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Conserved domains on  [gi|240256448|ref|NP_200529|]
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phosphatidylserine decarboxylase 2 [Arabidopsis thaliana]

Protein Classification

PLN02964 family protein (domain architecture ID 11477332)

PLN02964 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02964 PLN02964
phosphatidylserine decarboxylase
1-634 0e+00

phosphatidylserine decarboxylase


:

Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 1307.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448   1 MGNGNSREAKESRRSRLRHKLQKFRIHRRHLRSSRN-SAGMVIQRTVSAEDFSGIALLTLIGAEMKFKDKWLACVSFGEQ 79
Cdd:PLN02964   1 MGNGNSREAKESRRSKLRQKLQKFRIRRRHLRCSRGsSSGSVSQRAVSAEDFSGIALLTLVGAEMKFKDKWLACVSFGEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448  80 TFRTEISDTTQKPIWNSEKKLLLEKNGPSLARVSVFETNRVARNKIIGYCELDIFDFVVQEPESTCKSFNLLDPTSSN-V 158
Cdd:PLN02964  81 TFRTETSDSTDKPVWNSEKKLLLEKNGPHLARISVFETNRLSKNTLVGYCELDLFDFVTQEPESACESFDLLDPSSSNkV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 159 VGSIFLSCAIEDPVETERRFAKRILSIVDYNEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAAL 238
Cdd:PLN02964 161 VGSIFVSCSIEDPVETERSFARRILAIVDYDEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 239 LALQQEQEPIINNCPVCGEALQVSDKLNAMIHMTLCFDEGTGNQVMTGGFLTDRQASYGWMFKLSEWTHLSTYDVGLNTG 318
Cdd:PLN02964 241 LALQQEQEPIINNCPVCGEALGVSDKLNAMIHMTLCFDEGTGNQVMTGGFLTDKQASYGWMFKLSEWAHLSTYDVGLNTG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 319 SSASYIVVIDRKSKRLVEELIDSKIVLSMRAIYQSKIGLRLMDQGAKEILQRLSEKQGKKMSSVESAQKIPRFLEFFKDQ 398
Cdd:PLN02964 321 SSASHILVFDRKSKRLVEELIDSKIVLSMRAIYQSKIGLRLMDQGAKEILQRLSEKQGKKMNSVESAQDIPKFLEFFKDQ 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 399 INMAEVKYPLQHFKTFNEFFIRELKPGARPIACMNRNDVAVCAADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGKNVNPN 478
Cdd:PLN02964 401 INMDEVKYPLEHFKTFNEFFIRELKPGARPIACMDNDDVAVCAADCRLMAFQSVDDSTRFWIKGRKFSIKGLLGKKVHSD 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 479 AFLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNSKYCNVFTENKRTVAIISTAEFGKVAFVAIGAT 558
Cdd:PLN02964 481 AFLDGSLVIFRLAPQDYHRFHVPVSGVIEKFVDVPGSLYTVNPIAVNSKYCNVFTENKRAVCIISTAEFGKVAFVAIGAT 560
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256448 559 MVGSINFVRKEGEHVKKGDELGYFSFGGSTVICVFEKDAIGIDNDLLVNSGRSLETLVSVGMQLGVSTRTFARSTL 634
Cdd:PLN02964 561 MVGSITFVKKEGDHVKKGDELGYFSFGGSTVICVFEKDAIDIDEDLLANSERSLETLVSVGMTLGVSTRTFARQVL 636
 
Name Accession Description Interval E-value
PLN02964 PLN02964
phosphatidylserine decarboxylase
1-634 0e+00

