NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|704462060|ref|XP_010084687|]
View 

PREDICTED: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 isoform X2 [Pterocles gutturalis]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 311-647 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: 567.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08624     1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  391 IAESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKkqsvsg 470
Cdd:cd08624    81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  471 krqnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtaYEEMSSLVNY 550
Cdd:cd08624   155 ----------------------------------------------------------------------YEEMSSLVNY 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  551 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08624   165 IQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 244

                         330
                  ....*....|....*..
gi 704462060  631 QTMDVPMQQNMALFEFN 647
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, ...
 149-299 1.39e-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: 312.20  E-value: 1.39e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  149 EKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSH 228
Cdd:cd16209     1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704462060  229 HLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16209    81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 963-1137 9.63e-76

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: 247.67  E-value: 9.63e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   963 RVLELRERLEMDLLRLGEEQHDEVRRRKEQHATEQVTKITELAREKQAAELKALKEASESNIKDIKKKLEAKRVDRIQAM 1042
Cdd:pfam08703    2 QVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1043 MRNTGDKAAQERLKKEINNSHIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREKEIQLQQEALAEHQEKLKSLTREA 1122
Cdd:pfam08703   82 KKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAEV 161

                          170
                   ....*....|....*
gi 704462060  1123 QETVKNFATAGFAGE 1137
Cdd:pfam08703  162 RESVKSCLKEGFPDE 176
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-141 5.03e-61

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: 204.53  E-value: 5.03e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060    12 EVKEYLSKGERFIKWDDETASASP-VILRVDPKGFYLYWTDQNKEMEILDITSIRDTRVGRFAKIPKCQKLREVFNLDYP 90
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 704462060    91 HSTFLLKTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVRNPLTYN 141
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 681-800 5.48e-37

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: 135.36  E-value: 5.48e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  681 TLSVTILSGQFLSD------RSVKTYVEVELFGLPRDTKRKYRTKlTSTANSINPVWkEEAFVFEkIMMPELASLKIVAW 754
Cdd:cd00275     3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAKFKTK-VVKNNGFNPVW-NETFEFD-VTVPELAFLRFVVY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 704462060  755 EEGG---KFIGHRVIPVTAVHSGYHHVCLRSESNMPLTMPSLFVYLEIK 800
Cdd:cd00275    80 DEDSgddDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
DUF1154 super family cl05918
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
 875-913 1.04e-04

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


The actual alignment was detected with superfamily member pfam06631:

Pssm-ID: 461969  Cd Length: 45  Bit Score: 40.70  E-value: 1.04e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 704462060   875 SLAELQQMKLFLKLVKKQEKELRELERKGSKRReELLQK 913
Cdd:pfam06631    8 TLESLRQDKAYLKLLKKQQKELESLKKKHSKER-SAMQK 45
 
Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 311-647 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: 567.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08624     1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  391 IAESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKkqsvsg 470
Cdd:cd08624    81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  471 krqnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtaYEEMSSLVNY 550
Cdd:cd08624   155 ----------------------------------------------------------------------YEEMSSLVNY 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  551 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08624   165 IQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 244

                         330
                  ....*....|....*..
gi 704462060  631 QTMDVPMQQNMALFEFN 647
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, ...
 149-299 1.39e-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: 312.20  E-value: 1.39e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  149 EKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSH 228
Cdd:cd16209     1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704462060  229 HLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16209    81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 314-462 1.71e-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: 251.27  E-value: 1.71e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   314 MTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAIAE 393
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 704462060   394 SAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEkyplKPGVPLPSPKDLLGKILIKN 462
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLD----DDLTELPSPEDLKGKILIKG 142
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 963-1137 9.63e-76

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: 247.67  E-value: 9.63e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   963 RVLELRERLEMDLLRLGEEQHDEVRRRKEQHATEQVTKITELAREKQAAELKALKEASESNIKDIKKKLEAKRVDRIQAM 1042
Cdd:pfam08703    2 QVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1043 MRNTGDKAAQERLKKEINNSHIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREKEIQLQQEALAEHQEKLKSLTREA 1122
Cdd:pfam08703   82 KKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAEV 161

                          170
                   ....*....|....*
gi 704462060  1123 QETVKNFATAGFAGE 1137
Cdd:pfam08703  162 RESVKSCLKEGFPDE 176
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 545-659 1.33e-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: 1.33e-66
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060    545 SSLVNYIQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQ 624
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 704462060    625 MVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFM 659
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-141 5.03e-61

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: 204.53  E-value: 5.03e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060    12 EVKEYLSKGERFIKWDDETASASP-VILRVDPKGFYLYWTDQNKEMEILDITSIRDTRVGRFAKIPKCQKLREVFNLDYP 90
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 704462060    91 HSTFLLKTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVRNPLTYN 141
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
PLN02222 PLN02222
phosphoinositide phospholipase C 2
 219-798 8.93e-61

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 219.13  E-value: 8.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  219 PEIDEIFTSHhlKAKPYMTKEHLAKFINKKQRDSRlndilfppAKPEQVQSLIEKyepSGINIQRGQLSPEGMVWFLCGP 298
Cdd:PLN02222   25 REIKTIFEKY--SENGVMTVDHLHRFLIDVQKQDK--------ATREDAQSIINS---ASSLLHRNGLHLDAFFKYLFGD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  299 ENNVIALDKLvlYQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIItHGFTM 378
Cdd:PLN02222   92 NNPPLALHEV--HHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSDKDDIDVL-HGMTL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  379 TTEILFKDAIEAIAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKyPLKPgvpLPSPKDLLGKI 458
Cdd:PLN02222  169 TTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHL-TPDLQSKVAEMVTEIFGEILFTPPVGE-SLKE---FPSPNSLKKRI 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  459 LIKNKK-KQSVSGKRQNSLKKGRNVEPEVI---EQPAPMDAEDTVWAGDGVeeepeeedehlGNLDEEEikkmqsDEGTA 534
Cdd:PLN02222  244 IISTKPpKEYKEGKDDEVVQKGKDLGDEEVwgrEVPSFIQRNKSVDKNDSN-----------GDDDDDD------DDGED 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  535 GLEVTAYEEMSSLVNyIQPIK-----FDSFEVSAQKNRSYVISSFTELKAYDlltKFPVQFVEYNKRQMSRIYPKGTRMD 609
Cdd:PLN02222  307 KSKKNAPPQYKHLIA-IHAGKpkggiTECLKVDPDKVRRLSLSEEQLEKAAE---KYAKQIVRFTQHNLLRIYPKGTRVT 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  610 SSNYMPQMFWNVGCQMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRRPDKQFDPFSvDRIDVVVASTLSVTILSG 689
Cdd:PLN02222  383 SSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKKPDLLLKSGSDSDIFD-PKATLPVKTTLRVTIYMG 461

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  690 Q----------FLSDRSVKTYVEVELFGLPRDTKRKyRTKlTSTANSInPVWKEeafVFE-KIMMPELASLKIVAWE--- 755
Cdd:PLN02222  462 EgwyfdfrhthFDQYSPPDFYTRVGIAGVPGDTVMK-KTK-TLEDNWI-PAWDE---VFEfPLTVPELALLRLEVHEydm 535

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 704462060  756 -EGGKFIGHRVIPVTAVHSGYHHVCLRSESNMPLTMPSLFVYLE 798
Cdd:PLN02222  536 sEKDDFGGQTCLPVWELSQGIRAFPLHSRKGEKYKSVKLLVKVE 579
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-144 7.11e-57

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: 192.40  E-value: 7.11e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   17 LSKGERFIKWDDETASASPVILRVDPKGFYLYWTDQNKEMEILDITSIRDTRVGRFAKIPKCQKLREVfNLDYPHSTFLL 96
Cdd:cd13361     1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 704462060   97 KTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVRNPLTYNASR 144
Cdd:cd13361    80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 681-800 5.48e-37

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: 135.36  E-value: 5.48e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  681 TLSVTILSGQFLSD------RSVKTYVEVELFGLPRDTKRKYRTKlTSTANSINPVWkEEAFVFEkIMMPELASLKIVAW 754
Cdd:cd00275     3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAKFKTK-VVKNNGFNPVW-NETFEFD-VTVPELAFLRFVVY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 704462060  755 EEGG---KFIGHRVIPVTAVHSGYHHVCLRSESNMPLTMPSLFVYLEIK 800
Cdd:cd00275    80 DEDSgddDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 681-780 9.57e-13

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


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 65.59  E-value: 9.57e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060    681 TLSVTILSGQFLSDR----SVKTYVEVELFGlprDTKRKYRTKltSTANSINPVWKEEaFVFEkIMMPELASLKIVAWEE 756
Cdd:smart00239    1 TLTVKIISARNLPPKdkggKSDPYVKVSLDG---DPKEKKKTK--VVKNTLNPVWNET-FEFE-VPPPELAELEIEVYDK 73

                            90       100
                    ....*....|....*....|....*...
gi 704462060    757 GG----KFIGHRVIPVTAVHSGYHHVCL 780
Cdd:smart00239   74 DRfgrdDFIGQVTIPLSDLLLGGRHEKL 101
C2 pfam00168
C2 domain;
681-774 2.63e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 52.71  E-value: 2.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   681 TLSVTILSGQFL----SDRSVKTYVEVELfglpRDTKRKYRTKLTStaNSINPVWKEEaFVFEkIMMPELASLKIVAWEE 756
Cdd:pfam00168    2 RLTVTVIEAKNLppkdGNGTSDPYVKVYL----LDGKQKKKTKVVK--NTLNPVWNET-FTFS-VPDPENAVLEIEVYDY 73

                           90       100
                   ....*....|....*....|..
gi 704462060   757 GG----KFIGHRVIPVTAVHSG 774
Cdd:pfam00168   74 DRfgrdDFIGEVRIPLSELDSG 95
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 954-1132 5.22e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 5.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  954 VEVAESIDSRVLELRERLEMDLLRLgEEQHDEVRRRKEQHATEqvtkiteLAREK-QAAELKALKEASESNIKDIKKKLE 1032
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEEL-EEELAELEEELEELEEE-------LEELEeELEEAEEELEEAEAELAEAEEALL 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1033 AKRVDRIQAMMRNTGDKAAQERLKKEINN--SHIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREKEIQLQ-----Q 1105
Cdd:COG1196   369 EAEAELAEAEEELEELAEELLEALRAAAElaAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEaleeaA 448

                         170       180
                  ....*....|....*....|....*..
gi 704462060 1106 EALAEHQEKLKSLTREAQETVKNFATA 1132
Cdd:COG1196   449 EEEAELEEEEEALLELLAELLEEAALL 475
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 215-302 1.05e-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: 50.71  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   215 LCPRPEIDEIFTSHHlKAKPYMTKEHLAKFINKKQRDSRlndilfppAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWF 294
Cdd:pfam09279    5 LTQREEIDEIFQEYS-GDGQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAMTKDGFLMY 75


                   ....*...
gi 704462060   295 LCGPENNV 302
Cdd:pfam09279   76 LCSPDGSI 83
PTZ00121 PTZ00121
MAEBL; Provisional
 890-1127 6.48e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 6.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  890 KKQEKELRELERKGS----KRREELLQKYSVLFSEPVCYGGKKRMMHTRKTQKKRSLTTGDVGTGANPVEVAESIDSRVL 965
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKadelKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  966 --ELRERLEMDLLRLGEEQHDEVRRRKEQHAtEQVTKITELAREKQAAELKALKEASESNiKDIKKKLEAKRVDRiqamm 1043
Cdd:PTZ00121 1613 kkAEEAKIKAEELKKAEEEKKKVEQLKKKEA-EEKKKAEELKKAEEENKIKAAEEAKKAE-EDKKKAEEAKKAEE----- 1685

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1044 rntGDKAAQERLKKEinnshiQEVVQTIKQVTEKTARCQQKLEE-KQAENLRAIREKEIQLQQEalaEHQEKLKSLTREA 1122
Cdd:PTZ00121 1686 ---DEKKAAEALKKE------AEEAKKAEELKKKEAEEKKKAEElKKAEEENKIKAEEAKKEAE---EDKKKAEEAKKDE 1753


                  ....*
gi 704462060 1123 QETVK 1127
Cdd:PTZ00121 1754 EEKKK 1758
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 968-1124 2.91e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 2.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   968 RERLEMDLLRLGEEQHDEVRRRKEQHA--TEQVTKITELAREKQA-----AELKALKEASESNIKDIKKKLEAKRVDRIQ 1040
Cdd:TIGR02168  311 LANLERQLEELEAQLEELESKLDELAEelAELEEKLEELKEELESleaelEELEAELEELESRLEELEEQLETLRSKVAQ 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1041 amMRNTGDKAA----------------QERLKKEINNSHIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREKEIqlQ 1104
Cdd:TIGR02168  391 --LELQIASLNneierlearlerledrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE--L 466

                          170       180
                   ....*....|....*....|
gi 704462060  1105 QEALAEHQEKLKSLTREAQE 1124
Cdd:TIGR02168  467 REELEEAEQALDAAERELAQ 486
DUF1154 pfam06631
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
 875-913 1.04e-04

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


Pssm-ID: 461969  Cd Length: 45  Bit Score: 40.70  E-value: 1.04e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 704462060   875 SLAELQQMKLFLKLVKKQEKELRELERKGSKRReELLQK 913
Cdd:pfam06631    8 TLESLRQDKAYLKLLKKQQKELESLKKKHSKER-SAMQK 45
growth_prot_Scy NF041483
polarized growth protein Scy;
957-1058 2.41e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  957 AESIDSRVLELRERLEMDLlrlgEEQHDEVRRRK-EQ--HATEQVTKITELAREKQA-AELKALKEASESNIKDIKKKLE 1032
Cdd:NF041483 1116 ATAIRERAEELRDRITGEI----EELHERARRESaEQmkSAGERCDALVKAAEEQLAeAEAKAKELVSDANSEASKVRIA 1191

                          90       100       110
                  ....*....|....*....|....*....|.
gi 704462060 1033 AkrVDRIQAMMRNTGDKAAQ-----ERLKKE 1058
Cdd:NF041483 1192 A--VKKAEGLLKEAEQKKAElvreaEKIKAE 1220
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 981-1128 6.24e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 39.35  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  981 EQHDEVRRRKEQHAtEQVTKITELAREkqaaelkaLKEASESNIKDIKKKLEA--KRVDRIQAMMrntgdKAAQERLKKE 1058
Cdd:cd00176    40 KKHEALEAELAAHE-ERVEALNELGEQ--------LIEEGHPDAEEIQERLEElnQRWEELRELA-----EERRQRLEEA 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704462060 1059 IN-NSHIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREKEIQLQQEaLAEHQEKLKSLTREAQETVKN 1128
Cdd:cd00176   106 LDlQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEE-LEAHEPRLKSLNELAEELLEE 175
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1014-1132 9.55e-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: 9.55e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   1014 KALKEASEsnIKDIKKKLEAKRVDRIQAMmrntgdKAAQERLKKEINNSHIQEVVQTIKQVTEKtarcQQKLEEKQaenl 1093
Cdd:smart00935    8 KILQESPA--GKAAQKQLEKEFKKRQAEL------EKLEKELQKLKEKLQKDAATLSEAAREKK----EKELQKKV---- 71

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 704462060   1094 RAIREKEIQLQQEALAEHQEKLKSLTREAQETVKNFATA 1132
Cdd:smart00935   72 QEFQRKQQKLQQDLQKRQQEELQKILDKINKAIKEVAKK 110
 
Name Accession Description Interval E-value
PI-PLCc_beta2 cd08624
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta2; This subfamily ...
 311-647 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: 567.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08624     1 HQDMTQPLNHYFINSSHNTYLTAGQFSGLSSPEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTEILFKDAIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  391 IAESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKkqsvsg 470
Cdd:cd08624    81 IAESAFKTSPYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPEDLRGKILIKNKK------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  471 krqnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtaYEEMSSLVNY 550
Cdd:cd08624   155 ----------------------------------------------------------------------YEEMSSLVNY 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  551 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08624   165 IQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 244

                         330
                  ....*....|....*..
gi 704462060  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08624   245 QTMDLPMQQNMALFEFN 261
PI-PLCc_beta cd08591
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta; This subfamily ...
 311-647 0e+00

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


Pssm-ID: 176533 [Multi-domain]  Cd Length: 257  Bit Score: 553.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08591     1 YQDMDQPLSHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLSGCRCIELDCWDGKGEDEEPIITHGKTMCTEILFKDVIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  391 IAESAFKTSLYPVILSFENHVDSpKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKkqsvsg 470
Cdd:cd08591    81 IAETAFKTSEYPVILSFENHCSS-KQQAKMAEYCREIFGDLLLTEPLEKYPLEPGVPLPSPNDLKRKILIKNKK------ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  471 krqnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNY 550
Cdd:cd08591   154 -------------------------------------------------------------------------LSSLVNY 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  551 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08591   161 IQPVKFQGFEVAEKRNKHYEMSSFNESKGLGYLKKSPIEFVNYNKRQLSRIYPKGTRVDSSNYMPQIFWNAGCQMVALNF 240

