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Conserved domains on  [gi|20071759|gb|AAH27143|]
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Unknown (protein for MGC:36892) [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02964 super family cl33609
phosphatidylserine decarboxylase
1-513 0e+00

phosphatidylserine decarboxylase


The actual alignment was detected with superfamily member PLN02964:

Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 792.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759    1 MGHGSSKDSSSSRRGKMRQKL------RRIVRRESRSKHSADRFKLVSADDFAGIALLTLISAKMTFKDKWLASVTLGEQ 74
Cdd:PLN02964   1 MGNGNSREAKESRRSKLRQKLqkfrirRRHLRCSRGSSSGSVSQRAVSAEDFSGIALLTLVGAEMKFKDKWLACVSFGEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759   75 TFCTNITENTEEPVWNSEKKLLLESNGSHTARVSVYETNLLKKNNLIGYCEIDLLLFLTQDSDSDIVEVDLLDPSATDI- 153
Cdd:PLN02964  81 TFRTETSDSTDKPVWNSEKKLLLEKNGPHLARISVFETNRLSKNTLVGYCELDLFDFVTQEPESACESFDLLDPSSSNKv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  154 VGKLSFSCFIEDPEETEKDFARRILSIVDYNEDGLLSFSEFSDLINAFGNQVAADKKEELFKYADINGDGAVSIEELAAL 233
Cdd:PLN02964 161 VGSIFVSCSIEDPVETERSFARRILAIVDYDEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  234 LARHQEKEPLINTCPVCGESLDASNRVGSMVHMTLCFNEGARNNVMSGSFLTDKQASYGWLLKLSEWAHYSSEGTGSQLA 313
Cdd:PLN02964 241 LALQQEQEPIINNCPVCGEALGVSDKLNAMIHMTLCFDEGTGNQVMTGGFLTDKQASYGWMFKLSEWAHLSTYDVGLNTG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  314 TKTRHILVFDRMTKRLVEEIIDGKIVLAMRALYQNKPGVYFLEKGGKEIMQKLSEKQGDKMNSVDSIKEIPKFIDLFKDQ 393
Cdd:PLN02964 321 SSASHILVFDRKSKRLVEELIDSKIVLSMRAIYQSKIGLRLMDQGAKEILQRLSEKQGKKMNSVESAQDIPKFLEFFKDQ 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  394 LNLSETKYPLDHFKTFNEFFIRELKPGARPIAFIDRDDNAVCGADSRLMAFKNVEESTRIWIKGRRFSIKGLLGNDVSAT 473
Cdd:PLN02964 401 INMDEVKYPLEHFKTFNEFFIRELKPGARPIACMDNDDVAVCAADCRLMAFQSVDDSTRFWIKGRKFSIKGLLGKKVHSD 480
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 20071759  474 PFIGGALVIFRLAPQDYHRFHLPVSGTVERFVPIPGSLYT 513
Cdd:PLN02964 481 AFLDGSLVIFRLAPQDYHRFHVPVSGVIEKFVDVPGSLYT 520
 
Name Accession Description Interval E-value
PLN02964 PLN02964
phosphatidylserine decarboxylase
1-513 0e+00