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 1307.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448   1 MGNGNSREAKESRRSRLRHKLQKFRIHRRHLRSSRN-SAGMVIQRTVSAEDFSGIALLTLIGAEMKFKDKWLACVSFGEQ 79
Cdd:PLN02964   1 MGNGNSREAKESRRSKLRQKLQKFRIRRRHLRCSRGsSSGSVSQRAVSAEDFSGIALLTLVGAEMKFKDKWLACVSFGEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448  80 TFRTEISDTTQKPIWNSEKKLLLEKNGPSLARVSVFETNRVARNKIIGYCELDIFDFVVQEPESTCKSFNLLDPTSSN-V 158
Cdd:PLN02964  81 TFRTETSDSTDKPVWNSEKKLLLEKNGPHLARISVFETNRLSKNTLVGYCELDLFDFVTQEPESACESFDLLDPSSSNkV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 159 VGSIFLSCAIEDPVETERRFAKRILSIVDYNEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAAL 238
Cdd:PLN02964 161 VGSIFVSCSIEDPVETERSFARRILAIVDYDEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 239 LALQQEQEPIINNCPVCGEALQVSDKLNAMIHMTLCFDEGTGNQVMTGGFLTDRQASYGWMFKLSEWTHLSTYDVGLNTG 318
Cdd:PLN02964 241 LALQQEQEPIINNCPVCGEALGVSDKLNAMIHMTLCFDEGTGNQVMTGGFLTDKQASYGWMFKLSEWAHLSTYDVGLNTG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 319 SSASYIVVIDRKSKRLVEELIDSKIVLSMRAIYQSKIGLRLMDQGAKEILQRLSEKQGKKMSSVESAQKIPRFLEFFKDQ 398
Cdd:PLN02964 321 SSASHILVFDRKSKRLVEELIDSKIVLSMRAIYQSKIGLRLMDQGAKEILQRLSEKQGKKMNSVESAQDIPKFLEFFKDQ 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 399 INMAEVKYPLQHFKTFNEFFIRELKPGARPIACMNRNDVAVCAADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGKNVNPN 478
Cdd:PLN02964 401 INMDEVKYPLEHFKTFNEFFIRELKPGARPIACMDNDDVAVCAADCRLMAFQSVDDSTRFWIKGRKFSIKGLLGKKVHSD 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 479 AFLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNSKYCNVFTENKRTVAIISTAEFGKVAFVAIGAT 558
Cdd:PLN02964 481 AFLDGSLVIFRLAPQDYHRFHVPVSGVIEKFVDVPGSLYTVNPIAVNSKYCNVFTENKRAVCIISTAEFGKVAFVAIGAT 560
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256448 559 MVGSINFVRKEGEHVKKGDELGYFSFGGSTVICVFEKDAIGIDNDLLVNSGRSLETLVSVGMQLGVSTRTFARSTL 634
Cdd:PLN02964 561 MVGSITFVKKEGDHVKKGDELGYFSFGGSTVICVFEKDAIDIDEDLLANSERSLETLVSVGMTLGVSTRTFARQVL 636
PS_Dcarbxylase pfam02666
Phosphatidylserine decarboxylase; This is a family of phosphatidylserine decarboxylases, EC:4. ...
414-623 6.24e-65

Phosphatidylserine decarboxylase; This is a family of phosphatidylserine decarboxylases, EC:4.1.1.65. These enzymes catalyze the reaction: Phosphatidyl-L-serine <=> phosphatidylethanolamine + CO2. Phosphatidylserine decarboxylase plays a central role in the biosynthesis of aminophospholipids by converting phosphatidylserine to phosphatidylethanolamine.


Pssm-ID: 308345 [Multi-domain]  Cd Length: 198  Bit Score: 211.75  E-value: 6.24e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448  414 FNEFFIRELKPGARPIAcmNRNDVAVCAADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGKNVnPNAFLDGSLVIFRLAPQ 493
Cdd:pfam02666   1 LNAFFTRFLRDPARPIP--DDPGAVVSPADGKISEIGEIEDDSVIQVKGVTYSLEELLGDDK-LDKFKGGTFIVIYLSPF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448  494 DYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNsKYCNVFTENKRTVAIISTaEFGKVAFVAIGATMVGSINFVRKEGEHV 573
Cdd:pfam02666  78 DYHRNHAPVDGTVKEVRYIPGKLLPVNPLALK-EIPNLFALNERVVLVIET-TDGKVAVVQVGALNVGSIVLTVKPGDEV 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 240256448  574 KKGDELGYFSFgGSTVICVFEKDaiGIDNDLLVNSGRsletlVSVGMQLG 623
Cdd:pfam02666 156 KKGEELGYFKF-GSTVVLLFPKG--KFFEDLVEPGQK-----VKAGETIG 197
Psd COG0688
Phosphatidylserine decarboxylase [Lipid transport and metabolism];
375-608 5.90e-56

Phosphatidylserine decarboxylase [Lipid transport and metabolism];


Pssm-ID: 223760 [Multi-domain]  Cd Length: 239  Bit Score: 189.42  E-value: 5.90e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 375 QGKKMSSVESAQKIPRFLEFFKdqINMAEVKYPLQHFKTFNEFFIRELKPGARPIacmnrNDVAVCAADCRLMAFQsved 454
Cdd:COG0688   19 AGVRSPSPIIKREIYPFIAAFL--VDMSEAEKPLEPYASLNEFFTRFLKYFFRPI-----DPERVSPADGRIVVSP---- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 455 strfwIKGKKFSIRGLLGKNVNPNA-FLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVnskycnvFT 533
Cdd:COG0688   88 -----ADGRVYSVEELLGPDDELAYgDRDGTRVSIFLSPFDYHRNHAPVDGTIIEVRYVPGKFFSANLDKA-------FT 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256448 534 ENKRTVAIISTaEFGKVAFVAIGATMVGSINFVRKEGEHVKKGDELGYFSFG--GSTVICVFEKDAIGIDNDLLVNS 608
Cdd:COG0688  156 ENERNSVLIET-EQGKVVVVQVAGLVARRIVCYVKEGDTVKKGERIGGIRFGsrGSTVLPLFAEPRVAVGERVVAGE 231
PS_decarb TIGR00163
phosphatidylserine decarboxylase precursor; Phosphatidylserine decarboxylase is synthesized as ...
401-626 3.61e-42