                         330
                  ....*....|....*..
gi 704462060  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08591   241 QTPDLPMQLNQGKFEYN 257
PI-PLCc_beta3 cd08625
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta3; This subfamily ...
 313-647 4.74e-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: 458.36  E-value: 4.74e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  313 DMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEAIA 392
Cdd:cd08625     3 DMNQPLSHYFINSSHNTYLTAGQLTGLSSVEMYRQVLLTGCRCIELDCWKGRPPEEEPFITHGFTMTTEIPFKDVIEAIA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  393 ESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKkqsvsgkr 472
Cdd:cd08625    83 ESAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLVPGVQLPSPQELMGKILVKNKK-------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  473 qnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNYIQ 552
Cdd:cd08625   155 -----------------------------------------------------------------------MSTLVNYIE 163

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  553 PIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQT 632
Cdd:cd08625   164 PVKFKSFEAAAKRNKFFEMSSFVETKAMEQLTKSPMEFVEYNKKQLSRIYPKGTRVDSSNYMPQLFWNVGCQMVALNFQT 243

                         330
                  ....*....|....*
gi 704462060  633 MDVPMQQNMALFEFN 647
Cdd:cd08625   244 LDLAMQLNMGVFEYN 258
PI-PLCc_eukaryota cd08558
Catalytic domain of eukaryotic phosphoinositide-specific phospholipase C and similar proteins; ...
 311-647 1.94e-136

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: 413.39  E-value: 1.94e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08558     1 YQDMTQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGHTLTSKILFKDVIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPlkpgVPLPSPKDLLGKILIKNKKkqsvsg 470
Cdd:cd08558    79 IKEYAFVTSPYPVILSLENHC-SLEQQKKMAQILKEIFGDKLLTPPLDENP----VQLPSPEQLKGKILIKGKK------ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  471 krqnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtayeemsslvny 550
Cdd:cd08558       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  551 iqpikfdsfevsaqknrsYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08558   148 ------------------YHMSSFSETKALKLLKESPEEFVKYNKRQLSRVYPKGTRVDSSNYNPQPFWNAGCQMVALNY 209

                         330
                  ....*....|....*..
gi 704462060  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08558   210 QTPDLPMQLNQGKFEQN 226
PI-PLCc_beta1 cd08623
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta1; This subfamily ...
 312-647 1.11e-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: 410.24  E-value: 1.11e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  312 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEAI 391
Cdd:cd08623     2 EDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  392 AESAFKTSLYPVILSFENHVDSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKkqsvsgk 471
Cdd:cd08623    82 AECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKK------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  472 rqnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNYI 551
Cdd:cd08623   155 ------------------------------------------------------------------------MSNLVNYI 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  552 QPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQ 631
Cdd:cd08623   163 QPVKFESFEASKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQ 242

                         330
                  ....*....|....*.
gi 704462060  632 TMDVPMQQNMALFEFN 647
Cdd:cd08623   243 TVDLSMQINMGMYEYN 258
PI-PLCc_beta4 cd08626
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-beta4; This subfamily ...
 311-647 2.36e-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: 401.06  E-value: 2.36e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08626     1 YQDMDQPLAHYFINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCIELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKkqsvsg 470
Cdd:cd08626    81 IKDTAFVTSDYPVILSFENHC-SKPQQYKLAKYCEEIFGDLLLTKPLESHPLEPGVPLPSPNKLKRKILIKNKR------ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  471 krqnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNY 550
Cdd:cd08626   154 -------------------------------------------------------------------------LSSLVNY 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  551 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08626   161 AQPVKFQGFDVAEERNIHFNMSSFNESVGLGYLKTSAIEFVNYNKRQMSRIYPKGTRVDSSNYMPQIFWNAGCQMVSLNF 240

                         330
                  ....*....|....*..
gi 704462060  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08626   241 QTPDLGMQLNQGKFEYN 257
PI-PLCc_delta cd08593
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta; This subfamily ...
 311-647 3.79e-113

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: 352.80  E-value: 3.79e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08593     1 YQDMTQPLSHYFIASSHNTYLLEDQLKGPSSTEAYIRALKKGCRCVELDCWDG--PDGEPIIYHGHTLTSKILFKDVIQA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEkyplKPGVPLPSPKDLLGKILIKNKKkqsvsg 470
Cdd:cd08593    79 IREYAFKVSPYPVILSLENHC-SVEQQKVMAQHLKSILGDKLLTQPLD----GVLTALPSPEELKGKILVKGKK------ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  471 krqnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedEHLGnldeeeikkmqsdegtaglevtayEEMSSLVNY 550
Cdd:cd08593   148 -------------------------------------------LKLA------------------------KELSDLVIY 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  551 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08593   161 CKSVHFKSFEHSKENYHFYEMSSFSESKALKLAQESGNEFVRHNKRQLSRIYPAGLRTDSSNYDPQEMWNVGCQIVALNF 240

                         330
                  ....*....|....*..
gi 704462060  631 QTMDVPMQQNMALFEFN 647
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, ...
 149-299 1.39e-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: 312.20  E-value: 1.39e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  149 EKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSH 228
Cdd:cd16209     1 EKIYVKLKMQLNSEGKIPVKNFFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEAVFKTFLMQLCPRPEIDEIFTSY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704462060  229 HLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16209    81 HAKAKPYMTKEHLTKFINKKQRDSRLNEELFPPARPDQVQGLIEKYEPSGINAQRGQLSPEGMVWFLCGPE 151
PI-PLCc_PRIP_metazoa cd08597
Catalytic domain of metazoan phospholipase C related, but catalytically inactive protein; This ...
 312-647 2.52e-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: 302.42  E-value: 2.52e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  312 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAI 391
Cdd:cd08597     2 QDMTQPLSHYFIASSHNTYLIEDQLRGPSSVEGYVRALQRGCRCVELDCWDG--PNGEPVIYHGHTLTSKISFRSVIEAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  392 AESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPlekyPLKPGVPLPSPKDLLGKILIKNKKkqsvsgk 471
Cdd:cd08597    80 NEYAFVASEYPLILCIENHC-SEKQQLVMAQYLKEIFGDKLYTEP----PNEGESYLPSPHDLKGKIIIKGKK------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  472 rqnsLKKgrnvePEVIeqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtayEEMSSLVNYI 551
Cdd:cd08597   148 ----LKR-----RKLC------------------------------------------------------KELSDLVSLC 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  552 QPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQ 631
Cdd:cd08597   165 KSVRFQDFPTSAQNQKYWEVCSFSENLARRLANEFPEDFVNYNKKFLSRVYPSPMRVDSSNYNPQDFWNCGCQIVAMNYQ 244

                         330
                  ....*....|....*.
gi 704462060  632 TMDVPMQQNMALFEFN 647
Cdd:cd08597   245 TPGLMMDLNTGKFLEN 260
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 311-647 5.22e-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: 299.56  E-value: 5.22e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFS-----GISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTtEILFK 385
Cdd:cd00137     1 HHPDTQPLAHYSIPGTHDTYLTAGQFTikqvwGLTQTEMYRQQLLSGCRCVDIRCWDG--KPEEPIIYHGPTFL-DIFLK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  386 DAIEAIAESAFKTSLYPVILSFENHVDS-PKQQAKMAEYCRTIFGDMLLTeplekYPLKPGVPLPSPKDLLGKILIKNKK 464
Cdd:cd00137    78 EVIEAIAQFLKKNPPETIIMSLKNEVDSmDSFQAKMAEYCRTIFGDMLLT-----PPLKPTVPLPSLEDLRGKILLLNKK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  465 KQsvsgkrqnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaGLEVTAYEEM 544
Cdd:cd00137   153 NG--------------------------------------------------------------------FSGPTGSSND 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  545 SslvnyiqpiKFDSFEVSAQKNRSYVISSFTELKAYD----LLTKFPVQFVEYNKRQMSRIYPKGTR---------MDSS 611
Cdd:cd00137   165 T---------GFVSFEFSTQKNRSYNISSQDEYKAYDdekvKLIKATVQFVDYNKNQLSRNYPSGTSggtawyyyaMDSN 235

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 704462060  612 NYMPQMFWN---VGCQMVALNFQTMDVPMQQNMALFEFN 647
Cdd:cd00137   236 NYMPQMFWNanpAGCGIVILDFQTMDLPMQQYMAVIEFN 274
PI-PLCc_gamma cd08592
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma; This family ...
 312-647 1.15e-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: 291.25  E-value: 1.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  312 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAI 391
Cdd:cd08592     2 QDMNNPLSHYWIASSHNTYLTGDQLSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPIIYHGHTLTSKIKFMDVLKTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  392 AESAFKTSLYPVILSFENHVDSPkQQAKMAEYCRTIFGDMLLTEPLEkyplKPGVPLPSPKDLLGKILIKNKKkqsvsgk 471
Cdd:cd08592    80 KEHAFVTSEYPVILSIENHCSLP-QQRNMAQAFKEVFGDMLLTQPVD----RNADQLPSPNQLKRKIIIKHKK------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  472 rqnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtAYEEMsslvnyi 551
Cdd:cd08592   148 --------------------------------------------------------------------LFYEM------- 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  552 qpikfdsfevsaqknrsyviSSFTELKAYDLLTKF-PVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08592   153 --------------------SSFPETKAEKYLNRQkGKIFLKYNRRQLSRVYPKGQRVDSSNYDPVPMWNCGSQMVALNF 212

                         330
                  ....*....|....*..
gi 704462060  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08592   213 QTPDKPMQLNQALFMLN 229
PI-PLCc_delta3 cd08630
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta3; This subfamily ...
 311-647 3.46e-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: 277.29  E-value: 3.46e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08630     1 FQDMSQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEG--PGGEPVIYHGHTLTSKILFRDVIQA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvPLPSPKDLLGKILIKNKKKQsvsg 470
Cdd:cd08630    79 VRQHAFTASPYPVILSLENHC-GLEQQAAMARHLQTILGDMLVTQPLDSLNPE---ELPSPEELKGRVLVKGKKLQ---- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  471 krqnslkkgrnVEPevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtayeEMSSLVNY 550
Cdd:cd08630   151 -----------ISP----------------------------------------------------------ELSALAVY 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  551 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08630   162 CQATRLRTLEPAPVQPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQEMWNSGCQLVALNF 241

                         330
                  ....*....|....*..
gi 704462060  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08630   242 QTPGYEMDLNAGRFLVN 258
PI-PLC1c_yeast cd08598
Catalytic domain of putative yeast phosphatidylinositide-specific phospholipases C; This ...
 311-644 7.15e-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: 272.58  E-value: 7.15e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08598     1 EEDLSRPLNEYFISSSHNTYLLGRQLAGDSSVEGYIRALQRGCRCVEIDVWDG--DDGEPVVTHGYTLTSSVPFRDVCRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  391 IAESAFKTSLYPVILSFENHVDsPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvpLPSPKDLLGKILIKNKKkqsvsg 470
Cdd:cd08598    79 IKKYAFVTSPYPLILSLEVHCD-AEQQERMVEIMKETFGDLLVTEPLDGLEDE----LPSPEELRGKILIKVKK------ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  471 krqnslkkgrnvepeviEQPAPmdaedtvwagdgveeepeeedEHLGNLDEEEIKKMQSDegtaglevtayeemsslvny 550
Cdd:cd08598   148 -----------------ESKTP---------------------NHIFSLSERSLLKLLKD-------------------- 169

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  551 iqpikfdsfevsaqknrsyvissftelKAYDLltkfpvqfVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08598   170 ---------------------------KRAAL--------DKHNRRHLMRVYPSGTRISSSNFNPLPFWRAGVQMVALNW 214

                         330
                  ....*....|....
gi 704462060  631 QTMDVPMQQNMALF 644
Cdd:cd08598   215 QTYDLGMQLNEAMF 228
PI-PLCc_delta1 cd08629
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1; This subfamily ...
 311-647 2.82e-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: 2.82e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08629     1 YQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDG--PNQEPIIYHGYTFTSKILFCDVLRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvpLPSPKDLLGKILIKNKKkqsvsg 470
Cdd:cd08629    79 IRDYAFKASPYPVILSLENHC-SLEQQRVMARHLRAILGPILLDQPLDGVTTS----LPSPEQLKGKILLKGKK------ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  471 krqnsLKKGRnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtayeEMSSLVNY 550
Cdd:cd08629   148 -----LKLVP--------------------------------------------------------------ELSDMIIY 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  551 IQPIKFDSFEVSAQKNRS-YVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALN 629
Cdd:cd08629   161 CKSVHFGGFSSPGTSGQAfYEMASFSESRALRLLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALN 240

                         330
                  ....*....|....*...
gi 704462060  630 FQTMDVPMQQNMALFEFN 647
Cdd:cd08629   241 FQTPGPEMDVYLGCFQDN 258
PI-PLCc_zeta cd08595
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-zeta; This family ...
 311-647 5.13e-82

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: 268.73  E-value: 5.13e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08595     1 YQDMDHPLSDYFISSSHNTYLVSDQLVGPSDLDGYVSALRKGCRCLEIDCWDG--ADNEPVVYHGYTLTSKILFKEVITT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvPLPSPKDLLGKILIKNKKKqsvsg 470
Cdd:cd08595    79 VEKYAFEKSDYPVVLSLENHC-STEQQEIMAHYLVSILGEKLLRAPIDDPATG---ELPSPEALKFKILVKNKKK----- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  471 krqnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeIKKMQSDegtaglevtayeemssLVNY 550
Cdd:cd08595   150 -----------------------------------------------------IAKALSD----------------LVIY 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  551 IQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08595   161 TKSEKFCSFTHSRDNQHSYENNSIGENKARKLLKSSGADFVGHTQRFITRIYPKGTRASSSNYNPQEFWNVGCQMVALNF 240

                         330
                  ....*....|....*..
gi 704462060  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08595   241 QTLGAPMDLQNGKFLDN 257
PI-PLCc_delta4 cd08631
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta4; This subfamily ...
 311-647 3.22e-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: 3.22e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08631     1 YQDMTQPLCHYFICSSHNTYLMEDQLRGQSSVEGYIRALKRGCRCVEVDVWDG--PNGEPIVYHGHTFTSKILFKDVVAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLE-KYPlkpgVPLPSPKDLLGKILIKNKKkqsvs 469
Cdd:cd08631    79 VAQYAFQVSDYPVILSLENHC-GVEQQQTMAQHLTEILGEKLLSTTLDgVLP----TQLPSPEELRGKILLKGKK----- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  470 gkrqnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtagleVTAYEEMSSLVN 549
Cdd:cd08631   149 --------------------------------------------------------------------IRLSPELSDCVI 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  550 YIQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALN 629
Cdd:cd08631   161 YCKSVSFRSFTHSREHYHFYEISSFTETKARKLIREAGNEFVQHNTWQLSRVYPSGLRTDSSNYNPQEMWNAGCQMVALN 240

                         330
                  ....*....|....*...
gi 704462060  630 FQTMDVPMQQNMALFEFN 647
Cdd:cd08631   241 FQTAGLEMDLNDGLFRQN 258
PI-PLCc_epsilon cd08596
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-epsilon; This family ...
 312-647 6.17e-80

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


Pssm-ID: 176538 [Multi-domain]  Cd Length: 254  Bit Score: 262.48  E-value: 6.17e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  312 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRppDEEPIITHGFTMTTEILFKDAIEAI 391
Cdd:cd08596     2 EDLQYPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLTGCRCVELDCWDGD--DGMPIIYHGHTLTTKIPFKDVVEAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  392 AESAFKTSLYPVILSFENHVDSPkQQAKMAEYCRTIFGDMLLTEPLEKYPLKPGVPLPSPKDLLGKILIKNKKkqsvsgk 471
Cdd:cd08596    80 NRSAFITSDYPVILSIENHCSLQ-QQRKMAEIFKTVFGEKLVTKFLFESDFSDDPSLPSPLQLKNKILLKNKK------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  472 rqnslkkgrnvepevieqpAPmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtayeEMSSLVNYI 551
Cdd:cd08596   152 -------------------AP--------------------------------------------------ELSDLVIYC 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  552 QPIKFDSFEVSaqknRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQ 631
Cdd:cd08596   163 QAVKFPGLSTP----KCYHISSLNENAAKRLCRRYPQKLVQHTRCQLLRTYPAATRIDSSNPNPLIFWLHGLQLVALNYQ 238

                         330
                  ....*....|....*.
gi 704462060  632 TMDVPMQQNMALFEFN 647
Cdd:cd08596   239 TDDLPMHLNAAMFEAN 254
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 314-462 1.71e-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: 251.27  E-value: 1.71e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   314 MTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAIAE 393
Cdd:pfam00388    1 MSQPLSHYFISSSHNTYLTGDQLTGESSVEAYIRALLRGCRCVELDCWDG--PDGEPVVYHGYTLTSKIPFRDVLEAIKD 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 704462060   394 SAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEkyplKPGVPLPSPKDLLGKILIKN 462
Cdd:pfam00388   79 YAFVTSPYPVILSLENHC-SPEQQKKMAEILKEIFGDMLYTPPLD----DDLTELPSPEDLKGKILIKG 142
PI-PLCc_eta cd08594
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta; This family ...
 311-647 1.76e-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: 254.73  E-value: 1.76e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08594     1 NQDMTQPLSHYFIASSHNTYLTGDQLLSQSRVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKILFRDVIET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLtepLEKYPLKPGVPLPSPKDLLGKILIKNKKKQsvsg 470
Cdd:cd08594    79 INKYAFIKNEYPVILSIENHC-SVQQQKKMAQYLKEILGDKLD---LSSVISGDSKQLPSPQSLKGKILIKGKKWQ---- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  471 krqnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtayeemsslvny 550
Cdd:cd08594       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  551 iqpikfdsfevsaqknrsyvISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08594   151 --------------------VSSFSETRAHQIVQQKAAQFLRFNQRQLSRIYPSAYRIDSSNFNPQPYWNAGCQLVALNY 210