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 792.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759    1 MGHGSSKDSSSSRRGKMRQKL------RRIVRRESRSKHSADRFKLVSADDFAGIALLTLISAKMTFKDKWLASVTLGEQ 74
Cdd:PLN02964   1 MGNGNSREAKESRRSKLRQKLqkfrirRRHLRCSRGSSSGSVSQRAVSAEDFSGIALLTLVGAEMKFKDKWLACVSFGEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759   75 TFCTNITENTEEPVWNSEKKLLLESNGSHTARVSVYETNLLKKNNLIGYCEIDLLLFLTQDSDSDIVEVDLLDPSATDI- 153
Cdd:PLN02964  81 TFRTETSDSTDKPVWNSEKKLLLEKNGPHLARISVFETNRLSKNTLVGYCELDLFDFVTQEPESACESFDLLDPSSSNKv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  154 VGKLSFSCFIEDPEETEKDFARRILSIVDYNEDGLLSFSEFSDLINAFGNQVAADKKEELFKYADINGDGAVSIEELAAL 233
Cdd:PLN02964 161 VGSIFVSCSIEDPVETERSFARRILAIVDYDEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  234 LARHQEKEPLINTCPVCGESLDASNRVGSMVHMTLCFNEGARNNVMSGSFLTDKQASYGWLLKLSEWAHYSSEGTGSQLA 313
Cdd:PLN02964 241 LALQQEQEPIINNCPVCGEALGVSDKLNAMIHMTLCFDEGTGNQVMTGGFLTDKQASYGWMFKLSEWAHLSTYDVGLNTG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  314 TKTRHILVFDRMTKRLVEEIIDGKIVLAMRALYQNKPGVYFLEKGGKEIMQKLSEKQGDKMNSVDSIKEIPKFIDLFKDQ 393
Cdd:PLN02964 321 SSASHILVFDRKSKRLVEELIDSKIVLSMRAIYQSKIGLRLMDQGAKEILQRLSEKQGKKMNSVESAQDIPKFLEFFKDQ 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  394 LNLSETKYPLDHFKTFNEFFIRELKPGARPIAFIDRDDNAVCGADSRLMAFKNVEESTRIWIKGRRFSIKGLLGNDVSAT 473
Cdd:PLN02964 401 INMDEVKYPLEHFKTFNEFFIRELKPGARPIACMDNDDVAVCAADCRLMAFQSVDDSTRFWIKGRKFSIKGLLGKKVHSD 480
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 20071759  474 PFIGGALVIFRLAPQDYHRFHLPVSGTVERFVPIPGSLYT 513
Cdd:PLN02964 481 AFLDGSLVIFRLAPQDYHRFHVPVSGVIEKFVDVPGSLYT 520
PS_Dcarbxylase pfam02666
Phosphatidylserine decarboxylase; This is a family of phosphatidylserine decarboxylases, EC:4. ...
409-513 2.33e-31

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: 120.07  E-value: 2.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759   409 FNEFFIRELKPGARPIAfiDRDDNAVCGADSRLMAFKNVEESTRIWIKGRRFSIKGLLGNDvSATPFIGGALVIFRLAPQ 488
Cdd:pfam02666   1 LNAFFTRFLRDPARPIP--DDPGAVVSPADGKISEIGEIEDDSVIQVKGVTYSLEELLGDD-KLDKFKGGTFIVIYLSPF 77
                          90       100
                  ....*....|....*....|....*
gi 20071759   489 DYHRFHLPVSGTVERFVPIPGSLYT 513
Cdd:pfam02666  78 DYHRNHAPVDGTVKEVRYIPGKLLP 102
Psd COG0688
Phosphatidylserine decarboxylase [Lipid transport and metabolism];
370-513 8.90e-28

Phosphatidylserine decarboxylase [Lipid transport and metabolism];


Pssm-ID: 223760 [Multi-domain]  Cd Length: 239  Bit Score: 111.23  E-value: 8.90e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759 370 QGDKMNSVDSIKEIPKFIDLFKdqLNLSETKYPLDHFKTFNEFFIRELKPGARPIafidrDDNAVCGADSRLMAFKnvee 449
Cdd:COG0688  19 AGVRSPSPIIKREIYPFIAAFL--VDMSEAEKPLEPYASLNEFFTRFLKYFFRPI-----DPERVSPADGRIVVSP---- 87
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20071759 450 striwIKGRRFSIKGLLGNDVS-ATPFIGGALVIFRLAPQDYHRFHLPVSGTVERFVPIPGSLYT 513
Cdd:COG0688  88 -----ADGRVYSVEELLGPDDElAYGDRDGTRVSIFLSPFDYHRNHAPVDGTIIEVRYVPGKFFS 147
PS_decarb TIGR00163
phosphatidylserine decarboxylase precursor; Phosphatidylserine decarboxylase is synthesized as ...
396-512 5.85e-21

