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Conserved domains on  [gi|446522419|ref|WP_000599765|]
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MULTISPECIES: ATP-dependent endonuclease [Salmonella]

Protein Classification

ATP-dependent endonuclease( domain architecture ID 12109662)

OLD (overcoming lysogenization defect)-family ATP-dependent endonuclease may have DNAse as well as RNAse activity; contains a DUF2813 domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF2813 pfam11398
Protein of unknown function (DUF2813); This entry contains YjbD from Escherichia coli, which ...
1-375 0e+00

Protein of unknown function (DUF2813); This entry contains YjbD from Escherichia coli, which is annotated as a nucleotide triphosphate hydrolase.


:

Pssm-ID: 431868 [Multi-domain]  Cd Length: 372  Bit Score: 522.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419    1 MILERVEIVGFRGINRLSLMLEQNNVLIGENAWGKSSLLDALTLLLSPELDLYHFVREDFWFPPGDIKGREHHLHIILTF 80
Cdd:pfam11398   1 MHLERIEVVGFRGINRLSLHFDQLTVLIGENAWGKSSLLDALSLLLNPTKELYQFTLDDFHQPYAIENEPTRHLQIIFTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419   81 RETQPGRHRVRRYRALEACWSPCEDDFHRIFYRLEGECGADGSVMTLRSFLNSDGQPLLVENINDQVRHLVRLMPVLRLR 160
Cdd:pfam11398  81 KESAPGEHKARRYRSLSALWVPHKDGYQRIYYRVEGEINEDGDVTTTRSFLDEDGEPIPLDDIEELVRELISLHPVLRLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419  161 DARfmrRIRNGTVPNVPDVEVTARQLDFLARELATRPQNLTDGQIRQGLSAMVQLLEHYFSEQGAGQARHRLMRRRSQNE 240
Cdd:pfam11398 161 DAR---RLRNGTLDVEYCNSRLERRIDNLARRLITTPQQLSEGELKSGLQAMVQLLDHYFSFQNHRRHNHRNMREILTYG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419  241 QRSWRYLDIINRMIDKPGSRSHRVILLGLFSTLLQAKGTLRLHKDARPLLLVEDPETRLHPIMLSVAWQLLNLLPLQRIA 320
Cdd:pfam11398 238 QKLWNKLKSLNQLLKQDESKSLRLLLLGLLATLLQAKGPVELRRGARPILLLEDPEGRLHPTMLAIAWELLSLLPMQKIL 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446522419  321 TTNSGELLSLTPVEHVVRLVRESSRVAAWRLGPGGLSAEDGRRIAFHIRFNRASS 375
Cdd:pfam11398 318 TTNSSELLSQVPLSSICRLVRESDRTQSYQLGRKSLSREDLRRIAFHIRFNRPLA 372
TOPRIM_OLD cd01026
TOPRIM_OLD: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ...
376-472 7.48e-20

TOPRIM_OLD: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in bacterial and archaeal nucleases of the OLD (overcome lysogenization defect) family. The bacteriophage P2 OLD protein, which has DNase as well as RNase activity, consists of an N-terminal ABC-type ATPase domain and a C-terminal Toprim domain; the nuclease activity of OLD is stimulated by ATP, though the ATPase activity is not DNA-dependent. Functional details on OLD are scant and further experimentation is required to define the relationship between the ATPase and Toprim nuclease domains. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general acid in strand cleavage by nucleases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


:

Pssm-ID: 173776  Cd Length: 97  Bit Score: 84.64  E-value: 7.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419 376 LFARCWLLVEGETETWVINELARQCGHHFDAEGIKVIEFAQSGLKPLVKFARRMGIEWHVLVDGDEAGKKYAATVRSLLN 455
Cdd:cd01026    1 FFADKVILVEGDSEEILLPALAKKLGLDLDEAGISIIPVGGKNFKPFIKLLNALGIPVAVLTDLDAKRNEKKDDAGKGRN 80
                         90
                 ....*....|....*..
gi 446522419 456 NDREEEREHLTALPALD 472
Cdd:cd01026   81 KKLDSKDDVSKNLATLE 97
 
Name Accession Description Interval E-value
DUF2813 pfam11398
Protein of unknown function (DUF2813); This entry contains YjbD from Escherichia coli, which ...
1-375 0e+00

Protein of unknown function (DUF2813); This entry contains YjbD from Escherichia coli, which is annotated as a nucleotide triphosphate hydrolase.