                         330
                  ....*....|....*..
gi 704462060  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08594   211 QTEGRMLQLNRAKFRAN 227
PI-PLCc_gamma2 cd08628
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma2; This subfamily ...
 312-647 3.10e-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: 254.98  E-value: 3.10e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  312 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAI 391
Cdd:cd08628     2 QDMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRMGCRCIELDCWDG--PDGKPIIYHGWTRTTKIKFDDVVQAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  392 AESAFKTSLYPVILSFENHVDSpKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvpLPSPKDLLGKILIKNKKKQSVsgk 471
Cdd:cd08628    80 KDHAFVTSEYPVILSIEEHCSV-EQQRHMAKVFKEVFGDKLLMKPLEASADQ----LPSPTQLKEKIIIKHKKLIAI--- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  472 rqnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtayeEMSSLVNYI 551
Cdd:cd08628   152 -----------------------------------------------------------------------ELSDLVVYC 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  552 QPI--KFDSFEVSAQKNrsyvISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALN 629
Cdd:cd08628   161 KPTskTKDNLENPDFKE----IRSFVETKAPSIIRQKPVQLLKYNRKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALN 236

                         330
                  ....*....|....*...
gi 704462060  630 FQTMDVPMQQNMALFEFN 647
Cdd:cd08628   237 FQTADKYMQLNHALFSLN 254
PI-PLCc_eta2 cd08633
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta2; This subfamily ...
 312-647 3.13e-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: 3.13e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  312 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAI 391
Cdd:cd08633     2 QDMTQPLSHYFITSSHNTYLSGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDG--PDGEPIVHHGYTLTSKILFKDVIETI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  392 AESAFKTSLYPVILSFENHVDSPkQQAKMAEYCRTIFGDMLltePLEKYPLKPGVPLPSPKDLLGKILIKNKKkqsvsgk 471
Cdd:cd08633    80 NKYAFIKNEYPVILSIENHCSVP-QQKKMAQYLTEILGDKL---DLSSVISNDCTRLPSPEILKGKILVKGKK------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  472 rqnsLKKGrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtayeeMSSLVNYI 551
Cdd:cd08633   149 ----LSRA----------------------------------------------------------------LSDLVKYT 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  552 QPIKFDSFEVSAQKnrSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNFQ 631
Cdd:cd08633   161 KSVRVHDIETEATS--SWQVSSFSETKAHQILQQKPAQYLRFNQRQLSRIYPSSYRVDSSNYNPQPFWNAGCQMVALNYQ 238

                         330
                  ....*....|....*.
gi 704462060  632 TMDVPMQQNMALFEFN 647
Cdd:cd08633   239 SEGRMLQLNRAKFSAN 254
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
 963-1137 9.63e-76

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: 247.67  E-value: 9.63e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   963 RVLELRERLEMDLLRLGEEQHDEVRRRKEQHATEQVTKITELAREKQAAELKALKEASESNIKDIKKKLEAKRVDRIQAM 1042
Cdd:pfam08703    2 QVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1043 MRNTGDKAAQERLKKEINNSHIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREKEIQLQQEALAEHQEKLKSLTREA 1122
Cdd:pfam08703   82 KKRTSDKAAQERLKKEINNSHIQEVVQSIKQLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAEV 161

                          170
                   ....*....|....*
gi 704462060  1123 QETVKNFATAGFAGE 1137
Cdd:pfam08703  162 RESVKSCLKEGFPDE 176
PI-PLCc_eta1 cd08632
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-eta1; This subfamily ...
 311-647 2.93e-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: 232.61  E-value: 2.93e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEA 390
Cdd:cd08632     1 NQDMDQPLCNYFIASSHNTYLTGDQLLSQSKVDMYARVLQAGCRCVEVDCWDG--PDGEPVVHHGYTLTSKITFRDVIET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDML-LTEPLEKYPLKpgvpLPSPKDLLGKILIKNKkkqsvs 469
Cdd:cd08632    79 INKYAFVKNEFPVILSIENHC-SIQQQKKIAQYLKEIFGDKLdLSSVLTGDPKQ----LPSPQLLKGKILVKGK------ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  470 gkrqnslKKGRNVEPEVIeqpapmdAEDTVWAGDGVeeepeeedehlgnldeeeikkmqsDEGTAGlevtayeemsslvn 549
Cdd:cd08632   148 -------KLCRDLSDLVV-------YTNSVAAQDIV------------------------DDGSTG-------------- 175

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  550 yiqpikfdsfevsaqknrsyVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALN 629
Cdd:cd08632   176 --------------------NVLSFSETRAHQLVQQKAEQFMTYNQKQLTRIYPSAYRIDSSNFNPLPYWNVGCQLVALN 235

                         330
                  ....*....|....*...
gi 704462060  630 FQTMDVPMQQNMALFEFN 647
Cdd:cd08632   236 YQSEGRMMQLNRAKFMVN 253
PI-PLCc_gamma1 cd08627
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-gamma1; This subfamily ...
 312-647 3.97e-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: 3.97e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  312 QDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAI 391
Cdd:cd08627     2 EEMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDG--PDGMPVIYHGHTLTTKIKFSDVLHTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  392 AESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEkyplKPGVPLPSPKDLLGKILIKNKKkqsvsgk 471
Cdd:cd08627    80 KEHAFVTSEYPIILSIEDHC-SIVQQRNMAQHFKKVFGDMLLTKPVD----INADGLPSPNQLKRKILIKHKK------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  472 rqnslkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtAYEEMsslvnyi 551
Cdd:cd08627   148 --------------------------------------------------------------------LYRDM------- 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  552 qpikfdsfevsaqknrsyviSSFTELKAYDLLTKFP-VQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08627   153 --------------------SSFPETKAEKYVNRSKgKKFLQYNRRQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNF 212

                         330
                  ....*....|....*..
gi 704462060  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08627   213 QTPDKPMQMNQALFMLG 229
PLCYc smart00149
Phospholipase C, catalytic domain (part); domain Y; Phosphoinositide-specific phospholipases C. ...
 545-659 1.33e-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: 1.33e-66
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060    545 SSLVNYIQPIKFDSFEVSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQ 624
Cdd:smart00149    1 SDLVIYCAPVKFRSFESAESKNPFYEMSSFSETKAKKLLKKSPTDFVRYNQRQLSRVYPKGTRVDSSNYNPQVFWNHGCQ 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 704462060    625 MVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFM 659
Cdd:smart00149   81 MVALNFQTPDKPMQLNQGMFRANGGCGYVLKPDFL 115
EFh_PI-PLCbeta cd16200
EF-hand motif found in metazoan phosphoinositide-specific phospholipase C (PI-PLC)-beta ...
 149-299 7.20e-64

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


Pssm-ID: 320030 [Multi-domain]  Cd Length: 153  Bit Score: 213.26  E-value: 7.20e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  149 EKILVKLKMQLNAEGKIPVRNIFQMFPAD--RKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFT 226
Cdd:cd16200     1 KKLYTKLKLSVNITGKIPVKNIIKCFSSDkkRKRVLKALKALGLPDGKNDEIDPEDFTFEKFFKLYNKLCPRPDIDEIFK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 704462060  227 SHHLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16200    81 ELGGKRKPYLTLEQLVDFLNEEQRDPRLNEILFPFHTKEQAKKLIDKYEPNEKNKKKGQLTLEGFLRYLMSDE 153
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 314-463 3.09e-62

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


Pssm-ID: 197543 [Multi-domain]  Cd Length: 143  Bit Score: 208.29  E-value: 3.09e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060    314 MTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMTTEILFKDAIEAIAE 393
Cdd:smart00148    1 MDKPLSHYFIPSSHNTYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDG--PDGEPVIYHGHTFTLPIKLSEVLEAIKD 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060    394 SAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLKpgvpLPSPKDLLGKILIKNK 463
Cdd:smart00148   79 FAFVTSPYPVILSLENHC-SPDQQAKMAQMFKEIFGDMLYTPPLTSSLEV----LPSPEQLRGKILLKVR 143
PH_14 pfam17787
PH domain; This entry corresponds to the PH domain found at the N-terminus of phospholipase C ...
 12-141 5.03e-61

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: 204.53  E-value: 5.03e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060    12 EVKEYLSKGERFIKWDDETASASP-VILRVDPKGFYLYWTDQNKEMEILDITSIRDTRVGRFAKIPKCQKLREVFNLDYP 90
Cdd:pfam17787    1 EVPEKLQKGELFIKWDEESTVAEPnVLLKVDPKGFFLYWKSQGKEGEVLEITSIRDTRLGKFAKIPKDPKLREVLSMGGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 704462060    91 HSTFLLKTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVRNPLTYN 141
Cdd:pfam17787   81 DNSLEDKTLTVVSGTDMVNINFHNFVASNSEVAKNWAEGLRALAHNVLAAN 131
PLN02222 PLN02222
phosphoinositide phospholipase C 2
 219-798 8.93e-61

phosphoinositide phospholipase C 2


Pssm-ID: 177868 [Multi-domain]  Cd Length: 581  Bit Score: 219.13  E-value: 8.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  219 PEIDEIFTSHhlKAKPYMTKEHLAKFINKKQRDSRlndilfppAKPEQVQSLIEKyepSGINIQRGQLSPEGMVWFLCGP 298
Cdd:PLN02222   25 REIKTIFEKY--SENGVMTVDHLHRFLIDVQKQDK--------ATREDAQSIINS---ASSLLHRNGLHLDAFFKYLFGD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  299 ENNVIALDKLvlYQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDEEPIItHGFTM 378
Cdd:PLN02222   92 NNPPLALHEV--HHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSDKDDIDVL-HGMTL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  379 TTEILFKDAIEAIAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKyPLKPgvpLPSPKDLLGKI 458
Cdd:PLN02222  169 TTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHL-TPDLQSKVAEMVTEIFGEILFTPPVGE-SLKE---FPSPNSLKKRI 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  459 LIKNKK-KQSVSGKRQNSLKKGRNVEPEVI---EQPAPMDAEDTVWAGDGVeeepeeedehlGNLDEEEikkmqsDEGTA 534
Cdd:PLN02222  244 IISTKPpKEYKEGKDDEVVQKGKDLGDEEVwgrEVPSFIQRNKSVDKNDSN-----------GDDDDDD------DDGED 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  535 GLEVTAYEEMSSLVNyIQPIK-----FDSFEVSAQKNRSYVISSFTELKAYDlltKFPVQFVEYNKRQMSRIYPKGTRMD 609
Cdd:PLN02222  307 KSKKNAPPQYKHLIA-IHAGKpkggiTECLKVDPDKVRRLSLSEEQLEKAAE---KYAKQIVRFTQHNLLRIYPKGTRVT 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  610 SSNYMPQMFWNVGCQMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRRPDKQFDPFSvDRIDVVVASTLSVTILSG 689
Cdd:PLN02222  383 SSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKKPDLLLKSGSDSDIFD-PKATLPVKTTLRVTIYMG 461

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  690 Q----------FLSDRSVKTYVEVELFGLPRDTKRKyRTKlTSTANSInPVWKEeafVFE-KIMMPELASLKIVAWE--- 755
Cdd:PLN02222  462 EgwyfdfrhthFDQYSPPDFYTRVGIAGVPGDTVMK-KTK-TLEDNWI-PAWDE---VFEfPLTVPELALLRLEVHEydm 535

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 704462060  756 -EGGKFIGHRVIPVTAVHSGYHHVCLRSESNMPLTMPSLFVYLE 798
Cdd:PLN02222  536 sEKDDFGGQTCLPVWELSQGIRAFPLHSRKGEKYKSVKLLVKVE 579
EFh_PI-PLCbeta1 cd16208
EF-hand motif found in phosphoinositide phospholipase C beta 1 (PI-PLC-beta1); PI-PLC-beta1, ...
 149-299 1.89e-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: 1.89e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  149 EKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSH 228
Cdd:cd16208     1 EKAYTKLKLQVNPEGRIPVKNIYRLFSADRKRVETALEACNLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDHIFSEF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704462060  229 HLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16208    81 GAKSKPYLSVDQMTEFINSKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSTLAKKGQISVDGFMRYLSGEE 151
PLN02952 PLN02952
phosphoinositide phospholipase C
 310-795 9.79e-59

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 213.71  E-value: 9.79e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  310 LYQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDeEPIITHGFTMTTEILFKDAIE 389
Cdd:PLN02952  121 VHHDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPIVKALQRGVRVIELDLWPGSTKD-EILVLHGRTLTTPVPLIKCLK 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  390 AIAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLteplekYPLKPG-VPLPSPKDLLGKILIKNK-KKQS 467
Cdd:PLN02952  200 SIRDYAFSSSPYPVIITLEDHL-TPDLQAKVAEMATQIFGQMLY------YPESDSlVQFPSPESLKHRIIISTKpPKEY 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  468 VSGKRQNSLKKGRNVEPEViEQPAPMDAEdtvwagdgveeePEEEDEHLGNLD-EEEIKKMQSDEGTAGLEVTAYEEMSS 546
Cdd:PLN02952  273 LESSGPIVIKKKNNVSPSG-RNSSEETEE------------AQTLESMLFEQEaDSRSDSDQDDNKSGELQKPAYKRLIT 339

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  547 lVNYIQP---IKfDSFEVSAQKNRSYvisSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGC 623
Cdd:PLN02952  340 -IHAGKPkgtLK-DAMKVAVDKVRRL---SLSEQELEKAATTNGQDVVRFTQRNILRIYPKGTRITSSNYKPLIGWMHGA 414

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  624 QMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFM--RRPDKQ-FDPfsvdRIDVVVASTLSVTILSG----------Q 690
Cdd:PLN02952  415 QMIAFNMQGYGKSLWLMHGMFRANGGCGYLKKPDFLmkKGFHDEvFDP----KKKLPVKKTLKVKVYLGdgwrldfshtH 490

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  691 FLSDRSVKTYVEVELFGLPRDTKRKyRTKLTStaNSINPVWKEEaFVFeKIMMPELASLKIVAWE----EGGKFIGHRVI 766
Cdd:PLN02952  491 FDSYSPPDFYTKMYIVGVPADNAKK-KTKIIE--DNWYPAWNEE-FSF-PLTVPELALLRIEVREydmsEKDDFGGQTCL 565

                         490       500       510
                  ....*....|....*....|....*....|....
gi 704462060  767 PVTAVHSGYHHVCLRSE-----SNMPLTMPSLFV 795
Cdd:PLN02952  566 PVSELRPGIRSVPLHDKkgeklKNVRLLMRFIFV 599
PI-PLC-Y pfam00387
Phosphatidylinositol-specific phospholipase C, Y domain; This associates with pfam00388 to ...
 544-658 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 704462060   544 MSSLVNYIQPIKFDSFEvSAQKNRSYVISSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGC 623
Cdd:pfam00387    1 LSDLVVYTQSVKFKSFS-TPESKTPNHIFSFSESKALKLIKSSSAAFVKHNRRHLMRVYPKGTRVDSSNFNPQPFWNCGV 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 704462060   624 QMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEF 658
Cdd:pfam00387   80 QMVALNWQTPDEGMQLNEGMFADNGGCGYVLKPEF 114
PI-PLCc_plant cd08599
Catalytic domain of plant phosphatidylinositide-specific phospholipases C; This family ...
 311-647 2.59e-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: 200.68  E-value: 2.59e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  311 YQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGRPPDeePIITHGFTMTTEILFKDAIEA 390
Cdd:cd08599     1 HHDMTAPLSHYFIFSSHNSYLTGNQLSSRSSTAPIIEALLRGCRVIELDLWPGGRGD--ICVLHGGTLTKPVKFEDCIKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  391 IAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPlekyPLKPGVPLPSPKDLLGKILIKNKkkqsvsg 470
Cdd:cd08599    79 IKENAFTASEYPVIITLENHL-SPELQAKAAQILRETLGDKLFYPD----SEDLPEEFPSPEELKGKILISDK------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  471 krqnslkkgrnvePEVIEQpapmdaedtvwagdgveeepeeedehlgNLDEEEIKKMQSDEgtaglevtayeemsslvny 550
Cdd:cd08599   147 -------------PPVIRN----------------------------SLSETQLKKVIEGE------------------- 166

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  551 iqpikfdsfevsaqknrsyvissftelkaydlltkFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGCQMVALNF 630
Cdd:cd08599   167 -----------------------------------HPTDLIEFTQKNLLRVYPAGLRITSSNYDPMLAWMHGAQMVALNM 211

                         330
                  ....*....|....*..
gi 704462060  631 QTMDVPMQQNMALFEFN 647
Cdd:cd08599   212 QGYDRPLWLNRGKFRAN 228
PH_PLC_beta cd13361
Phospholipase C-beta (PLC-beta) pleckstrin homology (PH) domain; PLC-beta (PLCbeta) is ...
 17-144 7.11e-57