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: 91.82  E-value: 5.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759   396 LSETKYP-LDHFKTFNEFFIRELKPGARPIafiDRDDNAVCG-ADSRLMAFKNVEESTRIWIKGRRFSIKGLLGNDVSAT 473
Cdd:TIGR00163   1 LDEAEKPdLADYRSLNEFFIRPLKLERRPV---DKEPNALVSpADGVISEVGIINPNQILQVKGMDYSLEELLGEKNPLS 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 20071759   474 PFI--GGALVIFRLAPQDYHRFHLPVSGTVERFVPIPGSLY 512
Cdd:TIGR00163  78 PYFrnGGFFVVTYLSPRDYHRFHSPCDCRLRKMRYFPGDLF 118
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
174-235 5.07e-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: 49.47  E-value: 5.07e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20071759 174 ARRILSIVDYNEDGLLSFSEFSDLINAFGNQVAADKKEELFKYADINGDGAVSIEELAALLA 235
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
72-128 2.74e-03

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: 37.08  E-value: 2.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 20071759     72 GEQTFCTNITENTEEPVWNSEKKLLLESNGSHTARVSVYETNLLKKNNLIGYCEIDL 128
Cdd:smart00239  33 PKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKDRFGRDDFIGQVTIPL 89
 
Name Accession Description Interval E-value
PLN02964 PLN02964
phosphatidylserine decarboxylase
1-513 0e+00

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 792.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759    1 MGHGSSKDSSSSRRGKMRQKL------RRIVRRESRSKHSADRFKLVSADDFAGIALLTLISAKMTFKDKWLASVTLGEQ 74
Cdd:PLN02964   1 MGNGNSREAKESRRSKLRQKLqkfrirRRHLRCSRGSSSGSVSQRAVSAEDFSGIALLTLVGAEMKFKDKWLACVSFGEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759   75 TFCTNITENTEEPVWNSEKKLLLESNGSHTARVSVYETNLLKKNNLIGYCEIDLLLFLTQDSDSDIVEVDLLDPSATDI- 153
Cdd:PLN02964  81 TFRTETSDSTDKPVWNSEKKLLLEKNGPHLARISVFETNRLSKNTLVGYCELDLFDFVTQEPESACESFDLLDPSSSNKv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  154 VGKLSFSCFIEDPEETEKDFARRILSIVDYNEDGLLSFSEFSDLINAFGNQVAADKKEELFKYADINGDGAVSIEELAAL 233
Cdd:PLN02964 161 VGSIFVSCSIEDPVETERSFARRILAIVDYDEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  234 LARHQEKEPLINTCPVCGESLDASNRVGSMVHMTLCFNEGARNNVMSGSFLTDKQASYGWLLKLSEWAHYSSEGTGSQLA 313
Cdd:PLN02964 241 LALQQEQEPIINNCPVCGEALGVSDKLNAMIHMTLCFDEGTGNQVMTGGFLTDKQASYGWMFKLSEWAHLSTYDVGLNTG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  314 TKTRHILVFDRMTKRLVEEIIDGKIVLAMRALYQNKPGVYFLEKGGKEIMQKLSEKQGDKMNSVDSIKEIPKFIDLFKDQ 393
Cdd:PLN02964 321 SSASHILVFDRKSKRLVEELIDSKIVLSMRAIYQSKIGLRLMDQGAKEILQRLSEKQGKKMNSVESAQDIPKFLEFFKDQ 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  394 LNLSETKYPLDHFKTFNEFFIRELKPGARPIAFIDRDDNAVCGADSRLMAFKNVEESTRIWIKGRRFSIKGLLGNDVSAT 473
Cdd:PLN02964 401 INMDEVKYPLEHFKTFNEFFIRELKPGARPIACMDNDDVAVCAADCRLMAFQSVDDSTRFWIKGRKFSIKGLLGKKVHSD 480
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 20071759  474 PFIGGALVIFRLAPQDYHRFHLPVSGTVERFVPIPGSLYT 513
Cdd:PLN02964 481 AFLDGSLVIFRLAPQDYHRFHVPVSGVIEKFVDVPGSLYT 520
PRK00723 PRK00723
phosphatidylserine decarboxylase; Provisional
319-512 9.06e-42