phosphatidylserine decarboxylase precursor; Phosphatidylserine decarboxylase is synthesized as a single chain precursor. Generation of the pyruvoyl active site from a Ser is coupled to cleavage of a Gly-Ser bond between the larger (beta) and smaller (alpha chains). It is an integral membrane protein. A closely related family, possibly also active as phosphatidylserine decarboxylase, falls under model TIGR00164. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 272936 [Multi-domain]  Cd Length: 238  Bit Score: 152.29  E-value: 3.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448  401 MAEVKYP-LQHFKTFNEFFIRELKPGARPIacmNRNDVAVCA-ADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGKN--VN 476
Cdd:TIGR00163   1 LDEAEKPdLADYRSLNEFFIRPLKLERRPV---DKEPNALVSpADGVISEVGIINPNQILQVKGMDYSLEELLGEKnpLS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448  477 PNAFLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNsKYCNVFTENKRTVAIISTaEFGKVAFVAIG 556
Cdd:TIGR00163  78 PYFRNGGFFVVTYLSPRDYHRFHSPCDCRLRKMRYFPGDLFSVNPLGLQ-NVPNLFVRNERVILVFDT-EFGNMLMIPVG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448  557 ATMVGSINFV--------------------RKEGEHVKKGDELGYFSFgGSTVICVFEKDAIGIDNDLLVNSGrsletlV 616
Cdd:TIGR00163 156 ATNVGSIRTNfdgniqtnprheftqtwtynALGPVKLLKGEEMGYFEL-GSTVILLFEADAFQLSAHLAVGQE------V 228
                         250
                  ....*....|
gi 240256448  617 SVGMQLGVST 626
Cdd:TIGR00163 229 KIGELLAYEE 238
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
179-240 1.03e-08

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 51.78  E-value: 1.03e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256448 179 AKRILSIVDYNEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAALLA 240
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
PLN02964 PLN02964
phosphatidylserine decarboxylase
1-634 0e+00

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 1307.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448   1 MGNGNSREAKESRRSRLRHKLQKFRIHRRHLRSSRN-SAGMVIQRTVSAEDFSGIALLTLIGAEMKFKDKWLACVSFGEQ 79
Cdd:PLN02964   1 MGNGNSREAKESRRSKLRQKLQKFRIRRRHLRCSRGsSSGSVSQRAVSAEDFSGIALLTLVGAEMKFKDKWLACVSFGEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448  80 TFRTEISDTTQKPIWNSEKKLLLEKNGPSLARVSVFETNRVARNKIIGYCELDIFDFVVQEPESTCKSFNLLDPTSSN-V 158
Cdd:PLN02964  81 TFRTETSDSTDKPVWNSEKKLLLEKNGPHLARISVFETNRLSKNTLVGYCELDLFDFVTQEPESACESFDLLDPSSSNkV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 159 VGSIFLSCAIEDPVETERRFAKRILSIVDYNEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAAL 238
Cdd:PLN02964 161 VGSIFVSCSIEDPVETERSFARRILAIVDYDEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 239 LALQQEQEPIINNCPVCGEALQVSDKLNAMIHMTLCFDEGTGNQVMTGGFLTDRQASYGWMFKLSEWTHLSTYDVGLNTG 318
Cdd:PLN02964 241 LALQQEQEPIINNCPVCGEALGVSDKLNAMIHMTLCFDEGTGNQVMTGGFLTDKQASYGWMFKLSEWAHLSTYDVGLNTG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 319 SSASYIVVIDRKSKRLVEELIDSKIVLSMRAIYQSKIGLRLMDQGAKEILQRLSEKQGKKMSSVESAQKIPRFLEFFKDQ 398
Cdd:PLN02964 321 SSASHILVFDRKSKRLVEELIDSKIVLSMRAIYQSKIGLRLMDQGAKEILQRLSEKQGKKMNSVESAQDIPKFLEFFKDQ 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 399 INMAEVKYPLQHFKTFNEFFIRELKPGARPIACMNRNDVAVCAADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGKNVNPN 478
Cdd:PLN02964 401 INMDEVKYPLEHFKTFNEFFIRELKPGARPIACMDNDDVAVCAADCRLMAFQSVDDSTRFWIKGRKFSIKGLLGKKVHSD 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 479 AFLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNSKYCNVFTENKRTVAIISTAEFGKVAFVAIGAT 558
Cdd:PLN02964 481 AFLDGSLVIFRLAPQDYHRFHVPVSGVIEKFVDVPGSLYTVNPIAVNSKYCNVFTENKRAVCIISTAEFGKVAFVAIGAT 560
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256448 559 MVGSINFVRKEGEHVKKGDELGYFSFGGSTVICVFEKDAIGIDNDLLVNSGRSLETLVSVGMQLGVSTRTFARSTL 634
Cdd:PLN02964 561 MVGSITFVKKEGDHVKKGDELGYFSFGGSTVICVFEKDAIDIDEDLLANSERSLETLVSVGMTLGVSTRTFARQVL 636
PRK00723 PRK00723
phosphatidylserine decarboxylase; Provisional
323-625 3.79e-89