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: 192.40  E-value: 7.11e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   17 LSKGERFIKWDDETASASPVILRVDPKGFYLYWTDQNKEMEILDITSIRDTRVGRFAKIPKCQKLREVfNLDYPHSTFLL 96
Cdd:cd13361     1 LLKGSKFDKWDEDSSLETPVTLKVDEYGFFLYWKSEGKETEVLDLSLIRDVRTGKYPKDPKDLKEREV-NVGGSDEDLED 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 704462060   97 KTLTIVSGPDMVDLTFHNFVSYKENVGKSWAEDIMAIVRNPLTYNASR 144
Cdd:cd13361    80 RTLTIVSGTDLVNISFINFVAESEEVAKIWTEGLFKLAHNLLANNASP 127
PLN02228 PLN02228
Phosphoinositide phospholipase C
 217-780 3.50e-54

Phosphoinositide phospholipase C


Pssm-ID: 177873 [Multi-domain]  Cd Length: 567  Bit Score: 199.49  E-value: 3.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  217 PRPEIDEIFTSHHLKAKpyMTKEHLAKFINKKQRDSRlndilfppAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLC 296
Cdd:PLN02228   22 PPVSIKRLFEAYSRNGK--MSFDELLRFVSEVQGERH--------AGLDYVQDIFHSVKHHNVFHHHGLVHLNAFYRYLF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  297 GPENNVIALDKLVlYQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKGrPPDEEPIITHGF 376
Cdd:PLN02228   92 SDTNSPLPMSGQV-HHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWPN-PSGNAAEVRHGR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  377 TMTTEILFKDAIEAIAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPLkpgvpLPSPKDLLG 456
Cdd:PLN02228  170 TLTSHEDLQKCLNAIKDNAFQVSDYPVVITLEDHL-PPNLQAQVAKMLTKTFRGMLFRCTSESTKH-----FPSPEELKN 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  457 KILIKNKKKQSVsgkrqnslkkgrnVEPEVIEQPAPMDAEDTVWAGDGveeepeeedehlgnlDEEEikKMQSDEGTAGL 536
Cdd:PLN02228  244 KILISTKPPKEY-------------LESKTVQTTRTPTVKETSWKRVA---------------DAEN--KILEEYKDEES 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  537 EVTAYEEMSSL--VNYIQPIKfDSFEVSAQKNRSYvisSFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYM 614
Cdd:PLN02228  294 EAVGYRDLIAIhaANCKDPLK-DCLSDDPEKPIRV---SMDEQWLETMVRTRGTDLVRFTQRNLVRIYPKGTRVDSSNYD 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  615 PQMFWNVGCQMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRRPDKQFDPFSvdriDVVVASTLSVTILSGQ---- 690
Cdd:PLN02228  370 PHVGWTHGAQMVAFNMQGHGKQLWIMQGMFRANGGCGYVKKPRILLDEHTLFDPCK----RLPIKTTLKVKIYTGEgwdl 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  691 ------FLSDRSVKTYVEVELFGLPRDTKrKYRTKLtsTANSINPVWKEEAFVFEkIMMPELASL--KIVAWEEGGK--F 760
Cdd:PLN02228  446 dfhlthFDQYSPPDFFVKIGIAGVPRDTV-SYRTET--AVDQWFPIWGNDEFLFQ-LRVPELALLwfKVQDYDNDTQndF 521

                         570       580
                  ....*....|....*....|
gi 704462060  761 IGHRVIPVTAVHSGYHHVCL 780
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, ...
 149-299 4.64e-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: 170.87  E-value: 4.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  149 EKILVKLKMQLNAEGKIPVRNIFQMFPADRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSH 228
Cdd:cd16210     1 RKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIKPDEFTLEIFERFLNKLCLRPDIDKILLEI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704462060  229 HLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16210    81 GAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQVRQLIEKYEPNQQFLERDQMSMEGFSRYLGGEE 151
EFh_PI-PLC21 cd16213
EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family ...
 149-295 1.68e-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: 1.68e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  149 EKILVKLKMQLNAEGKIPVRNIFQMFPA---DRKRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIF 225
Cdd:cd16213     1 EKAYTKLTLQTDKEGKIPVKNIVKMFAQhkdDRKRVEKALEAIGLPSGKNDAIDPKKFTFEDFFNFYRRLTGRQEVEKIF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  226 TSHHLKAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFL 295
Cdd:cd16213    81 DELGAKKKPYLTTEQFVDFLNKTQRDPRLNEILYPYANPKRARDLINQYEPNKSFAKKGHLSVEGFLRYL 150
PLN02230 PLN02230
phosphoinositide phospholipase C 4
 310-798 3.95e-47

phosphoinositide phospholipase C 4


Pssm-ID: 177875 [Multi-domain]  Cd Length: 598  Bit Score: 179.13  E-value: 3.95e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  310 LYQDMTQPLSHYFINSSHNTYLTAGQFSGISSPEMYRQTLLAGCRCVELDCWKgRPPDEePIITHGFTMTTEILFKDAIE 389
Cdd:PLN02230  113 VHQNMDAPLSHYFIFTGHNSYLTGNQLSSNCSELPIADALRRGVRVVELDLWP-RGTDD-VCVKHGRTLTKEVKLGKCLD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  390 AIAESAFKTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPLEKYPlkpgvPLPSPKDLLGKILIKNKKK---- 465
Cdd:PLN02230  191 SIKANAFAISKYPVIITLEDHL-TPKLQFKVAKMITQTFGDMLYYHDSEGCQ-----EFPSPEELKEKILISTKPPkeyl 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  466 QSVSGKRQNSLKKGRNVEPEVIEQpapmDAEDTVwagdGVEEEPEEEDEHLGNL--DEEEIKKMQSDEgTAGLEVTAYEE 543
Cdd:PLN02230  265 EANDAKEKDNGEKGKDSDEDVWGK----EPEDLI----STQSDLDKVTSSVNDLnqDDEERGSCESDT-SCQLQAPEYKR 335

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  544 MSSlVNYIQPIKFDSFEVSAQKNRSYVISsFTELKAYDLLTKFPVQFVEYNKRQMSRIYPKGTRMDSSNYMPQMFWNVGC 623
Cdd:PLN02230  336 LIA-IHAGKPKGGLRMALKVDPNKIRRLS-LSEQLLEKAVASYGADVIRFTQKNFLRIYPKGTRFNSSNYKPQIGWMSGA 413

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  624 QMVALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRRPDKQFDPFsVDRIDVVVASTLSVTILSG----------QFLS 693
Cdd:PLN02230  414 QMIAFNMQGYGRALWLMEGMFRANGGCGYVKKPDFLMDAGPNGQDF-YPKDNSCPKKTLKVKVCMGdgwlldfkktHFDS 492

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  694 DRSVKTYVEVELFGLPRDTKRKyRTKLTStaNSINPVWKEEaFVFeKIMMPELASLKIVAWE----EGGKFIGHRVIPVT 769
Cdd:PLN02230  493 YSPPDFFVRVGIAGAPVDEVME-KTKIEY--DTWTPIWNKE-FIF-PLAVPELALLRVEVHEhdinEKDDFGGQTCLPVS 567

                         490       500
                  ....*....|....*....|....*....
gi 704462060  770 AVHSGYHHVCLRSESNMPLTMPSLFVYLE 798
Cdd:PLN02230  568 EIRQGIHAVPLFNRKGVKYSSTRLLMRFE 596
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 681-800 5.48e-37

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: 135.36  E-value: 5.48e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  681 TLSVTILSGQFLSD------RSVKTYVEVELFGLPRDTKRKYRTKlTSTANSINPVWkEEAFVFEkIMMPELASLKIVAW 754
Cdd:cd00275     3 TLTIKIISGQQLPKpkgdkgSIVDPYVEVEIHGLPADDSAKFKTK-VVKNNGFNPVW-NETFEFD-VTVPELAFLRFVVY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 704462060  755 EEGG---KFIGHRVIPVTAVHSGYHHVCLRSESNMPLTMPSLFVYLEIK 800
Cdd:cd00275    80 DEDSgddDFLGQACLPLDSLRQGYRHVPLLDSKGEPLELSTLFVHIDIT 128
EFh_PI-PLCbeta4 cd16211
EF-hand motif found in phosphoinositide phospholipase C beta 4 (PI-PLC-beta4); PI-PLC-beta4, ...
 154-295 2.25e-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: 120.60  E-value: 2.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  154 KLKMQLNAEGKIPVRNIFQMFPADR--KRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSHHLK 231
Cdd:cd16211     6 RLCFLVNPNGKIPVRSITRTFASGKteKIVFQSLKELGLPSGKNDEIEPEAFTFEKFYELYHKICPRTDIEELFKKINGD 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 704462060  232 AKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFL 295
Cdd:cd16211    86 KKDYLTVDQLISFLNEHQRDPRLNEILFPFYDRKRVMQIIETYEVDEEFKKKEQLSSDGFCRYL 149
PLN02223 PLN02223
phosphoinositide phospholipase C
 309-789 5.92e-27

phosphoinositide phospholipase C


Pssm-ID: 165867 [Multi-domain]  Cd Length: 537  Bit Score: 117.05  E-value: 5.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  309 VLYQDMTQPLSHYFINSSHNTYLTAGQ-FSGISSPEMYRQTLLAGCRCVELDCWkgrPPDEEPI-ITHGFTMTTEILFKD 386
Cdd:PLN02223  103 VRHHDMHAPLSHYFIHTSLKSYFTGNNvFGKLYSIEPIIDALEQGVRVVELDLL---PDGKDGIcVRPKWNFEKPLELQE 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  387 AIEAIAESAF-KTSLYPVILSFENHVdSPKQQAKMAEYCRTIFGDMLLTEPlekyPLKPGVPLPSPKDLLGKILIKNKKK 465
Cdd:PLN02223  180 CLDAIKEHAFtKCRSYPLIITFKDGL-KPDLQSKATQMIDQTFGDMVYHED----PQHSLEEFPSPAELQNKILISRRPP 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  466 QSVSGKRQNSLKKGRNVEPEVIEQPAPMDAEDTVwagdgveeepeeedehlgnldeeeikkmqsdegtaGLEVTayeEMS 545
Cdd:PLN02223  255 KELLYAKADDGGVGVRNELEIQEGPADKNYQSLV-----------------------------------GFHAV---EPR 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  546 SLVNYIQPIKFDSFEVSAQKNRSyvISSFTELKaydLLTKFPvqfveynKRQMSRIYPKgtrmdssnYMPQMFWNVGCQM 625
Cdd:PLN02223  297 GMLQKALTGKADDIQQPGWYERD--IISFTQKK---FLRTRP-------KKKNLLINAP--------YKPQRAWMHGAQL 356

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  626 VALNFQTMDVPMQQNMALFEFNGQCGYLLKHEFMRR--PDKQFDPfsvdRIDVVVASTLSVTILSGQ-FLSDRSVKT--- 699
Cdd:PLN02223  357 IALSRKDDKEKLWLMQGMFRANGGCGYVKKPDFLLNagPSGVFYP----TENPVVVKILKVKIYMGDgWIVDFKKRIgrl 432

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  700 -----YVEVELFGLPRDTKrkyRTKLTSTANSINPVWKEEaFVFeKIMMPELA--SLKIVAWE--EGGKFIGHRVIPVTA 770
Cdd:PLN02223  433 skpdlYVRISIAGVPHDEK---IMKTTVKNNEWKPTWGEE-FTF-PLTYPDLAliSFEVYDYEvsTADAFCGQTCLPVSE 507

                         490       500
                  ....*....|....*....|....*
gi 704462060  771 VHSGYHHVCLRSE------SNMPLT 789
Cdd:PLN02223  508 LIEGIRAVPLYDErgkacsSTMLLT 532
EFh_NorpA_like cd16212
EF-hand motif found in Drosophila melanogaster No receptor potential A protein (NorpA) and ...
 153-299 4.00e-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: 102.63  E-value: 4.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  153 VKLKMQLNAEGKIPVRNIFQMFPADR--KRVEAALSACHLPKGKNDAINPEDFPETVYKTFLMNLCPRPEIDEIFTSHHL 230
Cdd:cd16212     5 MRLGFMVDSGGKIPVKHIARTFASGKteKLVYQCLAEMGLPSGKGDSIEKEDFTFEKFYALYHKICPRNDIEELFTSITK 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 704462060  231 KAKPYMTKEHLAKFINKKQRDSRLNDILFPPAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16212    85 GKGEHISLAQLINFMNDKQRDPRLNEILYPLYDEKRCTEIIKAYEQNEENIKNKRMSKDGFIRYLMSDE 153
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 324-630 7.26e-24

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


Pssm-ID: 176498 [Multi-domain]  Cd Length: 179  Bit Score: 99.82  E-value: 7.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  324 NSSHNTYLTAGQfsgISSPEMYRQTLLAGCRCVELDCWKGrpPDEEPIITHGFTMT------TEILFKDAIEAIAESAFK 397
Cdd:cd08555     1 VLSHRGYSQNGQ---ENTLEAFYRALDAGARGLELDVRLT--KDGELVVYHGPTLDrttagiLPPTLEEVLELIADYLKN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  398 TSlYPVILSFENHVDS---PKQQAKMAEYCRTIFGDmllteplekyplkpgvplpspkDLLGKILIKnkkkqsvsgkrqn 474
Cdd:cd08555    76 PD-YTIILSLEIKQDSpeyDEFLAKVLKELRVYFDY----------------------DLRGKVVLS------------- 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  475 slkkgrnvepevieqpapmdaedtvwagdgveeepeeedehlgnldeeeikkmqsdegtaglevtayeemsslvnyiqpi 554
Cdd:cd08555       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 704462060  555 kfdsfevsaqknrSYVISSFTELKAYDLLTKFPVQFVEYNK-RQMSRIYPKGTrmdsSNYMPQMFWNVGCQMVALNF 630
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 ...
 195-299 1.18e-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: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  195 NDAINPEDFpetvyKTFLMNLCPRPEIDEIFTSHHlKAKPYMTKEHLAKFINKKQRdsrlndilFPPAKPEQVQSLIEKY 274
Cdd:cd16202    50 EDVLDEEEF-----VQFYNRLTKRPEIEELFKKYS-GDDEALTVEELRRFLQEEQK--------VKDVTLEWAEQLIETY 115

                          90       100
                  ....*....|....*....|....*
gi 704462060  275 EPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16202   116 EPSEDLKAQGLMSLDGFTLFLLSPD 140
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 681-780 9.57e-13

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


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 65.59  E-value: 9.57e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060    681 TLSVTILSGQFLSDR----SVKTYVEVELFGlprDTKRKYRTKltSTANSINPVWKEEaFVFEkIMMPELASLKIVAWEE 756
Cdd:smart00239    1 TLTVKIISARNLPPKdkggKSDPYVKVSLDG---DPKEKKKTK--VVKNTLNPVWNET-FEFE-VPPPELAELEIEVYDK 73

                            90       100
                    ....*....|....*....|....*...
gi 704462060    757 GG----KFIGHRVIPVTAVHSGYHHVCL 780
Cdd:smart00239   74 DRfgrdDFIGQVTIPLSDLLLGGRHEKL 101
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 155-299 8.61e-11

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 61.14  E-value: 8.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  155 LKMQLNAEGKIPVRNIFQM-----FPADRKRVEAALSACHlpKGKNDAINPEDFpetvyKTFLMNLCPRPEIDEIFTSHH 229
Cdd:cd15898     7 IKADKDGDGKLSLKEIKKLlkrlnIRVSEKELKKLFKEVD--TNGDGTLTFDEF-----EELYKSLTERPELEPIFKKYA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  230 LKAKPYMTKEHLAKFINKKQRDSRlndilfppaKPEQVQSLIEKYEPSGiniQRGQLSPEGMVWFLCGPE 299
Cdd:cd15898    80 GTNRDYMTLEEFIRFLREEQGENV---------SEEECEELIEKYEPER---ENRQLSFEGFTNFLLSPE 137
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 875-1124 1.20e-09

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: 62.45  E-value: 1.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   875 SLAELQQMKLFLKLVK---KQEKE--LRELERK-----GSKRREELLQKYSVLFSEP--VCYGGKKRMMHTRKTQKKRSL 942
Cdd:pfam17380  283 AVSERQQQEKFEKMEQerlRQEKEekAREVERRrkleeAEKARQAEMDRQAAIYAEQerMAMERERELERIRQEERKREL 362

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   943 TTgdvgtgANPVEVAESIdSRVLELrERLEMDLLRLGEEQHDEV------------RRRKEQHATEQVTKITELAREKQA 1010
Cdd:pfam17380  363 ER------IRQEEIAMEI-SRMREL-ERLQMERQQKNERVRQELeaarkvkileeeRQRKIQQQKVEMEQIRAEQEEARQ 434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1011 AELKALKEASESNIKDIKKKlEAKRVDRIQaMMRNTGDKAAQERLKKEINNSHIQEVVQTIKQVTEK--TARCQQKLEEk 1088
Cdd:pfam17380  435 REVRRLEEERAREMERVRLE-EQERQQQVE-RLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKelEERKQAMIEE- 511

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 704462060  1089 qaENLRAIREKEIQLQQEALAEHQEKlksltREAQE 1124
Cdd:pfam17380  512 --ERKRKLLEKEMEERQKAIYEEERR-----REAEE 540
C2 pfam00168
C2 domain;
681-774 2.63e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 52.71  E-value: 2.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   681 TLSVTILSGQFL----SDRSVKTYVEVELfglpRDTKRKYRTKLTStaNSINPVWKEEaFVFEkIMMPELASLKIVAWEE 756
Cdd:pfam00168    2 RLTVTVIEAKNLppkdGNGTSDPYVKVYL----LDGKQKKKTKVVK--NTLNPVWNET-FTFS-VPDPENAVLEIEVYDY 73