phosphatidylserine decarboxylase; Provisional


Pssm-ID: 179097  Cd Length: 297  Bit Score: 151.61  E-value: 9.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  319 ILVFDRMTKRLVEEIIDGKivLAMRALYQNKPGVYFLEKGGKEIMqkLSEKQGDKMNSVDSIKEIPKFIDLFkdQLNLSE 398
Cdd:PRK00723   2 IKYYNRKTKKYEIEKVAGE--KYLKWLYSSPIGKNLLELLIKKKI--FSKIYGWYCDSRLSRKKIKPFVNDF--NIDMSE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  399 TKYPLDHFKTFNEFFIRELKPGARPIafiDRDDNA-VCGADSRLMAFKNVEESTRIWIKGRRFSIKGLLGNDVSATPFIG 477
Cdd:PRK00723  76 SEKPLSDFKSFNDFFTRKLKPEARPI---DQGENIlISPGDGRLLAYENIDLNSLFQVKGKTYSLKELLGDPELAKKYAG 152
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 20071759  478 GALVIFRLAPQDYHRFHLPVSGTVERFVPIPGSLY 512
Cdd:PRK00723 153 GTCLILRLCPTDYHRFHFPDSGICEETRKIKGHYY 187
PS_Dcarbxylase pfam02666
Phosphatidylserine decarboxylase; This is a family of phosphatidylserine decarboxylases, EC:4. ...
409-513 2.33e-31

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: 120.07  E-value: 2.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759   409 FNEFFIRELKPGARPIAfiDRDDNAVCGADSRLMAFKNVEESTRIWIKGRRFSIKGLLGNDvSATPFIGGALVIFRLAPQ 488
Cdd:pfam02666   1 LNAFFTRFLRDPARPIP--DDPGAVVSPADGKISEIGEIEDDSVIQVKGVTYSLEELLGDD-KLDKFKGGTFIVIYLSPF 77
                          90       100
                  ....*....|....*....|....*
gi 20071759   489 DYHRFHLPVSGTVERFVPIPGSLYT 513
Cdd:pfam02666  78 DYHRNHAPVDGTVKEVRYIPGKLLP 102
psd PRK00044
phosphatidylserine decarboxylase; Reviewed
386-512 1.69e-30

phosphatidylserine decarboxylase; Reviewed


Pssm-ID: 234591  Cd Length: 288  Bit Score: 120.32  E-value: 1.69e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  386 FIDLF--KDQLNLSETKYP-LDHFKTFNEFFIRELKPGARPIafiDRDDNA-VCGADSRLMAFKNVEESTRIWIKGRRFS 461
Cdd:PRK00044  37 VIRLFikKYKVDMSEAQKPdPAAYKTFNDFFTRALKDGARPI---DEDPNAlVSPADGAISQLGPIEDGQIFQAKGHSYS 113
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 20071759  462 IKGLLGND-VSATPFIGGALVIFRLAPQDYHRFHLPVSGTVERFVPIPGSLY 512
Cdd:PRK00044 114 LEALLGGDaALADPFRNGSFATIYLSPRDYHRVHMPCDGTLREMIYVPGDLF 165
Psd COG0688
Phosphatidylserine decarboxylase [Lipid transport and metabolism];
370-513 8.90e-28

Phosphatidylserine decarboxylase [Lipid transport and metabolism];