phosphatidylserine decarboxylase; Provisional


Pssm-ID: 179097  Cd Length: 297  Bit Score: 278.73  E-value: 3.79e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 323 YIVVIDRKSKRLVEELIDSKIVLSMraIYQSKIGLRLMDQGAKEILqrLSEKQGKKMSSVESAQKIPRFLEFFkdQINMA 402
Cdd:PRK00723   1 MIKYYNRKTKKYEIEKVAGEKYLKW--LYSSPIGKNLLELLIKKKI--FSKIYGWYCDSRLSRKKIKPFVNDF--NIDMS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 403 EVKYPLQHFKTFNEFFIRELKPGARPIAcmNRNDVAVCAADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGKNVNPNAFLD 482
Cdd:PRK00723  75 ESEKPLSDFKSFNDFFTRKLKPEARPID--QGENILISPGDGRLLAYENIDLNSLFQVKGKTYSLKELLGDPELAKKYAG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 483 GSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNsKYCNVFTENKRTVAIISTAEFGKVAFVAIGATMVGS 562
Cdd:PRK00723 153 GTCLILRLCPTDYHRFHFPDSGICEETRKIKGHYYSVNPIALK-KIFELFCENKREWSIFKSENFGDILYVEVGATCVGS 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240256448 563 INFVRKEGEHVKKGDELGYFSFGGSTVICVFEKDAIGIDNDLLVNSGRSLETLVSVGMQLGVS 625
Cdd:PRK00723 232 IIQTYKPNKKVKKGDEKGYFKFGGSTVILFFEKNKIKIDADILEQSKLGYETKVLMGESIGRK 294
PS_Dcarbxylase pfam02666
Phosphatidylserine decarboxylase; This is a family of phosphatidylserine decarboxylases, EC:4. ...
414-623 6.24e-65

Phosphatidylserine decarboxylase; This is a family of phosphatidylserine decarboxylases, EC:4.1.1.65. These enzymes catalyze the reaction: Phosphatidyl-L-serine <=> phosphatidylethanolamine + CO2. Phosphatidylserine decarboxylase plays a central role in the biosynthesis of aminophospholipids by converting phosphatidylserine to phosphatidylethanolamine.


Pssm-ID: 308345 [Multi-domain]  Cd Length: 198  Bit Score: 211.75  E-value: 6.24e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448  414 FNEFFIRELKPGARPIAcmNRNDVAVCAADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGKNVnPNAFLDGSLVIFRLAPQ 493
Cdd:pfam02666   1 LNAFFTRFLRDPARPIP--DDPGAVVSPADGKISEIGEIEDDSVIQVKGVTYSLEELLGDDK-LDKFKGGTFIVIYLSPF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448  494 DYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNsKYCNVFTENKRTVAIISTaEFGKVAFVAIGATMVGSINFVRKEGEHV 573
Cdd:pfam02666  78 DYHRNHAPVDGTVKEVRYIPGKLLPVNPLALK-EIPNLFALNERVVLVIET-TDGKVAVVQVGALNVGSIVLTVKPGDEV 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 240256448  574 KKGDELGYFSFgGSTVICVFEKDaiGIDNDLLVNSGRsletlVSVGMQLG 623
Cdd:pfam02666 156 KKGEELGYFKF-GSTVVLLFPKG--KFFEDLVEPGQK-----VKAGETIG 197
Psd COG0688
Phosphatidylserine decarboxylase [Lipid transport and metabolism];
375-608 5.90e-56

Phosphatidylserine decarboxylase [Lipid transport and metabolism];


Pssm-ID: 223760 [Multi-domain]  Cd Length: 239  Bit Score: 189.42  E-value: 5.90e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 375 QGKKMSSVESAQKIPRFLEFFKdqINMAEVKYPLQHFKTFNEFFIRELKPGARPIacmnrNDVAVCAADCRLMAFQsved 454
Cdd:COG0688   19 AGVRSPSPIIKREIYPFIAAFL--VDMSEAEKPLEPYASLNEFFTRFLKYFFRPI-----DPERVSPADGRIVVSP---- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 455 strfwIKGKKFSIRGLLGKNVNPNA-FLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVnskycnvFT 533
Cdd:COG0688   88 -----ADGRVYSVEELLGPDDELAYgDRDGTRVSIFLSPFDYHRNHAPVDGTIIEVRYVPGKFFSANLDKA-------FT 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256448 534 ENKRTVAIISTaEFGKVAFVAIGATMVGSINFVRKEGEHVKKGDELGYFSFG--GSTVICVFEKDAIGIDNDLLVNS 608
Cdd:COG0688  156 ENERNSVLIET-EQGKVVVVQVAGLVARRIVCYVKEGDTVKKGERIGGIRFGsrGSTVLPLFAEPRVAVGERVVAGE 231
psd PRK00044
phosphatidylserine decarboxylase; Reviewed
388-623 1.17e-47

