpvcyRGKKRMIHARKTQKKRSlatgdvgtcanPVEMAESIDSRVLEL 965
Cdd:pfam17380  378 RELERlqmerqqKNERVRQELeaARKVKILEEE----RQRKIQQQKVEMEQIRA-----------EQEEARQREVRRLEE 442

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  966 RERLEMDLIQLGE-EHHGGIRRKKEQHAtEQVTKIIELAREKQTAEL----------KALKESSESNIKDIKKK--LEAK 1032
Cdd:pfam17380  443 ERAREMERVRLEEqERQQQVERLRQQEE-ERKRKKLELEKEKRDRKRaeeqrrkileKELEERKQAMIEEERKRklLEKE 521

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803860226 1033 RVDRIQTMMRNTSDKAAQERLKKEINNSHIQEVVQTIKLVTEKTARYQQKleEKQADNLRTIKEKESQLQQ 1103
Cdd:pfam17380  522 MEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM--EREREMMRQIVESEKARAE 590
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 965-1160 1.70e-05

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 49.33  E-value: 1.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  965 LRERLEMDLIQLGEEHHGGIRRKKEQHATEQVTKIIELAREKQTAELKALKESSESNIKDIKKKLEAKRVDRIQTM---- 1040
Cdd:pfam05483  599 LKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLeeve 678

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1041 -MRNTSDKAAqeRLKKEINNSHIQEVVQTIKLVTEKTARYQQKLEEKQADnLRTIKEKEsQLQQEALAEYEEKLKSLNME 1119
Cdd:pfam05483  679 kAKAIADEAV--KLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSE-LGLYKNKE-QEQSSAKAALEIELSNIKAE 754

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1803860226 1120 VQEMVKnytkagfpgQPEAQKEAVQSIPEGEQGSTAQLEEK 1160
Cdd:pfam05483  755 LLSLKK---------QLEIEKEEKEKLKMEAKENTAILKDK 786
C2 pfam00168
C2 domain;
667-749 2.38e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 44.23  E-value: 2.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  667 ILSGQFL----SDRSVKTYVEVELfglpRDTKRKYRTKLTStaNSINPVWKEEaFVFEkIMMPELASLKIVAWEEGG--- 739
Cdd:pfam00168    7 VIEAKNLppkdGNGTSDPYVKVYL----LDGKQKKKTKVVK--NTLNPVWNET-FTFS-VPDPENAVLEIEVYDYDRfgr 78

                           90
                   ....*....|.
gi 1803860226  740 -KFIGHRVIPV 749
Cdd:pfam00168   79 dDFIGEVRIPL 89
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1003-1159 1.37e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1003 AREKQTAELKALKESSESNIKDIKKKLEAKRVDRIQTMMRNTSDKAAQERLKKEINN--SHIQEVVQTIKLVTEKTARYQ 1080
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaNEISRLEQQKQILRERLANLE 315

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1803860226 1081 QKLEEKQADNLRtiKEKESQLQQEALAEYEEKLKSLNMEVQEMvknytkagfpgqPEAQKEAVQSIPEGEQGSTAQLEE 1159
Cdd:TIGR02168  316 RQLEELEAQLEE--LESKLDELAEELAELEEKLEELKEELESL------------EAELEELEAELEELESRLEELEEQ 380
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
 126-273 2.55e-04

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


Pssm-ID: 320035 [Multi-domain]  Cd Length: 141  Bit Score: 42.37  E-value: 2.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  126 LVKLKMQLNAegKIPVRNIFQMF-PADRKRVEAALsachlpkgkndainpeDFPEtvYKTFLMNLCPRPEIDEIFTSHHL 204
Cdd:cd16205     22 ILQLMHKLNV--NLPRRKVRQMFkEADTDDNQGTL----------------DFEE--FCAFYKMMSTRRELYLLLLSYSN 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1803860226  205 KaKPYMTKEHLAKFINKKQRDSRLNDilfppakpEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 273
Cdd:cd16205     82 K-KDYLTLEDLARFLEVEQKMTNVTL--------EYCLDIIEKFEPSEENKKNGLLGIDGFTNYMRSPA 141
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 978-1118 3.49e-04