                           90       100
                   ....*....|....*....|..
gi 704462060   757 GG----KFIGHRVIPVTAVHSG 774
Cdd:pfam00168   74 DRfgrdDFIGEVRIPLSELDSG 95
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 870-1120 3.15e-08

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: 57.83  E-value: 3.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   870 EPQTASLAELQQMKLFLKLVKKQEKELRELER--KGSKRREEL--LQKYSVLFSEP--VCYGGKKRMMHTRKTQkkrslt 943
Cdd:pfam17380  356 EERKRELERIRQEEIAMEISRMRELERLQMERqqKNERVRQELeaARKVKILEEERqrKIQQQKVEMEQIRAEQ------ 429

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   944 tgdvgtganpvEVAESIDSRVLELRERLEMDLLRLGEEQHDEVRRRKEQHATEQVTKITELAREKQAAEL---------- 1013
Cdd:pfam17380  430 -----------EEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRaeeqrrkile 498

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1014 KALKEASESNIKDIKKK--LEAKRVDRIQAMMRNTGDKAAQERLKKEINNSHIQEVVQTIKQVTEKTARCQQKleEKQAE 1091
Cdd:pfam17380  499 KELEERKQAMIEEERKRklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM--ERERE 576

                          250       260
                   ....*....|....*....|....*....
gi 704462060  1092 NLRAIREKEIQLQQEALAEHQEKLKSLTR 1120
Cdd:pfam17380  577 MMRQIVESEKARAEYEATTPITTIKPIYR 605
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 954-1132 5.22e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 5.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  954 VEVAESIDSRVLELRERLEMDLLRLgEEQHDEVRRRKEQHATEqvtkiteLAREK-QAAELKALKEASESNIKDIKKKLE 1032
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEEL-EEELAELEEELEELEEE-------LEELEeELEEAEEELEEAEAELAEAEEALL 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1033 AKRVDRIQAMMRNTGDKAAQERLKKEINN--SHIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREKEIQLQ-----Q 1105
Cdd:COG1196   369 EAEAELAEAEEELEELAEELLEALRAAAElaAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEaleeaA 448

                         170       180
                  ....*....|....*....|....*..
gi 704462060 1106 EALAEHQEKLKSLTREAQETVKNFATA 1132
Cdd:COG1196   449 EEEAELEEEEEALLELLAELLEEAALL 475
EF-hand_like pfam09279
Phosphoinositide-specific phospholipase C, efhand-like; Members of this family are ...
 215-302 1.05e-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: 50.71  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   215 LCPRPEIDEIFTSHHlKAKPYMTKEHLAKFINKKQRDSRlndilfppAKPEQVQSLIEKYEPSGINIQRGQLSPEGMVWF 294
Cdd:pfam09279    5 LTQREEIDEIFQEYS-GDGQKLSLDELVDFLREEQREED--------ASPALALSLIERYEPSETAKKQHAMTKDGFLMY 75


                   ....*...
gi 704462060   295 LCGPENNV 302
Cdd:pfam09279   76 LCSPDGSI 83
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 876-1124 4.99e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 4.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  876 LAELQQMKLFLKLVKKQEKELRELERKGSKRREELLQKYSVLfsepvcyggkkrmmHTRKTQKKRSLTtgdvgtganpvE 955
Cdd:COG1196   224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL--------------EAELEELRLELE-----------E 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  956 VAESIDSRVLELRErLEMDLLRLgEEQHDEVRRRKEQHATEQVTKITELAREK-QAAELKALKEASESNIKDIKKKLEAK 1034
Cdd:COG1196   279 LELELEEAQAEEYE-LLAELARL-EQDIARLEERRRELEERLEELEEELAELEeELEELEEELEELEEELEEAEEELEEA 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1035 RVDRIQAMMRNTGDKAAQERLKKEInNSHIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIR-EKEIQLQQEALAEHQE 1113
Cdd:COG1196   357 EAELAEAEEALLEAEAELAEAEEEL-EELAEELLEALRAAAELAAQLEELEEAEEALLERLERlEEELEELEEALAELEE 435

                         250
                  ....*....|.
gi 704462060 1114 KLKSLTREAQE 1124
Cdd:COG1196   436 EEEEEEEALEE 446
PTZ00121 PTZ00121
MAEBL; Provisional
 890-1127 6.48e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 6.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  890 KKQEKELRELERKGS----KRREELLQKYSVLFSEPVCYGGKKRMMHTRKTQKKRSLTTGDVGTGANPVEVAESIDSRVL 965
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKadelKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  966 --ELRERLEMDLLRLGEEQHDEVRRRKEQHAtEQVTKITELAREKQAAELKALKEASESNiKDIKKKLEAKRVDRiqamm 1043
Cdd:PTZ00121 1613 kkAEEAKIKAEELKKAEEEKKKVEQLKKKEA-EEKKKAEELKKAEEENKIKAAEEAKKAE-EDKKKAEEAKKAEE----- 1685

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1044 rntGDKAAQERLKKEinnshiQEVVQTIKQVTEKTARCQQKLEE-KQAENLRAIREKEIQLQQEalaEHQEKLKSLTREA 1122
Cdd:PTZ00121 1686 ---DEKKAAEALKKE------AEEAKKAEELKKKEAEEKKKAEElKKAEEENKIKAEEAKKEAE---EDKKKAEEAKKDE 1753


                  ....*
gi 704462060 1123 QETVK 1127
Cdd:PTZ00121 1754 EEKKK 1758
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
957-1132 1.07e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  957 AESIDSRVLELRERLE------MDLLRLgEEQHDEVRRRKEQHATEQVTKITELAR-EKQAAELKALKEASESNIKDIKK 1029
Cdd:COG4913   663 VASAEREIAELEAELErldassDDLAAL-EEQLEELEAELEELEEELDELKGEIGRlEKELEQAEEELDELQDRLEAAED 741

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1030 KLEAKRVDRIQAMMRNTGDKAAQERLKKEINNShiqevvqtIKQVTEKTARCQQKLEEKQA-----------------EN 1092
Cdd:COG4913   742 LARLELRALLEERFAAALGDAVERELRENLEER--------IDALRARLNRAEEELERAMRafnrewpaetadldadlES 813

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 704462060 1093 LRAIREKEIQLQQEALAEHQEKLK-SLTREAQETVKNFATA 1132
Cdd:COG4913   814 LPEYLALLDRLEEDGLPEYEERFKeLLNENSIEFVADLLSK 854
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
 209-299 1.53e-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: 48.97  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  209 KTFLMNLCPRPEIDEIFTSHHlKAKPYMTKEHLAKFINKKQRDsrlndilfpPAKPEQVQSLIEKYEPSGINIQRGQLSP 288
Cdd:cd16217    59 EEFYKLLTKREEIDVIFGEYA-KSDGTMSRNNLLNFLQEEQRE---------EVAPAYALSLIEKYEPDETAKAQRQMTK 128

                          90
                  ....*....|.
gi 704462060  289 EGMVWFLCGPE 299
Cdd:cd16217   129 DGFLMYLLSPE 139
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 960-1117 2.28e-06

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: 50.31  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  960 IDSRVLELRERLEmDLLRLGEEQHDEVRRRKEQHATEQvTKITELAREKQAAELKAlkEASESNIKDIKKKLEAKRVDR- 1038
Cdd:COG1579    15 LDSELDRLEHRLK-ELPAELAELEDELAALEARLEAAK-TELEDLEKEIKRLELEI--EEVEARIKKYEEQLGNVRNNKe 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1039 IQAMMRN-TGDKAAQERLKKEINNSH--IQEVVQTIKQVTEKTARCQQKLEEKQAEnlRAIREKEIQLQQEALAEHQEKL 1115
Cdd:COG1579    91 YEALQKEiESLKRRISDLEDEILELMerIEELEEELAELEAELAELEAELEEKKAE--LDEELAELEAELEELEAEREEL 168


                  ..
gi 704462060 1116 KS 1117
Cdd:COG1579   169 AA 170
PTZ00121 PTZ00121
MAEBL; Provisional
 887-1141 1.10e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  887 KLVKKQEKELRELERKGSKRREELLQKYSVLfsepvcyggkkRMMHTRKTQKKRSLTTGDVGTGANPVEVAESIDSRVLE 966
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEA-----------KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  967 LR--ERLEMDLLRLGEEQHDEVRRRKEQHATEQVTKI--TELARE-----KQAAELKALKEASESNIKDIKKKLE-AKRV 1036
Cdd:PTZ00121 1625 LKkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaAEEAKKaeedkKKAEEAKKAEEDEKKAAEALKKEAEeAKKA 1704

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1037 DRIQAMMRNTGDKAaqERLKK--EINNSHIQEV----------VQTIKQVTEKTARCQQ--KLEEKQAENLRaiREKEIQ 1102
Cdd:PTZ00121 1705 EELKKKEAEEKKKA--EELKKaeEENKIKAEEAkkeaeedkkkAEEAKKDEEEKKKIAHlkKEEEKKAEEIR--KEKEAV 1780

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 704462060 1103 LQQEALAEHQEKLKSLTREAQETVKNFATAGFAGELGTP 1141
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNL 1819
PTZ00121 PTZ00121
MAEBL; Provisional
 957-1170 1.10e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  957 AESIDSRVLELRERLE----MDLLRLGEEQH--DEVRRRKEQHATEQVTKitelAREKQAAElkALKEASESNIKDIKKK 1030
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEakkkADEAKKAEEAKkaDEAKKAEEAKKADEAKK----AEEKKKAD--ELKKAEELKKAEEKKK 1565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1031 LEAKRVD--------------------RIQAMMR--NTGDKAAQERLKKEINNSHIQEVVQTIKQVTEKTARCQQKLEE- 1087
Cdd:PTZ00121 1566 AEEAKKAeedknmalrkaeeakkaeeaRIEEVMKlyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEe 1645

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1088 -KQAENLR-AIREKEIQLQQEALAEHQEKLKS-LTREAQETVKNFATAGFAGELGTPKAagqsvpegEQVRTGHVEEKTP 1164
Cdd:PTZ00121 1646 kKKAEELKkAEEENKIKAAEEAKKAEEDKKKAeEAKKAEEDEKKAAEALKKEAEEAKKA--------EELKKKEAEEKKK 1717


                  ....*.
gi 704462060 1165 VAEVSR 1170
Cdd:PTZ00121 1718 AEELKK 1723
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 935-1126 1.11e-05

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 49.62  E-value: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   935 KTQKKRSLTTGDVGTGANPVEVAESIDSRVLE-LRE------RLEMDLLRLGEEQHDEVRRRKEQHATEQVTKITELARE 1007
Cdd:pfam05262  153 KTQIVIPLKKNILSGNVSDVDTDSISDKKVVEaLREdnekgvNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKA 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1008 KQAAELKalKEASESNIKDIKKKL-EAKRVDRIQAMMRNTGDKAAQERLKKEINNSHIQevvqtikqvTEKTARCQQKLE 1086
Cdd:pfam05262  233 QQKADFA--QDNADKQRDEVRQKQqEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIE---------IKKNDEEALKAK 301

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 704462060  1087 EKQAENLRAIREKEIQLQQEALAEHQEKLKSLTREAQETV 1126
Cdd:pfam05262  302 DHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTK 341
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
934-1161 1.50e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  934 RKTQKKR-SLTTGDVGTGANPVEVAESIDSRVLELRE-RLEMDLLRlgeEQHDEVRRRKEQHATEQVTKITELAR----- 1006
Cdd:COG4372     6 EKVGKARlSLFGLRPKTGILIAALSEQLRKALFELDKlQEELEQLR---EELEQAREELEQLEEELEQARSELEQleeel 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1007 ---EKQAAELKALKEASESNIKDIKKKLEAKRvDRIQAMmrntgdKAAQERLKKEIN--NSHIQEVVQTIKQVTEKTARC 1081
Cdd:COG4372    83 eelNEQLQAAQAELAQAQEELESLQEEAEELQ-EELEEL------QKERQDLEQQRKqlEAQIAELQSEIAEREEELKEL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1082 QQKLEEKQAEnlraIREKEIQLQQEALAEHQEKLKSLTREAQETVKNFATAGFAGELGTPKAAGQSVPEGEQVRTGHVEE 1161
Cdd:COG4372   156 EEQLESLQEE----LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 892-1096 1.51e-05

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 48.88  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   892 QEKELRELERKGSKRREELLQkysvLFSEPVCYGGKKRMMHTRKTQKKRSLT--TGDVGTGANPVEVAESIDSRVLELRE 969
Cdd:pfam15558  125 QEQRLKEKEEELQALREQNSL----QLQERLEEACHKRQLKEREEQKKVQENnlSELLNHQARKVLVDCQAKAEELLRRL 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   970 RLEMDLLR-------LGEEQHDEVRRR--KEQHATEQVTKITELAREKQAAELKALKEASESNIK---DIKKKLEAKRVD 1037
Cdd:pfam15558  201 SLEQSLQRsqenyeqLVEERHRELREKaqKEEEQFQRAKWRAEEKEEERQEHKEALAELADRKIQqarQVAHKTVQDKAQ 280

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 704462060  1038 RIQAM--MRNTGDKAAQERLKKEiNNSHIQEVVQTIKqvtEKTARCQQKLEEKQA--ENLRAI 1096
Cdd:pfam15558  281 RARELnlEREKNHHILKLKVEKE-EKCHREGIKEAIK---KKEQRSEQISREKEAtlEEARKT 339
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 968-1124 2.91e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 2.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   968 RERLEMDLLRLGEEQHDEVRRRKEQHA--TEQVTKITELAREKQA-----AELKALKEASESNIKDIKKKLEAKRVDRIQ 1040
Cdd:TIGR02168  311 LANLERQLEELEAQLEELESKLDELAEelAELEEKLEELKEELESleaelEELEAELEELESRLEELEEQLETLRSKVAQ 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1041 amMRNTGDKAA----------------QERLKKEINNSHIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREKEIqlQ 1104
Cdd:TIGR02168  391 --LELQIASLNneierlearlerledrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE--L 466

                          170       180
                   ....*....|....*....|
gi 704462060  1105 QEALAEHQEKLKSLTREAQE 1124
Cdd:TIGR02168  467 REELEEAEQALDAAERELAQ 486
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1004-1124 3.92e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 3.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1004 LAREKQAAELKALKEASESNIKDIKKKLEAKRVDRIQAMMRNTGDKAAQERLKKEINN--SHIQEVVQTIKQVTEKTARC 1081
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 704462060  1082 QQKLEEKQAEnlRAIREKEIQLQQEALAEHQEKLKSLTREAQE 1124
Cdd:TIGR02168  753 SKELTELEAE--IEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 1007-1129 5.01e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.51  E-value: 5.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1007 EKQAAELKALKEASESNIKDIKKKLEAkrvdriqammrntgdkaAQERLKKEINNSHiQEVVQTIKQVTEKTARCQQKLE 1086
Cdd:PRK00409  533 EQKAEEAEALLKEAEKLKEELEEKKEK-----------------LQEEEDKLLEEAE-KEAQQAIKEAKKEADEIIKELR 594

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 704462060 1087 EKQAENLRAIREKEIQLQQEALAEHQEKLKSLTREAQETVKNF 1129
Cdd:PRK00409  595 QLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEEL 637
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 974-1120 5.37e-05

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: 47.44  E-value: 5.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   974 DLLRLGEEQhDEVRRRKEQHATEQVTKITELAREKQAAELKALKEASESNIKDIKKKLEAKRVdRIQAMMRNTGdKAAQE 1053
Cdd:pfam09731  295 EIDQLSKKL-AELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFERERE-EIRESYEEKL-RTELE 371

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 704462060  1054 RlKKEINNSHIQEVVQTIKQvtektarcqqKLEEKQAENLRAIREKEIQLQQEALAEHQEKLKSLTR 1120
Cdd:pfam09731  372 R-QAEAHEEHLKDVLVEQEI----------ELQREFLQDIKEKVEEERAGRLLKLNELLANLKGLEK 427
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
879-1124 5.53e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 5.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  879 LQQMKLFLKLVKKQEKELRELERKGSKRRE--ELLQKYSVLFSEpvcygGKKRMmhTRKTQKKRSLTtgdvgtgaNPVEV 956
Cdd:PRK03918  268 IEELKKEIEELEEKVKELKELKEKAEEYIKlsEFYEEYLDELRE-----IEKRL--SRLEEEINGIE--------ERIKE 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  957 AESIDSRVLELRERLEMDLLRLGE-----EQHDEVRRRKEQhATEQVTKITELAREKQAAELKALKEASE------SNIK 1025
Cdd:PRK03918  333 LEEKEERLEELKKKLKELEKRLEEleerhELYEEAKAKKEE-LERLKKRLTGLTPEKLEKELEELEKAKEeieeeiSKIT 411

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1026 DIKKKLEAKRVDRIQAMMRNTGDKAAQERLKKEINNSH----IQEVVQTIKQVTEKTARCQQKLEE--KQAENLRAIREK 1099
Cdd:PRK03918  412 ARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHrkelLEEYTAELKRIEKELKEIEEKERKlrKELRELEKVLKK 491

                         250       260       270
                  ....*....|....*....|....*....|
gi 704462060 1100 EIQLQQ-----EALAEHQEKLKSLTREAQE 1124
Cdd:PRK03918  492 ESELIKlkelaEQLKELEEKLKKYNLEELE 521
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 984-1132 6.16e-05