Pssm-ID: 223760 [Multi-domain]  Cd Length: 239  Bit Score: 111.23  E-value: 8.90e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759 370 QGDKMNSVDSIKEIPKFIDLFKdqLNLSETKYPLDHFKTFNEFFIRELKPGARPIafidrDDNAVCGADSRLMAFKnvee 449
Cdd:COG0688  19 AGVRSPSPIIKREIYPFIAAFL--VDMSEAEKPLEPYASLNEFFTRFLKYFFRPI-----DPERVSPADGRIVVSP---- 87
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20071759 450 striwIKGRRFSIKGLLGNDVS-ATPFIGGALVIFRLAPQDYHRFHLPVSGTVERFVPIPGSLYT 513
Cdd:COG0688  88 -----ADGRVYSVEELLGPDDElAYGDRDGTRVSIFLSPFDYHRNHAPVDGTIIEVRYVPGKFFS 147
PRK03140 PRK03140
phosphatidylserine decarboxylase; Provisional
383-503 3.73e-27

phosphatidylserine decarboxylase; Provisional


Pssm-ID: 179544  Cd Length: 259  Bit Score: 110.08  E-value: 3.73e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  383 IPKFIDLFkdQLNLSETKYPLDHFKTFNEFFIRELKPGARPIafiDRDDNAVCG-ADSRLMAFKNVEESTRIWIKGRRFS 461
Cdd:PRK03140  35 IPSYAKVY--QINQDEMEKGLKEYRTLHELFTRKLKEGKRPI---DTDASSIVSpVDGVFADVGPIEDDKTFDVKGKRYS 109
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 20071759  462 IKGLLGNDVSATPFIGGALVIFRLAPQDYHRFHLPVSGTVER 503
Cdd:PRK03140 110 IAEMLGNEERAQRYAGGTYMVLYLSPSHYHRIHSPISGTVTE 151
PS_decarb TIGR00163
phosphatidylserine decarboxylase precursor; Phosphatidylserine decarboxylase is synthesized as ...
396-512 5.85e-21

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: 91.82  E-value: 5.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759   396 LSETKYP-LDHFKTFNEFFIRELKPGARPIafiDRDDNAVCG-ADSRLMAFKNVEESTRIWIKGRRFSIKGLLGNDVSAT 473
Cdd:TIGR00163   1 LDEAEKPdLADYRSLNEFFIRPLKLERRPV---DKEPNALVSpADGVISEVGIINPNQILQVKGMDYSLEELLGEKNPLS 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 20071759   474 PFI--GGALVIFRLAPQDYHRFHLPVSGTVERFVPIPGSLY 512
Cdd:TIGR00163  78 PYFrnGGFFVVTYLSPRDYHRFHSPCDCRLRKMRYFPGDLF 118
PRK03934 PRK03934
phosphatidylserine decarboxylase; Provisional
381-512 1.91e-17

phosphatidylserine decarboxylase; Provisional


Pssm-ID: 235177  Cd Length: 265  Bit Score: 82.30  E-value: 1.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  381 KEIPKFID---------LFKdqLNLSETKyPLDHFKTFNEFFIRELKpgaRPIAFIDRDDNAVCGADSRLMAFKNVEEST 451
Cdd:PRK03934  17 YKFPKFIQkfinasyvkIFK--IDMSEFK-PPENYKSLNALFTRSLK---KPREFDEDPNIFISPCDSLITECGSLEEDK 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20071759  452 RIWIKGRRFSIKGLLGNDVSaTPFIGGALVIFRLAPQDYHRFHLPVSGTVERFVPIPGSLY 512
Cdd:PRK03934  91 ALQIKGMEYSIEELLGESNS-ELVNGFDYINFYLSPKDYHRYHAPCDLEILEARYIPGKLY 150
PRK09629 PRK09629
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
403-513 8.05e-15

bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional


Pssm-ID: 104071 [Multi-domain]  Cd Length: 610  Bit Score: 77.08  E-value: 8.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  403 LDHFKTFNEFFIRELKPGARPIafiDRDDNAVCG-ADSRLMAFKNVEESTRIWIKGRRFSIKGLLGNDVS-ATPFIGGAL 480
Cdd:PRK09629 380 LTSYEHFNAFFTRALKADARPL---DTTPGAILSpADGAISQLGPIDHGRIFQAKGHSFSVLELLGGDPKlSAPFMGGEF 456
                         90       100       110
                 ....*....|....*....|....*....|...
gi 20071759  481 VIFRLAPQDYHRFHLPVSGTVERFVPIPGSLYT 513
Cdd:PRK09629 457 ATVYLSPKDYHRVHMPLAGTLREMVYVPGRIFS 489
PTZ00403 PTZ00403
phosphatidylserine decarboxylase; Provisional
394-496 2.81e-12

phosphatidylserine decarboxylase; Provisional


Pssm-ID: 173594  Cd Length: 353  Bit Score: 67.96  E-value: 2.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  394 LNLSETKYPLDHFKTFNEFFIRELKPGARPIAFIDrDDNAVCGADSRLMAFKNVEESTRIWIKGRRFSIKGLLG------ 467
Cdd:PTZ00403  95 INKEEIKYPIESYKSIGDFFSRYIREETRPIGDVS-DYSIVSPCDSELTDYGELSSEYLENVKGVKFNVNTFLGsdmqkk 173
                         90       100       110
                 ....*....|....*....|....*....|
gi 20071759  468 -NDVSATPFiggaLVIFRLAPQDYHRFHLP 496
Cdd:PTZ00403 174 yNDGSTKFF----YAIFYLSPKKYHHFHAP 199
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
174-235 5.07e-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: 49.47  E-value: 5.07e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20071759 174 ARRILSIVDYNEDGLLSFSEFSDLINAFGNQVAADKKEELFKYADINGDGAVSIEELAALLA 235
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PLN02938 PLN02938
phosphatidylserine decarboxylase
395-512 9.02e-08

phosphatidylserine decarboxylase


Pssm-ID: 178526  Cd Length: 428  Bit Score: 54.44  E-value: 9.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  395 NLSETKYPLDHFKTFNEFFIRELKPGARPiafIDRDDNA-VCGADSRLMAFKNVEES-TRI-WIKGRRFSIKGLLGND-- 469
Cdd:PLN02938 130 NLEEAALPLEEYASLREFFVRSLKEGARP---IDPDPNClVSPVDGIVLRFGELKGPgTMIeQVKGFSYSVSALLGANsl 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  470 -------------------------------------VSATPFIGGALVIFRLAPQDYHRFHLPVSGTVERFVPIPGSLY 512
Cdd:PLN02938 207 lpmtaegkeekeeetlkdksskswlrvslaspklrdpVSASPMKGLFYCVIYLGPGDYHRIHSPSDWNIEVRRHFSGRLF 286
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
173-241 1.35e-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: 44.58  E-value: 1.35e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20071759 173 FARRILSIVDYNEDGLLSFSEFSDLINAFGNQVAADKKEELFKYADINGDGAVSIEELAALLARHQEKE 241
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERP 69
EF-hand_8 pfam13833
EF-hand domain pair;
185-236 1.46e-05

EF-hand domain pair;


Pssm-ID: 316358 [Multi-domain]  Cd Length: 53  Bit Score: 42.18  E-value: 1.46e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 20071759   185 EDGLLSFSEFSDLINAFGNQ-VAADKKEELFKYADINGDGAVSIEELAALLAR 236
Cdd:pfam13833   1 EKGVITREDLRRALALLGLKgLSEEEVDILFREFDTDGDGYISFEEFCVLLER 53
C2 pfam00168
C2 domain;
68-128 1.59e-05

C2 domain;


Pssm-ID: 333895 [Multi-domain]  Cd Length: 103  Bit Score: 43.46  E-value: 1.59e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20071759    68 SVTLGEQTFCTNITENTEEPVWNSEKKLLLESNGSHTARVSVYETNLLKKNNLIGYCEIDL 128
Cdd:pfam00168  28 SLLDGKQKKKTKVVKNTLNPVWNETFTFSVPDLENQVLEIEVYDYDRFGKDDFLGEVRIPL 88
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
72-139 9.16e-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: 41.28  E-value: 9.16e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20071759  72 GEQTFCTNITENTEEPVWNSEKKLLLESNGSHTARVSVYETNLLKKNNLIGYCEIDLLLFLTQDSDSD 139
Cdd:cd00030  30 GKQKFKTKVVKNTLNPVWNETFEFPVLDPESDTLTVEVWDKDRFSKDDFLGEVEIPLSELLDSGKEGE 97
EF-hand_7 pfam13499
EF-hand domain pair;
171-234 1.36e-04