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 43.11  E-value: 3.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  978 EEHHGGIRRKKEQHaTEQVTKIIELAREK---------QTAELK----ALKESSESNIKDIKK----------------- 1027
Cdd:pfam15665   10 DEHEAEIQALKEAH-EEEIQQILAETREKilqykskigEELDLKrriqTLEESLEQHERMKRQaltefeqykrrveerel 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1028 KLEAKRVDRIQTMMRNTSD--KAAQERLK--------------------KEINNSHIQEVVQTIKLVTEKTARYQQKLEE 1085
Cdd:pfam15665   89 KAEAEHRQRVVELSREVEEakRAFEEKLEsfeqlqaqfeqekrkaleelRAKHRQEIQELLTTQRAQSASSLAEQEKLEE 168

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1803860226 1086 KQADNLRTIKEKESQLQQE---ALAEYEEKLKSLNM 1118
Cdd:pfam15665  169 LHKAELESLRKEVEDLRKEkkkLAEEYEQKLSKAQA 204
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 896-1161 4.00e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 4.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  896 ELERKGHKRREELLQKYSVLFSEPVCYR----GKKRMIHARKTQKKRSLATgdVGTCANPVEMAESIDSRVLELRERLEM 971
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRkeleELSRQISALRKDLARLEAE--VEQLEERIAQLSKELTELEAEIEELEE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  972 DLIQLGEEHHGGIRRKKEQHAT-----EQVTKIIELAREKQtAELKALKEssESNIKDIKKKLEAKRVDRIQTMMRNTSD 1046
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQieqlkEELKALREALDELR-AELTLLNE--EAANLRERLESLERRIAATERRLEDLEE 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1047 KAAQ-----ERLKKEINNSHIQEVVQTIKLvTEKTARYQQKLE-----EKQADNLR-TIKEKESQLQ--QEALAEYEEKL 1113
Cdd:TIGR02168  846 QIEElsediESLAAEIEELEELIEELESEL-EALLNERASLEEalallRSELEELSeELRELESKRSelRRELEELREKL 924

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1114 KSLNMEVQ--EMVKNYTKAGFPGQPEAQKEAVQSIPEGEQGSTAQLEEKI 1161
Cdd:TIGR02168  925 AQLELRLEglEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL 974
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1005-1161 5.25e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 5.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1005 EKQTAELKALKESSESNIKDIKKKLEAKRVDRIQTMMRNTSDKAAQERLKKEINNSHIQEVVQTIKLvtEKTARYQQK-- 1082
Cdd:COG3883     22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL--GERARALYRsg 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1083 -----LEE-----------KQADNLRTIKEKESQL---QQEALAEYEEKLKSLNMEVQEMVKNYTKAgfpgqpEAQKEAV 1143
Cdd:COG3883    100 gsvsyLDVllgsesfsdflDRLSALSKIADADADLleeLKADKAELEAKKAELEAKLAELEALKAEL------EAAKAEL 173

                          170
                   ....*....|....*...
gi 1803860226 1144 QSIPEGEQGSTAQLEEKI 1161
Cdd:COG3883    174 EAQQAEQEALLAQLSAEE 191
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 955-1188 5.62e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 5.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  955 AESIDSRVLELRERLEmdliQLGEEhhggIRRKKEQHATEQvTKIIELARE--KQTAELKALKESSESNIKDIKKK---- 1028
Cdd:COG3883     32 LEAAQAELDALQAELE----ELNEE----YNELQAELEALQ-AEIDKLQAEiaEAEAEIEERREELGERARALYRSggsv 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1029 ------LEAK-------RVDRIQTMMRNT--------SDKAAQERLKKEINNShIQEVVQTiklvtektaryQQKLEEKQ 1087
Cdd:COG3883    103 syldvlLGSEsfsdfldRLSALSKIADADadlleelkADKAELEAKKAELEAK-LAELEAL-----------KAELEAAK 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1088 ADNLRTIKEKESQLQQ--EALAEYEEKLKSLNMEVQEMVKNYTKAGFPGQPEAQKEAVQSIPEGEQGSTAQLEEKIPVAE 1165
Cdd:COG3883    171 AELEAQQAEQEALLAQlsAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250