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


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 44.95  E-value: 6.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   984 DEVRRRKEQhATEQVTKITELAREKQAAELKALKEASESNIKDIKKKLEAKRvDRIQAMMRNTGDKAAQeRLK---KEIN 1060
Cdd:pfam01442    7 DELSTYAEE-LQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYL-EELQAKLGQNVEELRQ-RLEpytEELR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1061 NSHIQEVVQTIKQVTEKTARCQQKLEEKQ----------AENLRA-IREKEIQLQQ---EALAEHQEKLKSLTREAQETV 1126
Cdd:pfam01442   84 KRLNADAEELQEKLAPYGEELRERLEQNVdalrarlapyAEELRQkLAERLEELKEslaPYAEEVQAQLSQRLQELREKL 163


                   ....*.
gi 704462060  1127 KNFATA 1132
Cdd:pfam01442  164 EPQAED 169
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 969-1124 6.75e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 6.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  969 ERLEmDLLrlgeeqhDEVRRRKEQhateqvtkiteLAREKQAA----ELKAlkeasesNIKDIKKKLEAKRVDRIQAMMR 1044
Cdd:COG1196   189 ERLE-DIL-------GELERQLEP-----------LERQAEKAeryrELKE-------ELKELEAELLLLKLRELEAELE 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1045 NTGDKAAQERLKKEINNSHIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIR-----EKEIQLQQEALAEHQEKLKSLT 1119
Cdd:COG1196   243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAelarlEQDIARLEERRRELEERLEELE 322


                  ....*
gi 704462060 1120 REAQE 1124
Cdd:COG1196   323 EELAE 327
PTZ00121 PTZ00121
MAEBL; Provisional
 887-1127 7.94e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 7.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  887 KLVKKQEKELRELERkgSKRREELLQKYSVLFSEPvcyggKKRMMHTRKTQKKRSLTTGDVGTGANPVEVAEsidsRVLE 966
Cdd:PTZ00121 1118 EEAKKKAEDARKAEE--ARKAEDARKAEEARKAED-----AKRVEIARKAEDARKAEEARKAEDAKKAEAAR----KAEE 1186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  967 LRERLEmdlLRLGEE--QHDEVRRRKEQHATEQVTKITElarEKQAAELKALKEASesnikdiKKKLEAKRVDRIqammR 1044
Cdd:PTZ00121 1187 VRKAEE---LRKAEDarKAEAARKAEEERKAEEARKAED---AKKAEAVKKAEEAK-------KDAEEAKKAEEE----R 1249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1045 NTgdkaAQERLKKEINNSHIQEVVQTIKQVTEKTARCQQKLEE-KQAENLRAIREKEIQLQQEALAEHQEKLKSLTREAQ 1123
Cdd:PTZ00121 1250 NN----EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEkKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325


                  ....
gi 704462060 1124 ETVK 1127
Cdd:PTZ00121 1326 EAKK 1329
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
955-1132 8.23e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 8.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  955 EVAESIDSRVLELRERLEMDllrlgEEQHDEVRRRKEQHATEQVTKiTELAREKQAAELKALKEASESNIK--DIKKKLE 1032
Cdd:PRK02224  516 ERREDLEELIAERRETIEEK-----RERAEELRERAAELEAEAEEK-REAAAEAEEEAEEAREEVAELNSKlaELKERIE 589

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1033 A-KRVDRIQAMMRNTGDKAA--QERLKK--EINN---SHIQEVVQTIKQVTEK--TARCQQKLEEKQ---------AENL 1093
Cdd:PRK02224  590 SlERIRTLLAAIADAEDEIErlREKREAlaELNDerrERLAEKRERKRELEAEfdEARIEEAREDKEraeeyleqvEEKL 669

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 704462060 1094 RAIREKEIQLQQ---------EALAEHQEKLKSL--TREAQETVKNFATA 1132
Cdd:PRK02224  670 DELREERDDLQAeigavenelEELEELRERREALenRVEALEALYDEAEE 719
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 682-776 8.36e-05

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


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 42.82  E-value: 8.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  682 LSVTILSGQFLSDR----SVKTYVEVELfglprDTKRKYRTKLTStaNSINPVWKEEaFVFEkIMMPELASLKIVAWEEG 757
Cdd:cd00030     1 LRVTVIEARNLPAKdlngKSDPYVKVSL-----GGKQKFKTKVVK--NTLNPVWNET-FEFP-VLDPESDTLTVEVWDKD 71

                          90       100
                  ....*....|....*....|...
gi 704462060  758 G----KFIGHRVIPVTAVHSGYH 776
Cdd:cd00030    72 RfskdDFLGEVEIPLSELLDSGK 94
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 874-1124 8.37e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 8.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   874 ASLAELQQMKLFLKLVKKQEKELRELERKGSKRREELLqKYSVLFSEPVCYGGKKRMMHTRKTQKKRSLTTGDVgtgANP 953
Cdd:TIGR02169  174 KALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELLKEKEALERQKEAIERQL---ASL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   954 VEVAESIDSRVLELRERLEmDLLRLGEEQHDEVRRRKEQHATEQVTKITELarEKQAAELKALKEASESNIKDIK---KK 1030
Cdd:TIGR02169  250 EEELEKLTEEISELEKRLE-EIEQLLEELNKKIKDLGEEEQLRVKEKIGEL--EAEIASLERSIAEKERELEDAEerlAK 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1031 LEAKRvDRIQAMMRNTGDKAAQERLKKEinnsHIQEVVQTIKQVTEKTarcQQKLEEKQAENlRAIREKeiqlqqeaLAE 1110
Cdd:TIGR02169  327 LEAEI-DKLLAEIEELEREIEEERKRRD----KLTEEYAELKEELEDL---RAELEEVDKEF-AETRDE--------LKD 389

                          250
                   ....*....|....
gi 704462060  1111 HQEKLKSLTREAQE 1124
Cdd:TIGR02169  390 YREKLEKLKREINE 403
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 872-1122 9.11e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 46.89  E-value: 9.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   872 QTASLAELQQMKLFLKLVKKQEKELRELERKGSKRREELLQKYS----VLFSEPVCYGGKKRM-MHTRKTQKKRSLTTGD 946
Cdd:TIGR00618  248 KREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKaaplAAHIKAVTQIEQQAQrIHTELQSKMRSRAKLL 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   947 VGTGANPVEVAESIDSRVLELRERLEMDLLRLGEEQHDEVRRRKEQhATEQVTKITELAREKQAAELKalkEASESNIKD 1026
Cdd:TIGR00618  328 MKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ-QHTLTQHIHTLQQQKTTLTQK---LQSLCKELD 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1027 IKKKLEAKRVDRIQAMMRNTGDKAaqeRLKKEINNShiQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREKEIQLQQE 1106
Cdd:TIGR00618  404 ILQREQATIDTRTSAFRDLQGQLA---HAKKQQELQ--QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK 478

                          250
                   ....*....|....*.
gi 704462060  1107 ALAEHQEKLKSLTREA 1122
Cdd:TIGR00618  479 EQIHLQETRKKAVVLA 494
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 963-1121 9.35e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 9.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   963 RVLELRERLEmDLLRLGEEQHDEVRRRkEQHATEQVTKITELARE------------KQAAELKALKEASESNIKDIKKK 1030
Cdd:TIGR02169  675 ELQRLRERLE-GLKRELSSLQSELRRI-ENRLDELSQELSDASRKigeiekeieqleQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1031 LEAKRVD------RIQAMMRNTGD-KAAQERLKKEINNSHIQEVVQTIKQVTEKTARCQQKLEEKQAE-----NLRAIRE 1098
Cdd:TIGR02169  753 IENVKSElkeleaRIEELEEDLHKlEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKlnrltLEKEYLE 832

                          170       180
                   ....*....|....*....|...
gi 704462060  1099 KEIQLQQEALAEHQEKLKSLTRE 1121
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKE 855
DUF1154 pfam06631
Protein of unknown function (DUF1154); This family represents a small conserved region of ...
 875-913 1.04e-04

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


Pssm-ID: 461969  Cd Length: 45  Bit Score: 40.70  E-value: 1.04e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 704462060   875 SLAELQQMKLFLKLVKKQEKELRELERKGSKRReELLQK 913
Cdd:pfam06631    8 TLESLRQDKAYLKLLKKQQKELESLKKKHSKER-SAMQK 45
PTZ00121 PTZ00121
MAEBL; Provisional
 889-1162 1.07e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  889 VKKQEKELR--ELERKGSKRR--EELLQKYSVLFSEPVCYGGKKRMMHTRKTQKKRSlttGDVGTGANPVEVAESIDSRV 964
Cdd:PTZ00121 1235 AKKDAEEAKkaEEERNNEEIRkfEEARMAHFARRQAAIKAEEARKADELKKAEEKKK---ADEAKKAEEKKKADEAKKKA 1311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  965 LELRERLEMdllrlgEEQHDEVRRRKE--QHATEQVTKITELAREKQAAELKALKEASESNIKDIKKKLEAKRvdRIQAM 1042
Cdd:PTZ00121 1312 EEAKKADEA------KKKAEEAKKKADaaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK--KADAA 1383

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1043 MRNTGDKAAQERLKKEINNSHIQ-EVVQTIKQVTEKTARCQQKLEE--------KQAENLRAIREKEIQLQQEALAEHQE 1113
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEEDKKKaDELKKAAAAKKKADEAKKKAEEkkkadeakKKAEEAKKADEAKKKAEEAKKAEEAK 1463

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 704462060 1114 KLKSLTREAQETVKNFATAGFAGELgtPKAAGQSVPEGEQVRTGHVEEK 1162
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKADEA--KKKAEEAKKKADEAKKAAEAKK 1510
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
887-1124 1.15e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  887 KLVKKQEKELRELE--RKGSKRREELLQKYSVLfsepvcyggKKRMMHTRKTQKKRSLTTGDVGTGANPVEV----AESI 960
Cdd:PRK03918  266 ERIEELKKEIEELEekVKELKELKEKAEEYIKL---------SEFYEEYLDELREIEKRLSRLEEEINGIEErikeLEEK 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  961 DSRVLELRERLEMDLLRLGE-----EQHDEVRRRKEQhATEQVTKITELAREKQAAELKALKEASESNIKDIKKKLEAKR 1035
Cdd:PRK03918  337 EERLEELKKKLKELEKRLEEleerhELYEEAKAKKEE-LERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1036 vdriqammrntgdkaaqeRLKKEINNshIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREKEIQLQQEALAEHQEKL 1115
Cdd:PRK03918  416 ------------------ELKKEIKE--LKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKE 475


                  ....*....
gi 704462060 1116 KSLTREAQE 1124
Cdd:PRK03918  476 RKLRKELRE 484
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
 152-299 2.03e-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: 42.75  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  152 LVKLKMQLNAegKIPVRNIFQMF-PADRKRVEAALsachlpkgkndainpeDFPEtvYKTFLMNLCPRPEIDEIFTSHHL 230
Cdd:cd16205    22 ILQLMHKLNV--NLPRRKVRQMFkEADTDDNQGTL----------------DFEE--FCAFYKMMSTRRELYLLLLSYSN 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 704462060  231 KaKPYMTKEHLAKFINKKQRDSRLNDilfppakpEQVQSLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 299
Cdd:cd16205    82 K-KDYLTLEDLARFLEVEQKMTNVTL--------EYCLDIIEKFEPSEENKKNGLLGIDGFTNYMRSPA 141
PDCD7 pfam16021
Programmed cell death protein 7;
875-1100 2.51e-04

Programmed cell death protein 7;


Pssm-ID: 464979 [Multi-domain]  Cd Length: 305  Bit Score: 44.72  E-value: 2.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   875 SLAELQQ-MKLFLKLVKK---QEKELRELERKGS------KRREEL---LQKYSVLFSEPVCYGGKKRMMHTRktQKKRS 941
Cdd:pfam16021    2 SLSELRQaLYSAARLVSRletLCLELRENVEDDSvwsesySRAAELkheLQEKLLLLEDPELLESLKRKLERR--QKKRL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   942 lttgdvgtganpvevaesidsRVLELRERLEmdllrlgEEQHDEVRRRKEQHA---TEQVTKITELAREKQAAELKALKE 1018
Cdd:pfam16021   80 ---------------------RRKRRKEERK-------EEKKEEQERRAEREAkidKWRRKQIQEVEEKKRERELKLAAD 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1019 ASESNIKdiKKKLEAKR-VDRIQA----------MMRNTGDKAAQErlKKEINNSHIQEVVQTIKQVTEKTARCQQKL-- 1085
Cdd:pfam16021  132 AVLSEVR--KKQADAKRmLDILRSleklrklrkeAARRKGIKPESE--CDEAFESHLEKLRSVWKKRTEEYSAEEKALkv 207

                          250
                   ....*....|....*..
gi 704462060  1086 --EEKQAENLRAIREKE 1100
Cdd:pfam16021  208 mlEGEQEEERKRRREKR 224
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 957-1191 2.51e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  957 AESIDSRVLELRERLEmdllRLgEEQHDEVRRRKEQhATEQVTKITELAREKQAaELKALKEASESNIKDIKKK------ 1030
Cdd:COG3883    32 LEAAQAELDALQAELE----EL-NEEYNELQAELEA-LQAEIDKLQAEIAEAEA-EIEERREELGERARALYRSggsvsy 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1031 ----LEAK-------RVDRIQAMMRNTGD-----KAAQERL--KKEINNSHIQEVVQTIKQVTEKTARCQQKLEEKQA-- 1090
Cdd:COG3883   105 ldvlLGSEsfsdfldRLSALSKIADADADlleelKADKAELeaKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAll 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1091 ENLRAIREKEIQLQQEALAEHQEKLKSLTREAQETVKNFATAGFAGELGTPKAAGQSVPEGEQVRTGHVEEKTPVAEVSR 1170
Cdd:COG3883   185 AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264

                         250       260
                  ....*....|....*....|.
gi 704462060 1171 LTPALAEPPGAQTDTEVETSI 1191
Cdd:COG3883   265 AGAAAGAAGAGAAAASAAGGG 285
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
882-1127 2.77e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.52  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  882 MKLFLKLVKKQEKELRELERKGSKRREELLQKYSVLFSEPVCYGGKKRMM--HTRKTQKKRSlttgdvgtgANPVEVAES 959
Cdd:COG1340     6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELreEAQELREKRD---------ELNEKVKEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  960 IDSR------VLELRERL-----EMDLLRLGEEQHDEVRRRKEQHATEQVTKITELAREKQ--------AAELKALKEAS 1020
Cdd:COG1340    77 KEERdelnekLNELREELdelrkELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKElvekikelEKELEKAKKAL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1021 ESN--IKDIKKKLEAKR--VDRIQAMMRNTGDKAaqERLKKEinnshIQEVVQTIKQVTEKTARCQQKLEEKQAEnLRAI 1096
Cdd:COG1340   157 EKNekLKELRAELKELRkeAEEIHKKIKELAEEA--QELHEE-----MIELYKEADELRKEADELHKEIVEAQEK-ADEL 228

                         250       260       270
                  ....*....|....*....|....*....|.
gi 704462060 1097 REKEIQLQQEaLAEHQEKLKSLtREAQETVK 1127
Cdd:COG1340   229 HEEIIELQKE-LRELRKELKKL-RKKQRALK 257
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
888-1123 3.11e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  888 LVKKQEKELRELERKGSKRREELLQKYSVLFSEpvcyggkkrmmhtrktqkkrslttgdvgtganpVEVAESIDSRVLEL 967
Cdd:COG4717    47 LLERLEKEADELFKPQGRKPELNLKELKELEEE---------------------------------LKEAEEKEEEYAEL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  968 RERLEmdllRLgEEQHDEVRRRKEQHATEqvtkITELAREKQAAELKALKEASESNIKDIKKKLEA--KRVDRIQAMMRn 1045
Cdd:COG4717    94 QEELE----EL-EEELEELEAELEELREE----LEKLEKLLQLLPLYQELEALEAELAELPERLEEleERLEELRELEE- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1046 tgdkaAQERLKKEINNSHiQEVVQTIKQVTEKTARCQQKLEEK--QAENLRAIREKEIQLQQEALAEHQEKLKSLTREAQ 1123
Cdd:COG4717   164 -----ELEELEAELAELQ-EELEELLEQLSLATEEELQDLAEEleELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 960-1129 3.99e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.44  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  960 IDSRVLELRERLEMDLLRLGEEQHDEVRRrKEQHATEQVTKITEL------AR---EKQAAELK-ALKEASESNikdikK 1029
Cdd:PRK04778  254 IEKEIQDLKEQIDENLALLEELDLDEAEE-KNEEIQERIDQLYDIlerevkARkyvEKNSDTLPdFLEHAKEQN-----K 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1030 KLEAKrVDRIQAMMR-NTGDKAAQERLKKEINNshIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIreKEIQLQQEAL 1108
Cdd:PRK04778  328 ELKEE-IDRVKQSYTlNESELESVRQLEKQLES--LEKQYDEITERIAEQEIAYSELQEELEEILKQL--EEIEKEQEKL 402