EF-hand domain pair;


Pssm-ID: 338778 [Multi-domain]  Cd Length: 68  Bit Score: 39.95  E-value: 1.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20071759   171 KDFARRILSIVDYNEDGLLSFSEFSDLINAFGNQVAADKKEE---LFKYADINGDGAVSIEELAALL 234
Cdd:pfam13499   1 EEKLKEAFKLLDKDGDGYLDVEELKKLLRKLFEEGEKLSDEEveeLFKEFDLDKDGRISFEEFLELY 67
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
165-230 1.83e-04

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: 43.20  E-value: 1.83e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20071759 165 DPEETEKDFaRRILSIVDYNEDGLLSFSEFSDLINAFGNQVAADKKEELFKYADINGDGAVSIEEL 230
Cdd:cd15899  29 TPEESKRRL-GVIVSKMDVDKDGFISAKELHSWILESFKRHAMEESKEQFRAVDPDEDGHVSWDEY 93
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
162-229 2.79e-04

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: 42.67  E-value: 2.79e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20071759 162 FIEDPEETEKDFARRILSIVDYNEDGLLSFSEFSDLINAFGN---QVAADKKEELFKYADINGDGAVSIEE 229
Cdd:cd16225  24 FEEDSEPKKRKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQehfQEAVEENEQIFKAVDTDKDGNVSWEE 94
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
78-160 6.13e-04

C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176009 [Multi-domain]  Cd Length: 124  Bit Score: 39.46  E-value: 6.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071759  78 TNITENTEEPVWNsEKKLLLESNGSHTARVSVYETNLLKKNNLIGYCEIDLLLFLTQDSDSDIVeVDLLDPSATdiVGKL 157
Cdd:cd04044  41 TKVKKDTSNPVWN-ETKYILVNSLTEPLNLTVYDFNDKRKDKLIGTAEFDLSSLLQNPEQENLT-KNLLRNGKP--VGEL 116

                ...
gi 20071759 158 SFS 160
Cdd:cd04044 117 NYD 119
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
72-141 1.25e-03

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 41.67  E-value: 1.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20071759   72 GEQTFCTNITENTEEPVWNSEKKLLLESNGSHTARVSVYETNLLKKNNLIGYCEIDLLLFLTQ-DSDSDIV 141
Cdd:COG5038 1071 EKSVYKTKVVKKTLNPVWNEEFTIEVLNRVKDVLTINVNDWDSGEKNDLLGTAEIDLSKLEPGgTTNSNIP 1141
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
72-128 2.74e-03

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: 37.08  E-value: 2.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 20071759     72 GEQTFCTNITENTEEPVWNSEKKLLLESNGSHTARVSVYETNLLKKNNLIGYCEIDL 128
Cdd:smart00239  33 PKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKDRFGRDDFIGQVTIPL 89
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
164-229 3.94e-03

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed calcium-binding protein ERC-55, or E6-binding protein (E6BP), or TCBP-49, is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. It is associated with tumorigenesis, in particular with transformation of cells of the cervix induced by human papillomavirus (HPV), through binding to human papillomavirus (HPV) E6 oncogenic protein. It specifically interacts with vitamin D receptor among nuclear receptors. RCN2 contains an N-terminal signal sequence followed by six copies of the EF-hand Ca2+-binding motif, and a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 38.95  E-value: 3.94e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20071759 164 EDPEETEK----DFARRILSIV---DYNEDGLLSFSEFSDLI-NAFGNQVAADKKEELFKYaDINGDGAVSIEE 229
Cdd:cd16224  21 EDADEFAKlspeEQQKRLKSIIkkiDTDSDGFLTEEELSSWIqQSFRHYALEDAKQQFPEY-DKDGDGAVTWDE 93
 
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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