                          250       260
                   ....*....|....*....|...
gi 1803860226 1166 VSRLTIAVPEPPGAETDVEIEES 1188
Cdd:COG3883    251 AAGAAGAAAGSAGAAGAAAGAAG 273
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1002-1187 7.00e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 7.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1002 LAREKQTAELKALKESSESNIKDIKKKLEAKRVDRiqtmmrntSDKAAQERLKKEINNSHIQEVVQTIKLVTEKTARyQQ 1081
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKEL--------EELEEELEQLRKELEELSRQISALRKDLARLEAE-VE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1082 KLEEKQADNLRTIKEKESQLQ---------QEALAEYEEKLKSLNMEVQEMVK-----NYTKAGFPGQPEAQKEAVQSIP 1147
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEeleerleeaEEELAEAEAEIEELEAQIEQLKEelkalREALDELRAELTLLNEEAANLR 823

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1803860226 1148 EGEQGSTAQLEEKIPVAEVSRLTIAVPEPPGAETDVEIEE 1187
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 953-1146 7.68e-04

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


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 43.48  E-value: 7.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  953 EMAESIDSRVLELRE---RLEMDLIQLGEEhhggIRRKKEQHAT--EQV---TKIIELAR--EKQTAELKALKESSESNI 1022
Cdd:pfam05667  342 EQLEDLESSIQELEKeikKLESSIKQVEEE----LEELKEQNEEleKQYkvkKKTLDLLPdaEENIAKLQALVDASAQRL 417

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1023 KDIKKKLEAKRVDRIQTMmrntsdkaaqERLKKEInnshiqevvqtiklvTEKTARYQQKLEEKQAdnLRT-IKEKESQL 1101
Cdd:pfam05667  418 VELAGQWEKHRVPLIEEY----------RALKEAK---------------SNKEDESQRKLEEIKE--LREkIKEVAEEA 470

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1803860226 1102 QQ--EALAEYEEKLKSLNMEVQ---------EMVKNYTKagfpgqpeaQKEAVQSI 1146
Cdd:pfam05667  471 KQkeELYKQLVAEYERLPKDVSrsaytrrilEIVKNIKK---------QKEEITKI 517
DUF874 pfam05917
Helicobacter pylori protein of unknown function (DUF874); This family consists of several ...
 992-1156 8.17e-04

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


Pssm-ID: 283549 [Multi-domain]  Cd Length: 398  Bit Score: 43.30  E-value: 8.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  992 ATEQVTKIIELAREKQTAElkalKESSESNIKDIKKKLEAKRVDRIQTMMRNTSDKAAQERLKKEINNSHIQEVVQTIKL 1071
Cdd:pfam05917  119 SAGDTDEQIELEQEKKEAE----NAEDRANKNGIELEQEKQKTNKSGIELANNQIKAEQEQQKTEQEKQKAEKEAIELEQ 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1072 VTEKTARYQQKLEEKQADnlrTIKEKESQLQQEALAEYEEKL---KSLNMEVQEMVKNYTKAG---FPGQPEAQKEAVQs 1145
Cdd:pfam05917  195 EKQKTIKTQRDLIKEQKD---FIKETEQNCQENHNQFFIEKGgikAGIAIEVEAECKTPKPAKtnqTPIQPKHLPNSKQ- 270

                          170
                   ....*....|.
gi 1803860226 1146 iPEGEQGSTAQ 1156
Cdd:pfam05917  271 -PHSQRGSKAQ 280
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 994-1130 8.68e-04

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


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 41.48  E-value: 8.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  994 EQVTKIIELAREKQTAELKALKESSESNIKDIKKKLEAKRvDRIQTMMRNTSDKAAQeRLK---KEINNSHIQEVVQTIK 1070
Cdd:pfam01442   18 EQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYL-EELQAKLGQNVEELRQ-RLEpytEELRKRLNADAEELQE 95

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1803860226 1071 LVTEKTARYQQKLEEKQ----------ADNLR-TIKEKESQLQQ---EALAEYEEKLKSLNMEVQEMVKNYTKA 1130
Cdd:pfam01442   96 KLAPYGEELRERLEQNVdalrarlapyAEELRqKLAERLEELKEslaPYAEEVQAQLSQRLQELREKLEPQAED 169
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 984-1122 9.43e-04