                         170       180
                  ....*....|....*....|.
gi 704462060 1109 AEHQEKLKSLTREAQETVKNF 1129
Cdd:PRK04778  403 SEMLQGLRKDELEAREKLERY 423
PTZ00121 PTZ00121
MAEBL; Provisional
 891-1127 4.01e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  891 KQEKELRELERKGSKRREELLQKysvlfSEPVcyggKKRMMHTRKTQKKRSLTTGDVGTGANPVEVAESIDSRVLElrER 970
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKK-----AEEA----KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE--EA 1277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  971 LEMDLLRLGEE--QHDEVRRRKEQHATEQVTKITELARE-------------------KQAAELKALKEASESNIKDIKK 1029
Cdd:PTZ00121 1278 RKADELKKAEEkkKADEAKKAEEKKKADEAKKKAEEAKKadeakkkaeeakkkadaakKKAEEAKKAAEAAKAEAEAAAD 1357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1030 KLEAKRVDRIQAMMRNTGDKAAQERLKKEINNSHIQEVVQTIKQVTEKTARCQQKLEE--KQAENLRAiREKEIQLQQEA 1107
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAakKKADEAKK-KAEEKKKADEA 1436

                         250       260
                  ....*....|....*....|..
gi 704462060 1108 --LAEHQEKLKSLTREAQETVK 1127
Cdd:PTZ00121 1437 kkKAEEAKKADEAKKKAEEAKK 1458
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 966-1124 5.03e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.75  E-value: 5.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   966 ELRERLEMDLLR-LGEEQHDEVRRRKE--QHATEQVTKITELAREKQAAELKALKeasesnikdikkklEAKRVDRIQAM 1042
Cdd:pfam13868   44 RLDEMMEEERERaLEEEEEKEEERKEErkRYRQELEEQIEEREQKRQEEYEEKLQ--------------EREQMDEIVER 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1043 MRntgDKAAQERLKKEINNSHIQEVVQTIKQVTEKtARCQQKLEEKQAE-------NLRAIREKEIQLQQEALAEHQEKL 1115
Cdd:pfam13868  110 IQ---EEDQAEAEEKLEKQRQLREEIDEFNEEQAE-WKELEKEEEREEDerileylKEKAEREEEREAEREEIEEEKERE 185


                   ....*....
gi 704462060  1116 KSLTREAQE 1124
Cdd:pfam13868  186 IARLRAQQE 194
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 980-1122 5.15e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.68  E-value: 5.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   980 EEQHDEVRR-RKEQHATEQVTKItelAREKQAAELKALKEASESNIKDIKKKLEAKRvdriqammrntgDKAAQERLKKE 1058
Cdd:TIGR02794   49 AQQANRIQQqKKPAAKKEQERQK---KLEQQAEEAEKQRAAEQARQKELEQRAAAEK------------AAKQAEQAAKQ 113

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 704462060  1059 INNSHIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREKE--IQLQQEALAEHQEKLKSLTREA 1122
Cdd:TIGR02794  114 AEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEakAKAAAEAKKKAEEAKKKAEAEA 179
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 678-777 5.18e-04

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


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 41.41  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  678 VASTLSVTILSGQFLSDRSVK----TYVEVELFGlprdTKRKYRTKLTSTA-NSINPVWKeEAFVFEkimMP----ELAS 748
Cdd:cd00276    12 TAERLTVVVLKARNLPPSDGKglsdPYVKVSLLQ----GGKKLKKKKTSVKkGTLNPVFN-EAFSFD---VPaeqlEEVS 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 704462060  749 LKIVAWEEGGK----FIGHRVIPVTAVHSGYHH 777
Cdd:cd00276    84 LVITVVDKDSVgrneVIGQVVLGPDSGGEELEH 116
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 960-1129 8.25e-04

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 43.30  E-value: 8.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   960 IDSRVLELRERLEMDLLRLGEEQHDEVRRrKEQHATEQVTKITEL------AR---EKQAAELKALKEASESNIKDIKKK 1030
Cdd:pfam06160  235 VDKEIQQLEEQLEENLALLENLELDEAEE-ALEEIEERIDQLYDLlekevdAKkyvEKNLPEIEDYLEHAEEQNKELKEE 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1031 LEakRVDriQAMMRNTGDKAAQERLKKEINNshIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIreKEIQLQQEalaE 1110
Cdd:pfam06160  314 LE--RVQ--QSYTLNENELERVRGLEKQLEE--LEKRYDEIVERLEEKEVAYSELQEELEEILEQL--EEIEEEQE---E 382

                          170       180
                   ....*....|....*....|..
gi 704462060  1111 HQEKLKSLT---REAQETVKNF 1129
Cdd:pfam06160  383 FKESLQSLRkdeLEAREKLDEF 404
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
934-1114 8.50e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  934 RKTQKKRSLTTGDVGTGANPVEVAESIDSRVLELRERLEmdllRLgEEQHDEVRRRKEQHATEqvtkITELAREKQAAEL 1013
Cdd:COG4717    60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE----EL-EEELEELEAELEELREE----LEKLEKLLQLLPL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1014 KALKEASESNIKDIK---KKLEAKRVDRIQAMMRNTGDKAAQERLKKEINN----------SHIQEVVQTIKQVTEKTAR 1080
Cdd:COG4717   131 YQELEALEAELAELPerlEELEERLEELRELEEELEELEAELAELQEELEElleqlslateEELQDLAEELEELQQRLAE 210

                         170       180       190
                  ....*....|....*....|....*....|....
gi 704462060 1081 CQQKLEEKQAEnLRAIREKEIQLQQEALAEHQEK 1114
Cdd:COG4717   211 LEEELEEAQEE-LEELEEELEQLENELEAAALEE 243
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 957-1153 1.00e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.87  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  957 AESIDSRVLELRERL-EMDLLRLGEEQHDEVRRRKEQHATEQvTKITELAREKQAAELKALKEASESNIKDIKKKLEAKR 1035
Cdd:PRK09510   89 AEELQQKQAAEQERLkQLEKERLAAQEQKKQAEEAAKQAALK-QKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEA 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1036 VDRIQAMMRNtgdKAAQERlKKEINNSHIQEVVQTIKQVTEKTARCQQKLEEKQ-----AENLRAIREKEIQLQQEALAE 1110
Cdd:PRK09510  168 KKKAEAEAAK---KAAAEA-KKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKkaaaeAKAAAAKAAAEAKAAAEKAAA 243

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 704462060 1111 HQEKLKSLTREAQETVKNFATAGFAGElGTPKAAGQSVPEGEQ 1153
Cdd:PRK09510  244 AKAAEKAAAAKAAAEVDDLFGGLDSGK-NAPKTGGGAKGNGAQ 285
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 877-1139 1.04e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  877 AELQQMKLFLKLVKKQEK----ELRELERKGSKRREELlqkysvlfsepvcyggkkrmmhtRKTQKKRSLTTGDVGTGAN 952
Cdd:COG4942    34 QEIAELEKELAALKKEEKallkQLAALERRIAALARRI-----------------------RALEQELAALEAELAELEK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  953 PVEVAE-SIDSRVLELRERL----------EMDLLRLGEEQHDEVRRrkeQHATEQVTKitelAREKQAAELKALKEAse 1021
Cdd:COG4942    91 EIAELRaELEAQKEELAELLralyrlgrqpPLALLLSPEDFLDAVRR---LQYLKYLAP----ARREQAEELRADLAE-- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1022 snIKDIKKKLEAKRVDRIQAMMRNTGDKAAQERLKKEinnshiqevvqtikqvtektarcQQKLEEKQAENLRAIREKEI 1101
Cdd:COG4942   162 --LAALRAELEAERAELEALLAELEEERAALEALKAE-----------------------RQKLLARLEKELAELAAELA 216

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 704462060 1102 QLQQEAlAEHQEKLKSLTREAQETVKNFATAGFAGELG 1139
Cdd:COG4942   217 ELQQEA-EELEALIARLEAEAAAAAERTPAAGFAALKG 253
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 872-1125 1.17e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   872 QTASLAEL-QQMKLFLKLVKKQEKELRELERKGSKRREELLQKYSVLFSepvcyggKKRMMHTRKTQKKRSLTTGDVGTg 950
Cdd:TIGR02168  675 RRREIEELeEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-------LSRQISALRKDLARLEAEVEQLE- 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   951 anpvEVAESIDSRVLELRERLEMDLLRLGEEQHDEVRRRKE--------QHATEQVTKITELAREKQAaELKALKEA--- 1019
Cdd:TIGR02168  747 ----ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieeleaqiEQLKEELKALREALDELRA-ELTLLNEEaan 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1020 -------SESNIKDIKKKLE--AKRVDRIQAMMrnTGDKAAQERLKKEINNSHIQ-EVVQTIKQVTEKTARCQQKLEEKQ 1089
Cdd:TIGR02168  822 lrerlesLERRIAATERRLEdlEEQIEELSEDI--ESLAAEIEELEELIEELESElEALLNERASLEEALALLRSELEEL 899

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 704462060  1090 AENLRAIREKEIQLQQEaLAEHQEKLKSLTREAQET 1125
Cdd:TIGR02168  900 SEELRELESKRSELRRE-LEELREKLAQLELRLEGL 934
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
968-1132 1.17e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  968 RERLEM--DLLRLGE-EQHDE--------VRR--RKEQHATEQVTKITElarEKQAAELKALKEASESNIKDIKKKLEAK 1034
Cdd:PRK02224  149 SDRQDMidDLLQLGKlEEYRErasdarlgVERvlSDQRGSLDQLKAQIE---EKEEKDLHERLNGLESELAELDEEIERY 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1035 RVDRIQAmmRNTGDkAAQERLKK-EINNSHIQEVVQTIKQVTEKTARCQQKLEE--KQAENLRAIREK---EIQ------ 1102
Cdd:PRK02224  226 EEQREQA--RETRD-EADEVLEEhEERREELETLEAEIEDLRETIAETEREREElaEEVRDLRERLEEleeERDdllaea 302

                         170       180       190
                  ....*....|....*....|....*....|....
gi 704462060 1103 ----LQQEALAEHQEKLKSLTREAQETVKNFATA 1132
Cdd:PRK02224  303 glddADAEAVEARREELEDRDEELRDRLEECRVA 336
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 981-1124 1.42e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   981 EQHDEVRRRKEQHATEQVTKItelaREKQAAElkalkeasesniKDIKKKLEAKRVDRIQAMMRNTGDKAAQERLKKEI- 1059
Cdd:pfam13868    3 ENSDELRELNSKLLAAKCNKE----RDAQIAE------------KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEe 66

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 704462060  1060 -NNSHIQEVVQTIKQVTEKTARCQQKLEEKQAENlRAIREKEIQLQQEALAEHQEKLKSLTREAQE 1124
Cdd:pfam13868   67 rKEERKRYRQELEEQIEEREQKRQEEYEEKLQER-EQMDEIVERIQEEDQAEAEEKLEKQRQLREE 131
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
987-1191 1.46e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 42.72  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  987 RRRKEQHATEQVTKITELAREKQAAELKALKEASESNIKDIKKKLEA-KRVDRIQAMMRNTGDKAAQERLKKEINNSHIQ 1065
Cdd:COG3064     7 EKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAeEEAREAKAEAEQRAAELAAEAAKKLAEAEKAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1066 EVVQtiKQVTEKTARcqqklEEKQAENLRAIREKEIQLQQEALAEHQEKL-KSLTREAQETVKNFATAGFAGELGTPKAA 1144
Cdd:COG3064    87 AEAE--KKAAAEKAK-----AAKEAEAAAAAEKAAAAAEKEKAEEAKRKAeEEAKRKAEEERKAAEAEAAAKAEAEAARA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 704462060 1145 GQSVPEGEQVRTGHVEEKTPVAEVSRLTPALAEPPGAQTDTEVETSI 1191
Cdd:COG3064   160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAA 206
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 889-1161 1.56e-03

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: 42.82  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   889 VKKQEKELRELERKGSKRREELLQKYSvlfsEPVCYGGKKRMMHTRKTQKKRSLTTGDVGTGANPVEVaESIDSRVLELR 968
Cdd:pfam09731  144 ATAVAKEAKDDAIQAVKAHTDSLKEAS----DTAEISREKATDSALQKAEALAEKLKEVINLAKQSEE-EAAPPLLDAAP 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   969 ERLEMDLLRLGEEQHDEVRRRKEQHATEQVTKITELAREKQAAELKALKEASESNIKDIKKKLEAK----------RVDR 1038
Cdd:pfam09731  219 ETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDlnsliahahrEIDQ 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1039 IQ---AMMRNTGDKAAQERLKKEINNSHIQEVvQTIKQVTEKTARCQQKLEEKQAENLRAIREK---EIQLQQEALAE-H 1111
Cdd:pfam09731  299 LSkklAELKKREEKHIERALEKQKEELDKLAE-ELSARLEEVRAADEAQLRLEFEREREEIRESyeeKLRTELERQAEaH 377

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 704462060  1112 QEKLKS--------LTREAQETVKNFATAGFAGELGTPKAAGQSVPEGEQVRTGHVEE 1161
Cdd:pfam09731  378 EEHLKDvlveqeieLQREFLQDIKEKVEEERAGRLLKLNELLANLKGLEKATSSHSEV 435
growth_prot_Scy NF041483
polarized growth protein Scy;
957-1058 2.41e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  957 AESIDSRVLELRERLEMDLlrlgEEQHDEVRRRK-EQ--HATEQVTKITELAREKQA-AELKALKEASESNIKDIKKKLE 1032
Cdd:NF041483 1116 ATAIRERAEELRDRITGEI----EELHERARRESaEQmkSAGERCDALVKAAEEQLAeAEAKAKELVSDANSEASKVRIA 1191

                          90       100       110
                  ....*....|....*....|....*....|.
gi 704462060 1033 AkrVDRIQAMMRNTGDKAAQ-----ERLKKE 1058
Cdd:NF041483 1192 A--VKKAEGLLKEAEQKKAElvreaEKIKAE 1220
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1039-1124 2.73e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1039 IQAMMRNTGDKAAQERLKK-----EINNSHIQEVVQTIKQVTEKTARCQQKLEEKQA--ENLRAIREKEIQLQQE-ALAE 1110
Cdd:COG4717    43 IRAMLLERLEKEADELFKPqgrkpELNLKELKELEEELKEAEEKEEEYAELQEELEEleEELEELEAELEELREElEKLE 122

                          90
                  ....*....|....
gi 704462060 1111 HQEKLKSLTREAQE 1124
Cdd:COG4717   123 KLLQLLPLYQELEA 136
PRK12704 PRK12704
phosphodiesterase; Provisional
 1004-1127 3.14e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1004 LAREKQAAELKALKEASESNIKDIKKKLEAKRVDRIQAmmrntgdkaAQERLKKeINNSHIQEVVQTIKQVTEKTARCQQ 1083
Cdd:PRK12704   24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLE---------AKEEIHK-LRNEFEKELRERRNELQKLEKRLLQ 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 704462060 1084 KLE--EKQAENLRAiREKEIQLQQEALAEHQEKLKSLTREAQETVK 1127
Cdd:PRK12704   94 KEEnlDRKLELLEK-REEELEKKEKELEQKQQELEKKEEELEELIE 138
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
973-1123 3.18e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  973 MDLLRLGEEQHDEVRRRKEQHATEQV-TKITELAREKQAAELKALKEASEsnIKDIKKKLEAkRVDRIQAMMRNTGD--K 1049
Cdd:COG4717   343 LDRIEELQELLREAEELEEELQLEELeQEIAALLAEAGVEDEEELRAALE--QAEEYQELKE-ELEELEEQLEELLGelE 419

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 704462060 1050 AAQERLKKEINNSHIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREKEIQLQQEALAEHQEKLKSLTREAQ 1123
Cdd:COG4717   420 ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWA 493
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 957-1130 3.19e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.48  E-value: 3.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   957 AESIDSRVLEL----RERLEMDllRLGEEQHDEVRRRKEQHATEQVTKITELAREKQAAELKALKEASESNIKDIKKKLE 1032
Cdd:pfam15709  340 AERAEMRRLEVerkrREQEEQR--RLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAA 417

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1033 AKRVDRIQAMMRNTGDKAAQERLKKEINNSHIQEvvQTIKQVTEKTARCQQKL----EEKQAENLRAIREKEIQLQQEAl 1108
Cdd:pfam15709  418 QERARQQQEEFRRKLQELQRKKQQEEAERAEAEK--QRQKELEMQLAEEQKRLmemaEEERLEYQRQKQEAEEKARLEA- 494

                          170       180
                   ....*....|....*....|..
gi 704462060  1109 AEHQEKLKSLTREAQETVKNFA 1130
Cdd:pfam15709  495 EERRQKEEEAARLALEEAMKQA 516
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 877-1116 3.30e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.96  E-value: 3.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   877 AELQQ----MKLFLKLVKKQEKELRELERKGSKRREELLQKYSVLFSEpvCYGGKKRMMHTRktQKKRSLTTgDVGTGAN 952
Cdd:TIGR00606  691 AELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI--IDLKEKEIPELR--NKLQKVNR-DIQRLKN 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   953 PVEVAESIDSRV---LELRERLEMD--LLRLGEEQHDEVRRRKEQHATE--------QVTKITELAREKQ---------A 1010
Cdd:TIGR00606  766 DIEEQETLLGTImpeEESAKVCLTDvtIMERFQMELKDVERKIAQQAAKlqgsdldrTVQQVNQEKQEKQheldtvvskI 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1011 AELKALKEASESNIKDIKKKLEAKRVDRIQAMMRNTGDKAAQERLKKEInnSHIQEVVQTIKQVTEKTARCQQKLEEKQA 1090
Cdd:TIGR00606  846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS--TEVQSLIREIKDAKEQDSPLETFLEKDQQ 923