phosphatidylserine decarboxylase; Reviewed


Pssm-ID: 234591  Cd Length: 288  Bit Score: 168.85  E-value: 1.17e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 388 IPRFLEFFKdqINMAEVKYP-LQHFKTFNEFFIRELKPGARPIAcmNRNDVAVCAADCRLMAFQSVEDSTRFWIKGKKFS 466
Cdd:PRK00044  38 IRLFIKKYK--VDMSEAQKPdPAAYKTFNDFFTRALKDGARPID--EDPNALVSPADGAISQLGPIEDGQIFQAKGHSYS 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 467 IRGLLGKNVN-PNAFLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNskycNV---FTENKRTVAII 542
Cdd:PRK00044 114 LEALLGGDAAlADPFRNGSFATIYLSPRDYHRVHMPCDGTLREMIYVPGDLFSVNPLTAR----NVpnlFARNERVVCLF 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 543 STaEFGKVAFVAIGATMVGSINFV-------RKEGE--------------HVKKGDELGYFSFgGSTVICVFEKDAIGID 601
Cdd:PRK00044 190 DT-EFGPMAQVLVGATIVGSIETVwagtvtpPREGIikrwdypeagdgaiTLKKGAEMGRFKL-GSTVINLFPPGKVQLA 267
                        250       260
                 ....*....|....*....|..
gi 240256448 602 NDLLVNSgrsletLVSVGMQLG 623
Cdd:PRK00044 268 EQLQAGS------VVRMGQPLA 283
PRK03140 PRK03140
phosphatidylserine decarboxylase; Provisional
388-604 2.02e-47

phosphatidylserine decarboxylase; Provisional


Pssm-ID: 179544  Cd Length: 259  Bit Score: 167.09  E-value: 2.02e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 388 IPRFLEFFkdQINMAEVKYPLQHFKTFNEFFIRELKPGARPIAcmNRNDVAVCAADCRLMAFQSVEDSTRFWIKGKKFSI 467
Cdd:PRK03140  35 IPSYAKVY--QINQDEMEKGLKEYRTLHELFTRKLKEGKRPID--TDASSIVSPVDGVFADVGPIEDDKTFDVKGKRYSI 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 468 RGLLGKNVNPNAFLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVnsKYC-NVFTENKRTVAIIsTAE 546
Cdd:PRK03140 111 AEMLGNEERAQRYAGGTYMVLYLSPSHYHRIHSPISGTVTEQFVLGRKSYPVNALGL--EYGkRPLSKNYRSVTEV-NSD 187
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 240256448 547 FGKVAFVAIGATMVGSINFVRkEGEHVKKGDELGYFSFgGSTVICVFEKDAIGIDNDL 604
Cdd:PRK03140 188 GEHMALVKVGAMFVNSIELTH-ERDTVQKGEEMAYFSF-GSTVVLLFEKDMIEPDQEL 243
PS_decarb TIGR00163
phosphatidylserine decarboxylase precursor; Phosphatidylserine decarboxylase is synthesized as ...
401-626 3.61e-42

phosphatidylserine decarboxylase precursor; Phosphatidylserine decarboxylase is synthesized as a single chain precursor. Generation of the pyruvoyl active site from a Ser is coupled to cleavage of a Gly-Ser bond between the larger (beta) and smaller (alpha chains). It is an integral membrane protein. A closely related family, possibly also active as phosphatidylserine decarboxylase, falls under model TIGR00164. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 272936 [Multi-domain]  Cd Length: 238  Bit Score: 152.29  E-value: 3.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448  401 MAEVKYP-LQHFKTFNEFFIRELKPGARPIacmNRNDVAVCA-ADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGKN--VN 476
Cdd:TIGR00163   1 LDEAEKPdLADYRSLNEFFIRPLKLERRPV---DKEPNALVSpADGVISEVGIINPNQILQVKGMDYSLEELLGEKnpLS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448  477 PNAFLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNsKYCNVFTENKRTVAIISTaEFGKVAFVAIG 556
Cdd:TIGR00163  78 PYFRNGGFFVVTYLSPRDYHRFHSPCDCRLRKMRYFPGDLFSVNPLGLQ-NVPNLFVRNERVILVFDT-EFGNMLMIPVG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448  557 ATMVGSINFV--------------------RKEGEHVKKGDELGYFSFgGSTVICVFEKDAIGIDNDLLVNSGrsletlV 616
Cdd:TIGR00163 156 ATNVGSIRTNfdgniqtnprheftqtwtynALGPVKLLKGEEMGYFEL-GSTVILLFEADAFQLSAHLAVGQE------V 228
                         250
                  ....*....|
gi 240256448  617 SVGMQLGVST 626
Cdd:TIGR00163 229 KIGELLAYEE 238
PRK03934 PRK03934
phosphatidylserine decarboxylase; Provisional
394-602 8.75e-30

phosphatidylserine decarboxylase; Provisional


Pssm-ID: 235177  Cd Length: 265  Bit Score: 118.12  E-value: 8.75e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 394 FFKdqINMAEVKyPLQHFKTFNEFFIRELKpgaRPIACMNRNDVAVCAADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGk 473
Cdd:PRK03934  34 IFK--IDMSEFK-PPENYKSLNALFTRSLK---KPREFDEDPNIFISPCDSLITECGSLEEDKALQIKGMEYSIEELLG- 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 474 NVNPNAFLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNsKYCNVFTENKRTVAIISTAEFGKVAFV 553
Cdd:PRK03934 107 ESNSELVNGFDYINFYLSPKDYHRYHAPCDLEILEARYIPGKLYPVNLPSLE-KNKNLFVKNERVVLKCKDKKGKRLYFV 185
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256448 554 AIGATMVGSINF-----VRKEGE------------HVKKGDELGYFSFgGSTVICVFEKDAIGIDN 602
Cdd:PRK03934 186 FVGALNVGKMRFnfderIQTNAKarfiqtyeyenlKLKKGEELGNFEM-GSTIVLFSQKGSLEFNL 250
PRK09629 PRK09629
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
398-627 6.73e-20

bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional


Pssm-ID: 104071 [Multi-domain]  Cd Length: 610  Bit Score: 93.64  E-value: 6.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 398 QINMAEVKYP-LQHFKTFNEFFIRELKPGARPiacMNRNDVAVCA-ADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGKNV 475
Cdd:PRK09629 369 QVDMSQALVEdLTSYEHFNAFFTRALKADARP---LDTTPGAILSpADGAISQLGPIDHGRIFQAKGHSFSVLELLGGDP 445
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 476 NPNA-FLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNSkYCNVFTENKRTVAIISTaEFGKVAFVA 554
Cdd:PRK09629 446 KLSApFMGGEFATVYLSPKDYHRVHMPLAGTLREMVYVPGRIFSVNQTTAEN-VPELFARNERVVCLFDT-ERGPMAVVL 523
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 555 IGATMVGSINFV--------RKEGE------------HVKKGDELGYFSFgGSTVICVFEKDAIGIDNDLLVNSGrslet 614
Cdd:PRK09629 524 VGAMIVASVETVwaglvtppKRELKtfsydeaarapiHLEKGAEMGRFKL-GSTAIVLFGPNQVKWAEQLTAGSK----- 597
                        250
                 ....*....|...
gi 240256448 615 lVSVGMQLGVSTR 627
Cdd:PRK09629 598 -VQMGQALAVPAQ 609
PTZ00403 PTZ00403
phosphatidylserine decarboxylase; Provisional
399-623 4.39e-19

phosphatidylserine decarboxylase; Provisional


Pssm-ID: 173594  Cd Length: 353  Bit Score: 89.14  E-value: 4.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 399 INMAEVKYPLQHFKTFNEFFIRELKPGARPIACMNRNDVaVCAADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGKNVnPN 478
Cdd:PTZ00403  95 INKEEIKYPIESYKSIGDFFSRYIREETRPIGDVSDYSI-VSPCDSELTDYGELSSEYLENVKGVKFNVNTFLGSDM-QK 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 479 AFLDGS----LVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPiAVNSKYCNVFTENKRtVAIISTAEFGKVAFVA 554
Cdd:PTZ00403 173 KYNDGStkffYAIFYLSPKKYHHFHAPFNFKYKIRRHISGELFPVFQ-GMFKIINNLFNINER-VILSGEWKGGNVYYAA 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 555 IGATMVGSINFVRKEG-------------------------EHVKKGDELGYFSFgGSTVICVFEKDAigiDNDLLVNSG 609
Cdd:PTZ00403 251 ISAYNVGNIKIINDEElvtnnlrtqlsymggdintkiydsyKSVEVGDEVGEFRM-GSSIVVIFENKK---NFSWNVKPN 326
                        250
                 ....*....|....
gi 240256448 610 RSletlVSVGMQLG 623
Cdd:PTZ00403 327 QT----VSVGQRLG 336
PLN02938 PLN02938
phosphatidylserine decarboxylase
400-594 2.63e-18

phosphatidylserine decarboxylase


Pssm-ID: 178526  Cd Length: 428  Bit Score: 87.57  E-value: 2.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 400 NMAEVKYPLQHFKTFNEFFIRELKPGARPI----ACMnrndvaVCAADCRLMAFQSVEDSTRF--WIKGKKFSIRGLLGK 473
Cdd:PLN02938 130 NLEEAALPLEEYASLREFFVRSLKEGARPIdpdpNCL------VSPVDGIVLRFGELKGPGTMieQVKGFSYSVSALLGA 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 474 NVNPNAFLDGSL----------------------------------------VIFrLAPQDYHRFHVPVSGVIEQFVDVS 513
Cdd:PLN02938 204 NSLLPMTAEGKEekeeetlkdksskswlrvslaspklrdpvsaspmkglfycVIY-LGPGDYHRIHSPSDWNIEVRRHFS 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 514 GSLYTVNPIAVNSKYcNVFTENKRTVaIISTAEFGKVAFVAIGATMVGSI----------NFVRKE-------------- 569
Cdd:PLN02938 283 GRLFPVNERATRTIR-NLYVENERVV-LEGEWQEGFMAMAAVGATNIGSIelfiepelrtNRPKKKifnseppeervyep 360
                        250       260
                 ....*....|....*....|....*...
gi 240256448 570 ---GEHVKKGDELGYFSFgGSTVICVFE 594
Cdd:PLN02938 361 egcGLCLKKGDEVAVFNL-GSTVVLVFE 387
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
179-240 1.03e-08

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 51.78  E-value: 1.03e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256448 179 AKRILSIVDYNEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAALLA 240
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
170-235 5.65e-07

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 51.29  E-value: 5.65e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256448 170 DPVETERRFaKRILSIVDYNEDGQLSFSEFSDLI-KAFGNLVAANKKEElFKAADLNGDGVVTIDEL 235
Cdd:cd15899   29 TPEESKRRL-GVIVSKMDVDKDGFISAKELHSWIlESFKRHAMEESKEQ-FRAVDPDEDGHVSWDEY 93
EF-hand_7 pfam13499
EF-hand domain pair;
180-239 5.39e-06

EF-hand domain pair;


Pssm-ID: 338778 [Multi-domain]  Cd Length: 68  Bit Score: 44.18  E-value: 5.39e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240256448  180 KRILSIVDYNEDGQLSFSEFSDLIKAFGNLVAANKKEE---LFKAADLNGDGVVTIDELAALL 239
Cdd:pfam13499   5 KEAFKLLDKDGDGYLDVEELKKLLRKLFEEGEKLSDEEveeLFKEFDLDKDGRISFEEFLELY 67
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
178-239 2.61e-05

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: 44.20  E-value: 2.61e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256448 178 FAKRILSIVDYNEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAALL 239
Cdd:cd15898    1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELY 62
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
169-234 3.61e-05

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 45.75  E-value: 3.61e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256448 169 EDPVETERRFAKRILSIVDYNEDGQLSFSEFSDLI--KAFGNLV-AANKKEELFKAADLNGDGVVTIDE 234
Cdd:cd16225   26 EDSEPKKRKKLKEIFKKVDVNTDGFLSAEELEDWImeKTQEHFQeAVEENEQIFKAVDTDKDGNVSWEE 94
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
176-235 5.85e-05

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 44.98  E-value: 5.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256448 176 RRFAKRILSIVDYNEDGQLSFSEFSDLIKAF-GNLVAANKKE-------ELFKAADLNGDGVVTIDEL 235
Cdd:cd16225  167 KNMVKEILHDLDQDGDEKLTLDEFVSLPPGTvEEQQAEDDDEwkkerkkEFEEVIDLNHDGKVTKEEL 234
EF-hand_8 pfam13833
EF-hand domain pair;
190-241 7.63e-05

EF-hand domain pair;


Pssm-ID: 316358 [Multi-domain]  Cd Length: 53  Bit Score: 40.25  E-value: 7.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240256448  190 EDGQLSFSEFSDLIKAFG-NLVAANKKEELFKAADLNGDGVVTIDELAALLAL 241
Cdd:pfam13833   1 EKGVITREDLRRALALLGlKGLSEEEVDILFREFDTDGDGYISFEEFCVLLER 53
PS_decarb_rel TIGR00164
phosphatidylserine decarboxylase precursor-related protein; Phosphatidylserine decarboxylase ...
480-592 1.78e-04

phosphatidylserine decarboxylase precursor-related protein; Phosphatidylserine decarboxylase is synthesized as a single chain precursor. Generation of the pyruvoyl active site from a Ser is coupled to cleavage of a Gly-Ser bond between the larger (beta) and smaller (alpha chains). It is an integral membrane protein. This protein has many regions of homology to known phosphatidylserine decarboxylases, including the Gly-Ser motif for chain cleavage and active site generation, but has a shorter amino end and a number of deletions along the length of the alignment to the phosphatidylserine decarboxylases. It is unclear whether this protein is a form of phosphatidylserine decarboxylase or is a related enzyme. It is found in Neisseria gonorrhoeae, Mycobacterium tuberculosis, and several archaeal species, all of which lack known phosphatidylserine decarboxylase. [Unknown function, General]


Pssm-ID: 129268  Cd Length: 189  Bit Score: 42.87  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448  480 FLDGS---LVIFrLAPQDYHRFHVPVSGVIEQFVDVSGSLYtvnpiavNSKYCNVFTENKRTVAIISTaEFGKVAFVAIG 556
Cdd:TIGR00164  55 FPDGDglkISIF-MSPFDVHVNRAPAGGKVTYVKHIDGSFV-------PAFLRKASTENERNAVLIKT-ASGEVGVVQIA 125
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 240256448  557 ATMVGSINFVRKEGEHVKKGDELGYFSFGGSTVICV 592
Cdd:TIGR00164 126 GFVARRIVCYVKEGEKVSRGQRIGMIRFGSRVDLYL 161
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
77-144 2.56e-04

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: 40.51  E-value: 2.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256448  77 GEQTFRTEISDTTQKPIWNSEKKLLLEKNGPSLARVSVFETNRVARNKIIGYCELDIFDFVVQEPEST 144
Cdd:cd00030   30 GKQKFKTKVVKNTLNPVWNETFEFPVLDPESDTLTVEVWDKDRFSKDDFLGEVEIPLSELLDSGKEGE 97
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
81-167 2.88e-04