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


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 43.21  E-value: 9.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  984 IRRKKEQHATEQVTKIIELAREKQTAELKALKESSESNIKDIKKKLEAKRVdRIQTMMRNtSDKAAQERlKKEINNSHIQ 1063
Cdd:pfam09731  306 LKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFERERE-EIRESYEE-KLRTELER-QAEAHEEHLK 382

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1803860226 1064 EVVQTIKLvtEKTARYQQKLEEKQadnlrtikEKESQLQQEALAEYEEKLKSLNMEVQE 1122
Cdd:pfam09731  383 DVLVEQEI--ELQREFLQDIKEKV--------EEERAGRLLKLNELLANLKGLEKATSS 431
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 986-1161 9.68e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 9.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  986 RKKEQHATEQV----TKIIELAR-----EKQTAELKALKESSESNIKDIKKKLEAKRvDRIQTMMRNTSDKAAQERLKKE 1056
Cdd:COG4942     47 KKEEKALLKQLaaleRRIAALARriralEQELAALEAELAELEKEIAELRAELEAQK-EELAELLRALYRLGRQPPLALL 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1057 INNSHIQEVVQTIKLVtEKTARYQQKLEEKQADNLRTIKEKESQLQQE------ALAEYEEKLKSLNMEVQEmvKNYTKA 1130
Cdd:COG4942    126 LSPEDFLDAVRRLQYL-KYLAPARREQAEELRADLAELAALRAELEAEraeleaLLAELEEERAALEALKAE--RQKLLA 202

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1803860226 1131 GFPGQPEAQKEAVQSIpegeQGSTAQLEEKI 1161
Cdd:COG4942    203 RLEKELAELAAELAEL----QQEAEELEALI 229
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 984-1115 1.01e-03

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


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 42.00  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  984 IRRKKEQHATEQVTKIIELAREKQTAELKalKESSESNIKD-IKKKLEAKRVDRIQTMMRNTSDKAAQERLKKEINNSH- 1061
Cdd:pfam13904   61 LAAKQRQRQKELQAQKEEREKEEQEAELR--KRLAKEKYQEwLQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQe 138

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1803860226 1062 -IQEVVQTIKLvtEKTARYQQKLEEKQADNLRTiKEKESQLQQEALAEYEEKLKS 1115
Cdd:pfam13904  139 eAKEVLQEWER--KKLEQQQRKREEEQREQLKK-EEEEQERKQLAEKAWQKWMKN 190
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 998-1189 1.03e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 43.07  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  998 KIIELAREKQTAELKALKESSEsnIKDIKKKLEAKRvdriqtmmrntSDKAAQERLKKEINNSHIQEVVQTIKL---VTE 1074
Cdd:pfam05262  181 KVVEALREDNEKGVNFRRDMTD--LKERESQEDAKR-----------AQQLKEELDKKQIDADKAQQKADFAQDnadKQR 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1075 KTARYQQKLEEKQADNLRTIKEKE-SQLQQEALAEYEEKLKSLNMEVQEMVKNYTKAGFpgqpEAQKEAVQSIPEGEQGS 1153
Cdd:pfam05262  248 DEVRQKQQEAKNLPKPADTSSPKEdKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAF----DLKQESKASEKEAEDKE 323

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1803860226 1154 TAQLEEKIPVAE-VSRLTIAVPEPPGAETDVEIEESI 1189
Cdd:pfam05262  324 LEAQKKREPVAEdLQKTKPQVEAQPTSLNEDAIDSSN 360
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 994-1177 1.05e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  994 EQVTKIIELAR-EKQTAELKALKESSESNIKDIKKKLEAKRvDRIQTMmrntsdKAAQERLKKEINNSHIQevvqtIKLV 1072
Cdd:COG1579      4 EDLRALLDLQElDSELDRLEHRLKELPAELAELEDELAALE-ARLEAA------KTELEDLEKEIKRLELE-----IEEV 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1073 TEKTARYQQKLEE----KQADNLrtikEKESQLQQEALAEYEEKLKSLNMEVQEMVKNYTKAgfpgqpEAQKEAVQSIPE 1148
Cdd:COG1579     72 EARIKKYEEQLGNvrnnKEYEAL----QKEIESLKRRISDLEDEILELMERIEELEEELAEL------EAELAELEAELE 141

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1803860226 1149 GEQGS----TAQLEEKIPVAEVSRLTIAVPEPP 1177
Cdd:COG1579    142 EKKAEldeeLAELEAELEELEAEREELAAKIPP 174
PTZ00121 PTZ00121
MAEBL; Provisional
 903-1149 1.08e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  903 KRREELLQKYSVLFSEPVCYRGKKRMIHARKTQKKRSLATGDVGTCANPVEMAESIDSRVL--ELRERLEMDLIQLGEEH 980
Cdd:PTZ00121  1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEE 1631

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  981 HGGIRRKKEQHAtEQVTKIIELAREKQTAELKALKESSESNiKDIKKKLEAKRVDRiqtmmrntSDKAAQERLKKEinns 1060
Cdd:PTZ00121  1632 KKKVEQLKKKEA-EEKKKAEELKKAEEENKIKAAEEAKKAE-EDKKKAEEAKKAEE--------DEKKAAEALKKE---- 1697

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1061 hiQEVVQTIKLVTEKTARYQQKLEE-KQADNLRTIKEKESQLQQEalaeyEEKLKSLNMEVQEMVKN----YTKAGFPGQ 1135
Cdd:PTZ00121  1698 --AEEAKKAEELKKKEAEEKKKAEElKKAEEENKIKAEEAKKEAE-----EDKKKAEEAKKDEEEKKkiahLKKEEEKKA 1770

                          250
                   ....*....|....
gi 1803860226 1136 PEAQKEAVQSIPEG 1149
Cdd:PTZ00121  1771 EEIRKEKEAVIEEE 1784
PTZ00121 PTZ00121
MAEBL; Provisional
 926-1169 1.14e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  926 KRMIHARKTQKKRSLATGDVGTCANPVEMAEsidsRVLELRERLEmdlIQLGEEhhggIRRKKEQHATEQVTKIIELARE 1005
Cdd:PTZ00121  1152 KRVEIARKAEDARKAEEARKAEDAKKAEAAR----KAEEVRKAEE---LRKAED----ARKAEAARKAEEERKAEEARKA 1220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1006 KQTAELKALKESSESNikdiKKKLEAKRVDRIqtmmRNTSdkaaQERLKKEINNSHIQEVVQTIKLVTEKTARYQQKLEE 1085
Cdd:PTZ00121  1221 EDAKKAEAVKKAEEAK----KDAEEAKKAEEE----RNNE----EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1086 -KQADNLRTIKEKESQLQQEALAEYEEKLKSLNMEVQEMVKNYTKAgfPGQPEAQKEAVQSIPEGEQGSTAQLEEKIPVA 1164
Cdd:PTZ00121  1289 kKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAA--KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366


                   ....*
gi 1803860226 1165 EVSRL 1169
Cdd:PTZ00121  1367 EAAEK 1371
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 953-1161 1.28e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  953 EMAESIDSRVLELRERLEMDL---IQLGEEHHGGIRRKKEQHATEQVtKIIELAREKQTAELKALKESSESNI--KDIKK 1027
Cdd:TIGR00618  584 EDIPNLQNITVRLQDLTEKLSeaeDMLACEQHALLRKLQPEQDLQDV-RLHLQQCSQELALKLTALHALQLTLtqERVRE 662

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1028 KLEAKRVDRIQTMMRNTSDKAAQERLKKEINN-----SHIQEVVQTIKLVTEKTARYQQKLEEKQADNLRTIKEKES--- 1099
Cdd:TIGR00618  663 HALSIRVLPKELLASRQLALQKMQSEKEQLTYwkemlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDaln 742

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1803860226 1100 QLQQEALAEYEEKLKSLNMEVQEMVKNYTKAGFPGQPEAQKEAV----QSIPEGEQGSTAQLEEKI 1161
Cdd:TIGR00618  743 QSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEiqffNRLREEDTHLLKTLEAEI 808
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1037-1165 1.39e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1037 IQTMMRNTSDKAAQERLKK-----EINNSHIQEVVQTIKLVTEKTARYQQKLEEKQA--DNLRTIKEKESQLQQE----- 1104
Cdd:COG4717     43 IRAMLLERLEKEADELFKPqgrkpELNLKELKELEEELKEAEEKEEEYAELQEELEEleEELEELEAELEELREElekle 122

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1803860226 1105 ---ALAEYEEKLKSLNMEVQEmvknytkagFPGQPEAQKEAVQSIpegeqgstAQLEEKIPVAE 1165
Cdd:COG4717    123 kllQLLPLYQELEALEAELAE---------LPERLEELEERLEEL--------RELEEELEELE 169
AhaH TIGR02926
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
 956-1033 1.40e-03

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


Pssm-ID: 131972 [Multi-domain]  Cd Length: 85  Bit Score: 39.06  E-value: 1.40e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1803860226  956 ESIDSRVLELRERLEmDLIQLGEEHHGGIRRKKEQHATEQVTKIIELAREKQTAELKALKESSESNIKDIKKKLEAKR 1033
Cdd:TIGR02926    9 EDAEELIEEAEEERK-QRIAEAREEARELLEEAEEEASKLGEEIIKEAEEEIEKEAEKIREEGEKEIEAMKSKAKEKI 85
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 931-1122 1.67e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  931 ARKTQKKRSLATGDVGTCANpVEMAESI---DSRVLELRERlEMDLIQLGEehhggirRKKEQHATEQVTKIIELAREKq 1007
Cdd:pfam17380  309 AREVERRRKLEEAEKARQAE-MDRQAAIyaeQERMAMERER-ELERIRQEE-------RKRELERIRQEEIAMEISRMR- 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1008 taELKALKESSESNIKDIKKKLEAKRVDRIQTMMRN---TSDKAAQERLKKEINNSHIQEVvqtiklvtektaryqQKLE 1084
Cdd:pfam17380  379 --ELERLQMERQQKNERVRQELEAARKVKILEEERQrkiQQQKVEMEQIRAEQEEARQREV---------------RRLE 441

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1803860226 1085 EKQADNLRTIKEKESQLQQ--EALAEYEE--KLKSLNMEVQE 1122
Cdd:pfam17380  442 EERAREMERVRLEEQERQQqvERLRQQEEerKRKKLELEKEK 483
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 956-1142 1.87e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.19  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  956 ESIDSRVLELR---ERLEMDLIQLGEEHHGGIRRKKEqhateqvtkiIELAREKQTAELKALKESSESNIKDIkKKLEak 1032
Cdd:pfam07888   69 EQWERQRRELEsrvAELKEELRQSREKHEELEEKYKE----------LSASSEELSEEKDALLAQRAAHEARI-RELE-- 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1033 rvDRIQTMMRNTSDKAAQ-ERLKKEINNSHIQEvvqtiKLVTEKTARYQQKLEEKQADNLRTikEKESQLQQEALAEYEE 1111
Cdd:pfam07888  136 --EDIKTLTQRVLERETElERMKERAKKAGAQR-----KEEEAERKQLQAKLQQTEEELRSL--SKEFQELRNSLAQRDT 206

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1803860226 1112 KLKSLNMEVQEMVKNYTKAgfpGQPEAQKEA 1142
Cdd:pfam07888  207 QVLQLQDTITTLTQKLTTA---HRKEAENEA 234
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 968-1122 2.06e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 42.42  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  968 RLEMDLIQLgeehhggiRRKKEQHATEQVTKIIELAReKQTAELKALKESSESN------IKDIKKKLEAKRVDRIQTMM 1041
Cdd:pfam05557    6 ESKARLSQL--------QNEKKQMELEHKRARIELEK-KASALKRQLDRESDRNqelqkrIRLLEKREAEAEEALREQAE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1042 RNTSDKAAQERLKKEIN--NSHIQEVVQTIKLVTEKTARYQQKLEEKQADNLRTIKEKES-----QLQQEALAEYEEKLK 1114
Cdd:pfam05557   77 LNRLKKKYLEALNKKLNekESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEElqerlDLLKAKASEAEQLRQ 156


                   ....*...
gi 1803860226 1115 SLNMEVQE 1122
Cdd:pfam05557  157 NLEKQQSS 164
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 895-1181 3.00e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  895 RELERK-----GHKRREELLQKYSVLFSEP--VCYRGKKRMIHARKTQKKRSLATgdvgtcANPVEMAESIdSRVLELrE 967
Cdd:pfam17380  310 REVERRrkleeAEKARQAEMDRQAAIYAEQerMAMERERELERIRQEERKRELER------IRQEEIAMEI-SRMREL-E 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  968 RLEMDLIQ-----------------LGEEHHGGIR---------RKKEQHATEQVTKIIELAREKQTAELKALKESSESN 1021
Cdd:pfam17380  382 RLQMERQQknervrqeleaarkvkiLEEERQRKIQqqkvemeqiRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQ 461

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1022 IKDIKKKlEAKRVDRIQTMMRNTSDKAAQERLKKEINNSHIQEVVQTIKLVTEKTARYQQKLEEKQadnlRTIKEKESQL 1101
Cdd:pfam17380  462 VERLRQQ-EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ----KAIYEEERRR 536

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1102 QQEalaeyEEKLKSLNME----VQEMVKNYTKAGFPGQP-EAQKEAVQSIPEGEQgSTAQLEEKIPVAEVS---RLTIAV 1173
Cdd:pfam17380  537 EAE-----EERRKQQEMEerrrIQEQMRKATEERSRLEAmEREREMMRQIVESEK-ARAEYEATTPITTIKpiyRPRISE 610


                   ....*...
gi 1803860226 1174 PEPPGAET 1181
Cdd:pfam17380  611 YQPPDVES 618
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 954-1103 3.84e-03

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


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 39.55  E-value: 3.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  954 MAESIDSRVLE----LRERLEMDLIQLgeehhggiRRKKEQHATE---QVTKIIELAREKQTAELKALKESSESNIKDIK 1026
Cdd:pfam01442   23 VAQELVDRLEKeteaLRERLQKDLEEV--------RAKLEPYLEElqaKLGQNVEELRQRLEPYTEELRKRLNADAEELQ 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1027 KKLEAKRVDRIQTMMRNTSdkAAQERLK---KEINNSHIQEVVQTIKLVTEKTARYQQKLEEKQADNLRTIKEKESQLQQ 1103
Cdd:pfam01442   95 EKLAPYGEELRERLEQNVD--ALRARLApyaEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELREKLEPQAEDLRE 172
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 1018-1126 4.50e-03

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


Pssm-ID: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 38.87  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1018 SESNIKDIKKKLEAKRVDRIQTmmrnTSDKAAQERLKKEinnsHIQEVVQTiklVTEKTARYQQKLEEKQADNLRTIKEK 1097
Cdd:pfam00836   40 KDSSLEEIQKKLEAAEERRKSL----EAQKLKQLAEKRE----KEEEALQK---ADEENNNFSKMAEEKLKQKMEAYKEN 108

                           90       100
                   ....*....|....*....|....*....
gi 1803860226 1098 EsQLQQEALaeyEEKLKSLNMEVQEMVKN 1126
Cdd:pfam00836  109 R-EAQIAAL---KEKLKEKEKHVEEVRKN 133
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 986-1123 5.25e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 5.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  986 RKKEQHATEQVTKIIELAREKQTAE-----LKALKESSESNIKDIKKKLEAK--RVDRIQTMM-RNTSDKAAQERLKKEI 1057
Cdd:TIGR04523  148 KKKEKELEKLNNKYNDLKKQKEELEnelnlLEKEKLNIQKNIDKIKNKLLKLelLLSNLKKKIqKNKSLESQISELKKQN 227

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1803860226 1058 NN--SHIQEVVQTIKLVTEKTARYQQKLE---EKQADNLRTIKEKESQLQQ--EALAEYEEKLKSLNMEVQEM 1123
Cdd:TIGR04523  228 NQlkDNIEKKQQEINEKTTEISNTQTQLNqlkDEQNKIKKQLSEKQKELEQnnKKIKELEKQLNQLKSEISDL 300
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 961-1122 5.67e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 5.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  961 RVLELRERLEmdliqlgeEHHGGIRRKKEQHATEQVTKIielarEKQTAELKALKESSESNIKDIKKKLEAKRVDRIQTM 1040
Cdd:COG1196    214 RYRELKEELK--------ELEAELLLLKLRELEAELEEL-----EAELEELEAELEELEAELAELEAELEELRLELEELE 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1041 MRNTSDKAAQERLKKEInnshiQEVVQTIKLVTEKTARYQQKLEEKQADNLRTIKEKESQLQQ-----EALAEYEEKLKS 1115
Cdd:COG1196    281 LELEEAQAEEYELLAEL-----ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEleeleEELEEAEEELEE 355


                   ....*..
gi 1803860226 1116 LNMEVQE 1122
Cdd:COG1196    356 AEAELAE 362
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 992-1096 6.70e-03

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


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 37.56  E-value: 6.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  992 ATEQVTKIIELAREKQtAELKALKESSEsNIKDIKKKLEAKRVDRIQTMMRntsdkaaQERLKKEINNShiqevvqtikl 1071
Cdd:pfam18595   31 VEKDLRSCIKLLEEIE-AELAKLEEAKK-KLKELRDALEEKEIELRELERR-------EERLQRQLENA----------- 90

                           90       100
                   ....*....|....*....|....*
gi 1803860226 1072 vTEKTARYQQKLEEKQADNLRTIKE 1096
Cdd:pfam18595   91 -QEKLERLREQAEEKREAAQARLEE 114
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 986-1144 8.03e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 8.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  986 RKKEQHATEQVTKIIELAREKQTAE-----LKALKESSESNIKDIKKKLEAK---------RVDRIQTMMRNTSDKAAQE 1051
Cdd:TIGR04523  401 QNQEKLNQQKDEQIKKLQQEKELLEkeierLKETIIKNNSEIKDLTNQDSVKeliiknldnTRESLETQLKVLSRSINKI 480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226 1052 RLKKEINNSHIQEVVQTIKLVTEKTaryqQKLEEKQAD---NLRTIKEKESQLQQEaLAEYEEKLKSLNMEVQEMVKNYT 1128
Cdd:TIGR04523  481 KQNLEQKQKELKSKEKELKKLNEEK----KELEEKVKDltkKISSLKEKIEKLESE-KKEKESKISDLEDELNKDDFELK 555

                          170
                   ....*....|....*..
gi 1803860226 1129 KAGFPGQ-PEAQKEAVQ 1144
Cdd:TIGR04523  556 KENLEKEiDEKNKEIEE 572
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 988-1123 8.11e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.26  E-value: 8.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  988 KEQHATEQVTKIIELAREKQTAELKALKESSE-------SNIKDIKKKLEAKRVDRIQTMMRNTSDKAAQERLKKEI--- 1057
Cdd:pfam07888   41 QERAELLQAQEAANRQREKEKERYKRDREQWErqrreleSRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKdal 120

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1803860226 1058 ------NNSHIQEVVQTIKLVTEKTARYQQKLEE-----KQADNLRTIKEKESQLQQEALAEYEEKLKSLNMEVQEM 1123
Cdd:pfam07888  121 laqraaHEARIRELEEDIKTLTQRVLERETELERmkeraKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 956-1104 8.55e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.11  E-value: 8.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  956 ESIDSRVLELRERLEM------DLIQLGEEHhggirRKKEQHATEQVTKIIELAREKQtaelkaLKESSESNIKDIKKKL 1029
Cdd:pfam05557  128 QSTNSELEELQERLDLlkakasEAEQLRQNL-----EKQQSSLAEAEQRIKELEFEIQ------SQEQDSEIVKNSKSEL 196

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1803860226 1030 EakrvdRIQTMMRNtsdkaaQERLKKEinNSHIQEVVQTIKLVTEKTARYQQKLE--EKQADNLRTIKEKESQLQQE 1104
Cdd:pfam05557  197 A-----RIPELEKE------LERLREH--NKHLNENIENKLLLKEEVEDLKRKLEreEKYREEAATLELEKEKLEQE 260
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1012-1130 9.71e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.95  E-value: 9.71e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803860226  1012 KALKESSEsnIKDIKKKLEAKRVDRIQTMmrntsdKAAQERLKKEINNSHIQEVVQTIKLVTEKTARYQQKLEEKQadnl 1091
Cdd:smart00935    8 KILQESPA--GKAAQKQLEKEFKKRQAEL------EKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQ---- 75

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1803860226  1092 rtikEKESQLQQEALAEYEEKLKSLNMEVQEMVKNYTKA 1130
Cdd:smart00935   76 ----RKQQKLQQDLQKRQQEELQKILDKINKAIKEVAKK 110
 
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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