                          250       260
                   ....*....|....*....|....*...
gi 704462060  1091 ENLRAIREKEI--QLQQEALAEHQEKLK 1116
Cdd:TIGR00606  924 EKEELISSKETsnKKAQDKVNDIKEKVK 951
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 877-1128 3.31e-03

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: 41.55  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   877 AELQQMKLfLKLVKKQEKELR-------ELERKGSKRREELLQKYSVLFSEPVCYGGKKRMMHTRKTQKKrSLTTGDVGT 949
Cdd:pfam05667  238 EEYRKRKR-TKLLKRIAEQLRsaalagtEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKL-QFTNEAPAA 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   950 GANPVEVAESIDsrvlELRERLEMDLLRLgEEQHDEVRRRKEQHATE------QVTKITELAREKQA------------- 1010
Cdd:pfam05667  316 TSSPPTKVETEE----ELQQQREEELEEL-QEQLEDLESSIQELEKEikklesSIKQVEEELEELKEqneelekqykvkk 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1011 -------------AELKALKEASESNIKDIKKKLEAKRVDRIQAMmrntgdkaaqERLKKEInnshiqevvqtikqvTEK 1077
Cdd:pfam05667  391 ktldllpdaeeniAKLQALVDASAQRLVELAGQWEKHRVPLIEEY----------RALKEAK---------------SNK 445

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 704462060  1078 TARCQQKLEEkqaenLRAIREK------EIQLQQEALAEHQEKLKSLTREAQ---------ETVKN 1128
Cdd:pfam05667  446 EDESQRKLEE-----IKELREKikevaeEAKQKEELYKQLVAEYERLPKDVSrsaytrrilEIVKN 506
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 958-1099 3.34e-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: 39.94  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   958 ESIDSRVLELRERLEmdllrlgeEQHDEVRRRKEQHATE---QVTKITELAREKQAAELKALKEASESNIKDIKKKLEAk 1034
Cdd:pfam01442   40 ERLQKDLEEVRAKLE--------PYLEELQAKLGQNVEElrqRLEPYTEELRKRLNADAEELQEKLAPYGEELRERLEQ- 110

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 704462060  1035 RVDRIQAMMRNTGDKaAQERLKKEINNSHiQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREK 1099
Cdd:pfam01442  111 NVDALRARLAPYAEE-LRQKLAERLEELK-ESLAPYAEEVQAQLSQRLQELREKLEPQAEDLREK 173
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 963-1145 3.56e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   963 RVLELRERLEMDLLRLGEEQHDEVRRRKEQHATEqvtkitelAREKQAAELKALKEAsesnIKDIKKKLEAKRvdriqam 1042
Cdd:TIGR02794   90 RQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE--------AKAKQAAEAKAKAEA----EAERKAKEEAAK------- 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1043 mrntgdKAAQERLKKEINNSHIQEVVQTIKQVTE----KTARCQQKLEEKQAENLRAIREKEIQLQQEALAEHQEKLKSL 1118
Cdd:TIGR02794  151 ------QAEEEAKAKAAAEAKKKAEEAKKKAEAEakakAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAE 224

                          170       180
                   ....*....|....*....|....*..
gi 704462060  1119 TREAQETVKNFATAGFAGELGTPKAAG 1145
Cdd:TIGR02794  225 AERKADEAELGDIFGLASGSNAEKQGG 251
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 955-1086 3.74e-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: 3.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   955 EVAESIDSRVLELRERLEmdllRLGEEQHDEVRRRKEQhATEQVTKITELAREKQAAELKALKEASESNIKDIKKKLEAk 1034
Cdd:pfam01442   59 ELQAKLGQNVEELRQRLE----PYTEELRKRLNADAEE-LQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAE- 132

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 704462060  1035 RVDRIQAMMRNTGDkAAQERLkkeinNSHIQEVVQtikQVTEKTARCQQKLE 1086
Cdd:pfam01442  133 RLEELKESLAPYAE-EVQAQL-----SQRLQELRE---KLEPQAEDLREKLD 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 957-1128 3.78e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   957 AESIDSRVLELRERLEmdllRLGEEQHDeVRRRKEQHATEQVTKITELAR-EKQAAELKALKEASESNIKDIKKKLEA-- 1033
Cdd:TIGR02168  798 LKALREALDELRAELT----LLNEEAAN-LRERLESLERRIAATERRLEDlEEQIEELSEDIESLAAEIEELEELIEEle 872

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1034 KRVDRIQAMMRNTGDKAAQERLKKEINNSHIQEVVQTIKQVTEKTARCQQKLEE----------KQAENLRAIREKEiQL 1103
Cdd:TIGR02168  873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQlelrleglevRIDNLQERLSEEY-SL 951

                          170       180
                   ....*....|....*....|....*
gi 704462060  1104 QQEALAEHQEKLKSLTREAQETVKN 1128
Cdd:TIGR02168  952 TLEEAEALENKIEDDEEEARRRLKR 976
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1049-1125 3.96e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 3.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 704462060 1049 KAAQERLKKEINNSHiqevvQTIKQVTEKTARCQQKLEEKQAEnLRAIrEKEIQLQQEALAEHQEKLKSLTREAQET 1125
Cdd:COG3883    29 QAELEAAQAELDALQ-----AELEELNEEYNELQAELEALQAE-IDKL-QAEIAEAEAEIEERREELGERARALYRS 98
PTZ00121 PTZ00121
MAEBL; Provisional
 890-1092 4.55e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  890 KKQEKELRELERKGSKRREELlqkysvlfsepvcyggKKRMMHTRKTQKKRSLTTGDVGTGANPVEVAESIDSRVLELRE 969
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEAL----------------KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  970 RLEMDLLRLGEEQHDEVRRRKEQH-ATEQVTKITELAREKQAAELKALKEASESNIKDIKKKLEAKRvDRIQAMMRNTGD 1048
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKIAHlKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF-DNFANIIEGGKE 1816

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 704462060 1049 KAAQERLKKEINNSHIQEVVQTIKQVTEKTARCQQKLEEKQAEN 1092
Cdd:PTZ00121 1817 GNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNEN 1860
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 886-1124 5.00e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.79  E-value: 5.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   886 LKLVK-KQEKELRELERKGSKRREELLQKYSvlfsepvcyggKKRMMHTRKTQKkrslttgdvgtganpvEVAESIDSRV 964
Cdd:pfam15558   12 LMLARhKEEQRMRELQQQAALAWEELRRRDQ-----------KRQETLERERRL----------------LLQQSQEQWQ 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   965 LELRERLEmdllRLGEEQHdEVRRRKEQHATEQVTKITELAREKQ----------AAELKALKEASESNIKDIKKKLEAK 1034
Cdd:pfam15558   65 AEKEQRKA----RLGREER-RRADRREKQVIEKESRWREQAEDQEnqrqekleraRQEAEQRKQCQEQRLKEKEEELQAL 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1035 RVDRIQAMMRNTgDKAAQERLK------KEINNSHIQEVV--QTIKQVTEKTARC-------------------QQKLEE 1087
Cdd:pfam15558  140 REQNSLQLQERL-EEACHKRQLkereeqKKVQENNLSELLnhQARKVLVDCQAKAeellrrlsleqslqrsqenYEQLVE 218

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 704462060  1088 KQAENLRA-IREKEIQLQQ------EALAEHQEKLKSLTREAQE 1124
Cdd:pfam15558  219 ERHRELREkAQKEEEQFQRakwraeEKEEERQEHKEALAELADR 262
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
998-1124 5.15e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.63  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  998 VTKITELAREKQAAELKALKEASesnIKdIKKKLEAKRVDRIQAMMRNTGDKAAQErlkkeinNSHIQEVVQTIKQVTEK 1077
Cdd:COG2268   191 RRKIAEIIRDARIAEAEAERETE---IA-IAQANREAEEAELEQEREIETARIAEA-------EAELAKKKAEERREAET 259

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 704462060 1078 T-ARCQQKLEEKQAENLRAI--------REKEIQLQQEALAEHQEKLKSLTREAQE 1124
Cdd:COG2268   260 ArAEAEAAYEIAEANAEREVqrqleiaeREREIELQEKEAEREEAELEADVRKPAE 315
PH_PLC_ELMO1 cd01248
Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain; The ...
 17-88 5.19e-03

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


Pssm-ID: 269952  Cd Length: 108  Bit Score: 37.69  E-value: 5.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 704462060   17 LSKGERFIKWDdETASASPVILRVDPKGFYLYWTDQNKEME--ILDITSIRDTRVGRFAKIPKCQKLREVFNLD 88
Cdd:cd01248     1 LQQGTLLLKYR-EGSKPKERTFYLDPDGTRITWESSKKKSEkkSIDISDIKEIRPGKDTDGFKRKKKSNKPKEE 73
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 1055-1129 5.42e-03

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 40.39  E-value: 5.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1055 LKKEINNSHIQEVVQTIKQVTEKTARCQQKLEEKQ--AENLRAIREKEIQLQQEaLAEHQEKL---KSLTREAQETVKNF 1129
Cdd:pfam04849  228 RKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEelQQHLQASKEAQRQLTSE-LQELQDRYaecLGMLHEAQEELKEL 306
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 966-1125 5.55e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.41  E-value: 5.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   966 ELRERLEMDLLRLGEEQHDEVRRRKEQHATEQVTKITELAREKQAAELKALKEA--SESNIKDIKKKLEAKRVDRIQamm 1043
Cdd:pfam15558   36 ELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVieKESRWREQAEDQENQRQEKLE--- 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1044 rntgDKAAQERLKKeinnshiqevvqtikqvtektaRCQ-QKLEEKQAEnLRAIREKEIQLQQEAL--AEHQEKLKS--L 1118
Cdd:pfam15558  113 ----RARQEAEQRK----------------------QCQeQRLKEKEEE-LQALREQNSLQLQERLeeACHKRQLKEreE 165


                   ....*..
gi 704462060  1119 TREAQET 1125
Cdd:pfam15558  166 QKKVQEN 172
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 966-1124 5.83e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  966 ELRERLEMDLLRLGEEQHDEVRRRKEQHATEQvtKITELAR-----EKQAAELKALKEASESNIKDIKKKLEAKRvDRIQ 1040
Cdd:COG4942    31 QLQQEIAELEKELAALKKEEKALLKQLAALER--RIAALARriralEQELAALEAELAELEKEIAELRAELEAQK-EELA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1041 AMMRNTGDKAAQERLKKEINNSHIQEVV---QTIKQVTEktARcqqkleEKQAENLRAIREkEIQLQQEALAEHQEKLKS 1117
Cdd:COG4942   108 ELLRALYRLGRQPPLALLLSPEDFLDAVrrlQYLKYLAP--AR------REQAEELRADLA-ELAALRAELEAERAELEA 178


                  ....*..
gi 704462060 1118 LTREAQE 1124
Cdd:COG4942   179 LLAELEE 185
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 981-1128 6.24e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 39.35  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  981 EQHDEVRRRKEQHAtEQVTKITELAREkqaaelkaLKEASESNIKDIKKKLEA--KRVDRIQAMMrntgdKAAQERLKKE 1058
Cdd:cd00176    40 KKHEALEAELAAHE-ERVEALNELGEQ--------LIEEGHPDAEEIQERLEElnQRWEELRELA-----EERRQRLEEA 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704462060 1059 IN-NSHIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREKEIQLQQEaLAEHQEKLKSLTREAQETVKN 1128
Cdd:cd00176   106 LDlQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEE-LEAHEPRLKSLNELAEELLEE 175
PTZ00121 PTZ00121
MAEBL; Provisional
 980-1170 6.76e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  980 EEQHDEVRRRKE--QHATEQVTKITEL----AREKQAAELKalKEASESNIKD-IKKKLEAKRvdRIQAMMRNTGDKAAQ 1052
Cdd:PTZ00121 1384 KKKAEEKKKADEakKKAEEDKKKADELkkaaAAKKKADEAK--KKAEEKKKADeAKKKAEEAK--KADEAKKKAEEAKKA 1459

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060 1053 ERLKKEINNSHIQEVVQTIKQVTEKTARCQQKLEE--KQAENLRAIREKEIQLQQEALAEHQEKLKSLtREAQETVKnfa 1130
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEakKKADEAKKAAEAKKKADEAKKAEEAKKADEA-KKAEEAKK--- 1535

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 704462060 1131 tagfAGEL--GTPKAAGQSVPEGEQVRTGhvEEKTPVAEVSR 1170
Cdd:PTZ00121 1536 ----ADEAkkAEEKKKADELKKAEELKKA--EEKKKAEEAKK 1571
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 953-1128 7.73e-03

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


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 40.43  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   953 PVEVAESIDS----RVLELRERLEMDLlrlgeeqhDEVRRRKEQhATEQVTKITELAREKQA-----AELKALKEASESN 1023
Cdd:pfam13166  266 PAERKAALEAhfddEFTEFQNRLQKLI--------EKVESAISS-LLAQLPAVSDLASLLSAfeldvEDIESEAEVLNSQ 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1024 IKDIKKKLEAKRVDRIQAmmrntgdkAAQERLKKEINNshIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREKEIQL 1103
Cdd:pfam13166  337 LDGLRRALEAKRKDPFKS--------IELDSVDAKIES--INDLVASINELIAKHNEITDNFEEEKNKAKKKLRLHLVEE 406

                          170       180
                   ....*....|....*....|....*
gi 704462060  1104 QQEALAEHQEKLKSLTREAQETVKN 1128
Cdd:pfam13166  407 FKSEIDEYKDKYAGLEKAINSLEKE 431
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 873-1124 7.90e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 7.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   873 TASLAELQQMKLFLKLVKKQ---------EKELRELERKGSKRREELLQKYSVLfsepvcyggkKRMMHTRKTQKKRslt 943
Cdd:pfam13868   25 DAQIAEKKRIKAEEKEEERRldemmeeerERALEEEEEKEEERKEERKRYRQEL----------EEQIEEREQKRQE--- 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   944 tgdvgtganpvevaesidSRVLELRERLEMDLL---RLGEEQHDEVRRRKEQHAT-EQVTKITELAREKQAAELKALKEA 1019
Cdd:pfam13868   92 ------------------EYEEKLQEREQMDEIverIQEEDQAEAEEKLEKQRQLrEEIDEFNEEQAEWKELEKEEEREE 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1020 SESNIKDIKKKleAKRVDRIQAMMRNtgDKAAQERLKKEInnSHIQEVVQTIKQVTEK--TARCQQKLEEKQAENLRAIR 1097
Cdd:pfam13868  154 DERILEYLKEK--AEREEEREAEREE--IEEEKEREIARL--RAQQEKAQDEKAERDElrAKLYQEEQERKERQKEREEA 227

                          250       260       270
                   ....*....|....*....|....*....|.
gi 704462060  1098 EKEIQLQQEALAEHQE----KLKSLTREAQE 1124
Cdd:pfam13868  228 EKKARQRQELQQAREEqielKERRLAEEAER 258
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 889-1131 8.61e-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: 8.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   889 VKKQEKELRELERKGSKRREELLQKYSVLFSEPVCYGGKKRMMHTRKTQKkRSLTTgdvgTGANPVEVAESIDSRV---- 964
Cdd:TIGR04523  344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-NDLES----KIQNQEKLNQQKDEQIkklq 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   965 --LELRERLEMDLLRLGEEQHDEVRRRKEQ-HATEQVTKITELAREKQAAELKALK---EASESNIKDIKKKLEAKrVDR 1038
Cdd:TIGR04523  419 qeKELLEKEIERLKETIIKNNSEIKDLTNQdSVKELIIKNLDNTRESLETQLKVLSrsiNKIKQNLEQKQKELKSK-EKE 497

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1039 IQAMMRNTGD-KAAQERLKKEIN--NSHIQEVVQTIKQVTEKTARCQQKLEEKQAENLRAIREKEIQLQQ---EALAEHQ 1112
Cdd:TIGR04523  498 LKKLNEEKKElEEKVKDLTKKISslKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNkeiEELKQTQ 577

                          250
                   ....*....|....*....
gi 704462060  1113 EKLKSLTREAQETVKNFAT 1131
Cdd:TIGR04523  578 KSLKKKQEEKQELIDQKEK 596
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1009-1124 8.93e-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: 39.88  E-value: 8.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060  1009 QAAELKALKEASESNIKDIKKKLEAKRVDRIQAMMRNTGDKAAQERLKKEINnSHIQEVVQTIKQVTEKTARCQQKLEEK 1088
Cdd:pfam07888   28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELE-SRVAELKEELRQSREKHEELEEKYKEL 106

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 704462060  1089 QAENLRAIREKEIQLQQEA-----LAEHQEKLKSLTREAQE 1124
Cdd:pfam07888  107 SASSEELSEEKDALLAQRAahearIRELEEDIKTLTQRVLE 147
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1014-1132 9.55e-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: 9.55e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704462060   1014 KALKEASEsnIKDIKKKLEAKRVDRIQAMmrntgdKAAQERLKKEINNSHIQEVVQTIKQVTEKtarcQQKLEEKQaenl 1093
Cdd:smart00935    8 KILQESPA--GKAAQKQLEKEFKKRQAEL------EKLEKELQKLKEKLQKDAATLSEAAREKK----EKELQKKV---- 71

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 704462060   1094 RAIREKEIQLQQEALAEHQEKLKSLTREAQETVKNFATA 1132
Cdd:smart00935   72 QEFQRKQQKLQQDLQKRQQEELQKILDKINKAIKEVAKK 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH