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Conserved domains on  [gi|14548191|sp|O15162|]
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RecName: Full=Phospholipid scramblase 1; Short=PL scramblase 1; AltName: Full=Ca(2+)-dependent phospholipid scramblase 1; AltName: Full=Erythrocyte phospholipid scramblase; AltName: Full=Mg(2+)-dependent nuclease; AltName: Full=MmTRA1b

Protein Classification

phospholipid scramblase family protein( domain architecture ID 10510595)

phospholipid scramblase family protein similar to mammalian phospholipid scramblase and Saccharomyces cerevisiae altered inheritance rate of mitochondria protein 25

Gene Ontology:  GO:0017128
PubMed:  11487015|19010806

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Scramblase pfam03803
Scramblase; Scramblase is palmitoylated and contains a potential protein kinase C ...
 86-307 1.10e-124

Scramblase; Scramblase is palmitoylated and contains a potential protein kinase C phosphorylation site. Scramblase exhibits Ca2+-activated phospholipid scrambling activity in vitro. There are also possible SH3 and WW binding motifs. Scramblase is involved in the redistribution of phospholipids after cell activation or injury.


:

Pssm-ID: 252175  Cd Length: 221  Bit Score: 355.89  E-value: 1.10e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191    86 MPAP-QPPLNCPPGLEYLSQIDQILIHQQIELLEVLTGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRI 164
Cdd:pfam03803   1 MSGPgQPPANCPAGLEYLLQLDQILVHQQIEPLEVFTGFETANRYVVKNVNGQPLYYAMERSNCCARQCCGTHRPFVMRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191   165 IDNMGQEVITLERPLRcSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCCGDVD 244
Cdd:pfam03803  81 TDNFGNEVMTLKRPFS-CISCCPSCLQEQEIQAPPGTTIGEVLQTWHLWRPNYELQNADGNQVLSIFGPCFKCDCGGDWE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14548191   245 FEIKSLDeQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLIDFMFFES 307
Cdd:pfam03803 160 FPVKTAD-GEVVGSISRNWPGLGREAFTDADTYVVRFPLDLDVKLKAVLLGAAFLIDFMYFER 221
PHA03378 super family cl33729
EBNA-3B; Provisional
 22-97 1.06e-05

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.98  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191   22 PPQYPPTAFQGPPGYSGYPGPQVSYPP---PPAGHSGPG--PAGFPVPNQPVYNQPVYNQPvgAAGVPWMPAPQPPLNCP 96
Cdd:PHA03378 706 PPAAPPGRAQRPAAATGRARPPAAAPGrarPPAAAPGRArpPAAAPGRARPPAAAPGRARP--PAAAPGAPTPQPPPQAP 783


                 .
gi 14548191   97 P 97
Cdd:PHA03378 784 P 784
 
Name Accession Description Interval E-value
Scramblase pfam03803
Scramblase; Scramblase is palmitoylated and contains a potential protein kinase C ...
 86-307 1.10e-124

Scramblase; Scramblase is palmitoylated and contains a potential protein kinase C phosphorylation site. Scramblase exhibits Ca2+-activated phospholipid scrambling activity in vitro. There are also possible SH3 and WW binding motifs. Scramblase is involved in the redistribution of phospholipids after cell activation or injury.


Pssm-ID: 252175  Cd Length: 221  Bit Score: 355.89  E-value: 1.10e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191    86 MPAP-QPPLNCPPGLEYLSQIDQILIHQQIELLEVLTGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRI 164
Cdd:pfam03803   1 MSGPgQPPANCPAGLEYLLQLDQILVHQQIEPLEVFTGFETANRYVVKNVNGQPLYYAMERSNCCARQCCGTHRPFVMRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191   165 IDNMGQEVITLERPLRcSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCCGDVD 244
Cdd:pfam03803  81 TDNFGNEVMTLKRPFS-CISCCPSCLQEQEIQAPPGTTIGEVLQTWHLWRPNYELQNADGNQVLSIFGPCFKCDCGGDWE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14548191   245 FEIKSLDeQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLIDFMFFES 307
Cdd:pfam03803 160 FPVKTAD-GEVVGSISRNWPGLGREAFTDADTYVVRFPLDLDVKLKAVLLGAAFLIDFMYFER 221
YxjI COG4894
Putative phospholipid scramblase YxjI, Tubby2 superfamily [Lipid transport and metabolism];
106-303 9.78e-11

Putative phospholipid scramblase YxjI, Tubby2 superfamily [Lipid transport and metabolism];


Pssm-ID: 443922  Cd Length: 163  Bit Score: 59.47  E-value: 9.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191 106 DQILIHQQIellevltgFETNNKYEIKNSFGQRVYFAAEDtdcctrnccGPSRPFTLRIIDNMGQEVITLERPLrcsscc 185
Cdd:COG4894   2 RTLYIKQKI--------FSLGDDFTIYDENGQPVYLVKGK---------FFSLGDTLSIYDADGNELATIKQKL------ 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191 186 cPCCLQEIEIQApPGVPIGYVIQTWHPCLPKFTIQNEKREdvLKISGPCVvcsccgDVDFEIKSLDEqcVVGKISKHWtg 265
Cdd:COG4894  59 -FSLLPTFEIYD-DGEPVATIKKKFTFFKDRFTIEADGLD--LEIEGDFW------DHDFEITRGGK--VVASVSKKW-- 124