C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated 4 (NEDD4) and NEDD4-like (NEDD4L/NEDD42); Nedd4 and Nedd4-2 are two of the nine members of the Human Nedd4 family. All vertebrates appear to have both Nedd4 and Nedd4-2 genes. They are thought to participate in the regulation of epithelial Na+ channel (ENaC) activity. They also have identical specificity for ubiquitin conjugating enzymes (E2). Nedd4 and Nedd4-2 are composed of a C2 domain, 2-4 WW domains, and a ubiquitin ligase Hect domain. Their WW domains can bind PPxY (PY) or LPSY motifs, and in vitro studies suggest that WW3 and WW4 of both proteins bind PY motifs in the key substrates, with WW3 generally exhibiting higher affinity. Most Nedd4 family members, especially Nedd4-2, also have multiple splice variants, which might play different roles in regulating their substrates. 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: 175999 [Multi-domain]  Cd Length: 133  Bit Score: 41.18  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448  81 FRTEISDTTQKPIWNSE---------KKLLLEkngpslarvsVFETNRVARNKIIGYCELDIFDFVVQEPESTC----KS 147
Cdd:cd04033   41 VQTKTIKKTLNPKWNEEfffrvnpreHRLLFE----------VFDENRLTRDDFLGQVEVPLNNLPTETPGNERrytfKD 110
                         90       100
                 ....*....|....*....|..
gi 240256448 148 FnLLDPTS--SNVVGSIFLSCA 167
Cdd:cd04033  111 Y-LLRPRSskSRVKGHLRLYMA 131
PRK05305 PRK05305
phosphatidylserine decarboxylase; Provisional
499-585 1.26e-03

phosphatidylserine decarboxylase; Provisional


Pssm-ID: 235400  Cd Length: 206  Bit Score: 40.16  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256448 499 HV---PVSGVIEQFVDVSGslytvnpiavnsKYCNVF-----TENKRTVAIISTAEFGKVAFVAI-GAtmvgsinFVR-- 567
Cdd:PRK05305  92 HVnraPVSGTVTKVEYRPG------------KFLNAFldkasEENERNAVVIETADGGEIGVVQIaGL-------IARri 152
                         90       100
                 ....*....|....*....|..
gi 240256448 568 ----KEGEHVKKGDELGYFSFG 585
Cdd:PRK05305 153 vcyvKEGDEVERGERFGLIRFG 174
C2 pfam00168
C2 domain;
73-143 2.80e-03

C2 domain;


Pssm-ID: 333895 [Multi-domain]  Cd Length: 103  Bit Score: 37.30  E-value: 2.80e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256448   73 CVSFGEQTFRTEISDTTQKPIWNSEKKLLLEKNGPSLARVSVFETNRVARNKIIGYCELDIFDFVVQEPES 143
Cdd:pfam00168  28 SLLDGKQKKKTKVVKNTLNPVWNETFTFSVPDLENQVLEIEVYDYDRFGKDDFLGEVRIPLSELDSGEVLD 98
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
172-246 3.38e-03

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: 38.03  E-value: 3.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256448 172 VETERRFAKRILSIVDYNEDGQLSFSEFSDLIKAFgnlvaANKKE--ELFKAADLNGDGVVTIDELAALLALQQEQE 246
Cdd:cd15898   31 IRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSL-----TERPElePIFKKYAGTNRDYMTLEEFIRFLREEQGEN 102
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
186-237 5.56e-03

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 38.84  E-value: 5.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256448 186 VDYNEDGQLSFSEF---------SDLIKAFGNLVAANKK-----EELFKAADLNGDGVVTIDELAA 237
Cdd:cd16227   81 ADEDGDGKVTWEEYladsfgyddEDNEEMIKDSTEDDLKlleddKEMFEAADLNKDGKLDKTEFSA 146
C2B_RasA1_RasA4 cd04025
C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase ...
72-142 8.56e-03

C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase activating protein 1s ), Ras-specific GAP members, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. Both proteins contain two C2 domains, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175991 [Multi-domain]  Cd Length: 123  Bit Score: 36.69  E-value: 8.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256448  72 ACVSFGEQTFRTEISDTTQKPIWNSEKKLLLEKNGPSLARVSVFETNRVARNKIIGYCELDIFDFVVQEPE 142
Cdd:cd04025   25 VRVFYNGQTLETSVVKKSCYPRWNEVFEFELMEGADSPLSVEVWDWDLVSKNDFLGKVVFSIQTLQQAKQE 95
EF-hand_5 pfam13202
EF hand;
216-239 8.95e-03

EF hand;


Pssm-ID: 338631  Cd Length: 25  Bit Score: 33.81  E-value: 8.95e-03
                          10        20
                  ....*....|....*....|....
gi 240256448  216 EELFKAADLNGDGVVTIDELAALL 239
Cdd:pfam13202   2 KDAFRQFDLNGDGKISKEELKRLL 25
Dockerin_II cd14254
Type II dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein ...
187-238 9.50e-03

Type II dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type II dockerins, which are responsible for mediating attachment of the cellulosome complex to the bacterial cell wall.


Pssm-ID: 271213  Cd Length: 54  Bit Score: 34.49  E-value: 9.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 240256448 187 DYNEDGQLSFSEFSDLIKAFGNLVAANKKEelfkAADLNGDGVVTIDELAAL 238
Cdd:cd14254    2 DVNGDGVVDIADLALVSQHFGKTSDAGYVP----AADLNGDGVIDAADLALL 49
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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