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 14548191 266 ilreaFTDADNFGIQFPldlDVKMKAVMIGACFLIDFM 303
Cdd:COG4894 125 -----FSWRDTYELDID---DEEDRPLVIALAIAIDAV 154
PHA03378 PHA03378
EBNA-3B; Provisional
 22-97 1.06e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.98  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191   22 PPQYPPTAFQGPPGYSGYPGPQVSYPP---PPAGHSGPG--PAGFPVPNQPVYNQPVYNQPvgAAGVPWMPAPQPPLNCP 96
Cdd:PHA03378 706 PPAAPPGRAQRPAAATGRARPPAAAPGrarPPAAAPGRArpPAAAPGRARPPAAAPGRARP--PAAAPGAPTPQPPPQAP 783


                 .
gi 14548191   97 P 97
Cdd:PHA03378 784 P 784
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 18-97 2.82e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 39.37  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191    18 PVGYPPQYPPTAFQGPpgysGYPGPQVSYPPPPAGHSGPGPAGFP----VPNQPVYNQPVYNQPVGAAgvPWMPAPQPPL 93
Cdd:pfam03154 423 QLPPPPAQPPVLTQSQ----SLPPPAASHPPTSGLHQVPSQSPFPqhpfVPGGPPPITPPSGPPTSTS--SAMPGIQPPS 496


                  ....
gi 14548191    94 NCPP 97
Cdd:pfam03154 497 SASV 500
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 3-98 5.43e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 38.51  E-value: 5.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191   3 KQNSQMNASHPETNLPVGYPPQYPPTAFQGPPgysGYPGPQVSyppPPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGAAg 82
Cdd:COG5180 332 GQPTERPAGVPEAASDAGQPPSAYPPAEEAVP---GKPLEQGA---PRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPP- 404

                        90
                ....*....|....*.
gi 14548191  83 vpwMPAPQPPLNCPPG 98
Cdd:COG5180 405 ---MGAGDLVQAALDG 417
 
Name Accession Description Interval E-value
Scramblase pfam03803
Scramblase; Scramblase is palmitoylated and contains a potential protein kinase C ...
 86-307 1.10e-124

Scramblase; Scramblase is palmitoylated and contains a potential protein kinase C phosphorylation site. Scramblase exhibits Ca2+-activated phospholipid scrambling activity in vitro. There are also possible SH3 and WW binding motifs. Scramblase is involved in the redistribution of phospholipids after cell activation or injury.


Pssm-ID: 252175  Cd Length: 221  Bit Score: 355.89  E-value: 1.10e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191    86 MPAP-QPPLNCPPGLEYLSQIDQILIHQQIELLEVLTGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRI 164
Cdd:pfam03803   1 MSGPgQPPANCPAGLEYLLQLDQILVHQQIEPLEVFTGFETANRYVVKNVNGQPLYYAMERSNCCARQCCGTHRPFVMRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191   165 IDNMGQEVITLERPLRcSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCCGDVD 244
Cdd:pfam03803  81 TDNFGNEVMTLKRPFS-CISCCPSCLQEQEIQAPPGTTIGEVLQTWHLWRPNYELQNADGNQVLSIFGPCFKCDCGGDWE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14548191   245 FEIKSLDeQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLIDFMFFES 307
Cdd:pfam03803 160 FPVKTAD-GEVVGSISRNWPGLGREAFTDADTYVVRFPLDLDVKLKAVLLGAAFLIDFMYFER 221
YxjI COG4894
Putative phospholipid scramblase YxjI, Tubby2 superfamily [Lipid transport and metabolism];
106-303 9.78e-11

Putative phospholipid scramblase YxjI, Tubby2 superfamily [Lipid transport and metabolism];


Pssm-ID: 443922  Cd Length: 163  Bit Score: 59.47  E-value: 9.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191 106 DQILIHQQIellevltgFETNNKYEIKNSFGQRVYFAAEDtdcctrnccGPSRPFTLRIIDNMGQEVITLERPLrcsscc 185
Cdd:COG4894   2 RTLYIKQKI--------FSLGDDFTIYDENGQPVYLVKGK---------FFSLGDTLSIYDADGNELATIKQKL------ 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191 186 cPCCLQEIEIQApPGVPIGYVIQTWHPCLPKFTIQNEKREdvLKISGPCVvcsccgDVDFEIKSLDEqcVVGKISKHWtg 265
Cdd:COG4894  59 -FSLLPTFEIYD-DGEPVATIKKKFTFFKDRFTIEADGLD--LEIEGDFW------DHDFEITRGGK--VVASVSKKW-- 124

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 14548191 266 ilreaFTDADNFGIQFPldlDVKMKAVMIGACFLIDFM 303
Cdd:COG4894 125 -----FSWRDTYELDID---DEEDRPLVIALAIAIDAV 154
PHA03378 PHA03378
EBNA-3B; Provisional
 22-97 1.06e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.98  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191   22 PPQYPPTAFQGPPGYSGYPGPQVSYPP---PPAGHSGPG--PAGFPVPNQPVYNQPVYNQPvgAAGVPWMPAPQPPLNCP 96
Cdd:PHA03378 706 PPAAPPGRAQRPAAATGRARPPAAAPGrarPPAAAPGRArpPAAAPGRARPPAAAPGRARP--PAAAPGAPTPQPPPQAP 783


                 .
gi 14548191   97 P 97
Cdd:PHA03378 784 P 784
PHA03377 PHA03377
EBNA-3C; Provisional
 10-91 3.14e-04

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 42.35  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191    10 ASHPETNLPVGYPPQYP----------PTAFQGPPGYSGYPGP---QVSYPPPPagHSGPGPagfPVPNQPVYNQPVYNQ 76
Cdd:PHA03377  801 AQHPRYRHSWAYWSQYPghghpqgpwaPRPPHLPPQWDGSAGHgqdQVSQFPHL--QSETGP---PRLQLSQVPQLPYSQ 875

                          90
                  ....*....|....*
gi 14548191    77 PVGAAGVPWMPAPQP 91
Cdd:PHA03377  876 TLVSSSAPSWSSPQP 890
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 13-97 9.72e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 9.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191    13 PETNLPVGYPPQYPPTAFQGP-PGYSGYPGPQVSYPPPPAGHSGPGPAG----FPVPNQPVYNQPVYNQPVG-AAGVPWM 86
Cdd:PRK10263  751 PVQQPQQPVAPQQQYQQPQQPvAPQPQYQQPQQPVAPQPQYQQPQQPVApqpqYQQPQQPVAPQPQYQQPQQpVAPQPQY 830

                          90
                  ....*....|.
gi 14548191    87 PAPQPPLNCPP 97
Cdd:PRK10263  831 QQPQQPVAPQP 841
PHA03378 PHA03378
EBNA-3B; Provisional
 22-97 1.23e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.44  E-value: 1.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14548191   22 PPQYPPTAFQGPPGYSGYPGPQVSYPP---PPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPP 97
Cdd:PHA03378 726 PPAAAPGRARPPAAAPGRARPPAAAPGrarPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGP 804
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 18-97 2.82e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 39.37  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191    18 PVGYPPQYPPTAFQGPpgysGYPGPQVSYPPPPAGHSGPGPAGFP----VPNQPVYNQPVYNQPVGAAgvPWMPAPQPPL 93
Cdd:pfam03154 423 QLPPPPAQPPVLTQSQ----SLPPPAASHPPTSGLHQVPSQSPFPqhpfVPGGPPPITPPSGPPTSTS--SAMPGIQPPS 496


                  ....
gi 14548191    94 NCPP 97
Cdd:pfam03154 497 SASV 500
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 8-87 5.16e-03

MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 37.66  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191     8 MNASHPETNLPVGYP---PQYPPTAFQG----------PPGYSGYPGPqvsYPPPPAGHSGPGPagFPVPNQPvynqpvY 74
Cdd:pfam15822 153 MGGQYPAPNMPYPSPgpyPAVPPPQSPGaappvpwgtvPPGPWGPPAP---YPDPTGSYPMPGL--YPTPNNP------F 221

                          90
                  ....*....|...
gi 14548191    75 NQPVGAAGVPWMP 87
Cdd:pfam15822 222 QVPSGPSGAPPMP 234
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 3-98 5.43e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 38.51  E-value: 5.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191   3 KQNSQMNASHPETNLPVGYPPQYPPTAFQGPPgysGYPGPQVSyppPPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGAAg 82
Cdd:COG5180 332 GQPTERPAGVPEAASDAGQPPSAYPPAEEAVP---GKPLEQGA---PRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPP- 404

                        90
                ....*....|....*.
gi 14548191  83 vpwMPAPQPPLNCPPG 98
Cdd:COG5180 405 ---MGAGDLVQAALDG 417
DUF3824 pfam12868
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It ...
 20-92 8.74e-03

Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It is proline-rich, and the function is not known.


Pssm-ID: 372351 [Multi-domain]  Cd Length: 145  Bit Score: 36.26  E-value: 8.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14548191    20 GYPPQ-YPPTAfQGPPGYSGYPGPQVSYPPPPAGhSGPGPAGFPVPNQPV--YNQPVYNQPVGAAGvPWMPAPQPP 92
Cdd:pfam12868  55 PYSPSpYPPSP-AGPYASQGQYYPETNYFPPPPG-STPQPPVDPQPNAPPppYNPADYPPPPGAAP-PPQPYQYPP 127
dnaA PRK14086
chromosomal replication initiator protein DnaA;
22-103 9.56e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 37.50  E-value: 9.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14548191   22 PPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGAAgvPWMPAP------QPPLNC 95
Cdd:PRK14086  97 PPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARPAYPAYQQRPEPG--AWPRAAddygwqQQRLGF 174


                 ....*...
gi 14548191   96 PPGLEYLS 103
Cdd:PRK14086 175 PPRAPYAS 182
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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