Pssm-ID: 431868 [Multi-domain]  Cd Length: 372  Bit Score: 522.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419    1 MILERVEIVGFRGINRLSLMLEQNNVLIGENAWGKSSLLDALTLLLSPELDLYHFVREDFWFPPGDIKGREHHLHIILTF 80
Cdd:pfam11398   1 MHLERIEVVGFRGINRLSLHFDQLTVLIGENAWGKSSLLDALSLLLNPTKELYQFTLDDFHQPYAIENEPTRHLQIIFTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419   81 RETQPGRHRVRRYRALEACWSPCEDDFHRIFYRLEGECGADGSVMTLRSFLNSDGQPLLVENINDQVRHLVRLMPVLRLR 160
Cdd:pfam11398  81 KESAPGEHKARRYRSLSALWVPHKDGYQRIYYRVEGEINEDGDVTTTRSFLDEDGEPIPLDDIEELVRELISLHPVLRLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419  161 DARfmrRIRNGTVPNVPDVEVTARQLDFLARELATRPQNLTDGQIRQGLSAMVQLLEHYFSEQGAGQARHRLMRRRSQNE 240
Cdd:pfam11398 161 DAR---RLRNGTLDVEYCNSRLERRIDNLARRLITTPQQLSEGELKSGLQAMVQLLDHYFSFQNHRRHNHRNMREILTYG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419  241 QRSWRYLDIINRMIDKPGSRSHRVILLGLFSTLLQAKGTLRLHKDARPLLLVEDPETRLHPIMLSVAWQLLNLLPLQRIA 320
Cdd:pfam11398 238 QKLWNKLKSLNQLLKQDESKSLRLLLLGLLATLLQAKGPVELRRGARPILLLEDPEGRLHPTMLAIAWELLSLLPMQKIL 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446522419  321 TTNSGELLSLTPVEHVVRLVRESSRVAAWRLGPGGLSAEDGRRIAFHIRFNRASS 375
Cdd:pfam11398 318 TTNSSELLSQVPLSSICRLVRESDRTQSYQLGRKSLSREDLRRIAFHIRFNRPLA 372
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
1-457 1.44e-68

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 225.27  E-value: 1.44e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419   1 MILERVEIVGFRGINRLSLMLEQN-NVLIGENAWGKsslldaltlllsPELDLYHFVREDFWFppgDIKGREHHLHIILT 79
Cdd:COG3593    1 MKLEKIKIKNFRSIKDLSIELSDDlTVLVGENNSGKssilea-lrlllGPSSSRKFDEEDFYL---GDDPDLPEIEIELT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419  80 FRETqpgrhrvrryraleacwspceddfhrifyrlegecgadgsvmtLRSFLNSDGQPLLVENINDQVRHLvrlmpvlrl 159
Cdd:COG3593   77 FGSL-------------------------------------------LSRLLRLLLKEEDKEELEEALEEL--------- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419 160 rdarfmrrirngtvpnvpdvevtarqldflarelatrpqnltDGQIRQGLSAMVQLLEHYFSEQGAGqarHRLMRRRSQN 239
Cdd:COG3593  105 ------------------------------------------NEELKEALKALNELLSEYLKELLDG---LDLELELSLD 139
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419 240 EQRSW------RYLDIINRMIDKPGSRSHRVILLGLFSTLLQAKGtlrlhKDARPLLLVEDPETRLHPIMLSVAWQLLNL 313
Cdd:COG3593  140 ELEDLlkslslRIEDGKELPLDRLGSGFQRLILLALLSALAELKR-----APANPILLIEEPEAHLHPQAQRRLLKLLKE 214
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419 314 L---PLQRIATTNSGELLSLTPVEHVVRLVRESSRVAAWRLGPggLSAEDGRRIAFHIRFNRASSLFARCWLLVEGETET 390
Cdd:COG3593  215 LsekPNQVIITTHSPHLLSEVPLENIRRLRRDSGGTTSTKLID--LDDEDLRKLLRYLGVTRSELLFARKVILVEGDTEV 292
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446522419 391 WVINELARQCGHHFDAEGIKVIEFAQ-SGLKPLVKFARRMGIEWHVLVDGDEAGKkyAATVRSLLNND 457
Cdd:COG3593  293 ILLPALARKLGKDLDEEGISIIPVGGkSNLKPLAKLLKALGIPVAVLTDGDEAGK--AETIEKLKEKG 358
TOPRIM_OLD cd01026
TOPRIM_OLD: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ...
376-472 7.48e-20

TOPRIM_OLD: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in bacterial and archaeal nucleases of the OLD (overcome lysogenization defect) family. The bacteriophage P2 OLD protein, which has DNase as well as RNase activity, consists of an N-terminal ABC-type ATPase domain and a C-terminal Toprim domain; the nuclease activity of OLD is stimulated by ATP, though the ATPase activity is not DNA-dependent. Functional details on OLD are scant and further experimentation is required to define the relationship between the ATPase and Toprim nuclease domains. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general acid in strand cleavage by nucleases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 173776  Cd Length: 97  Bit Score: 84.64  E-value: 7.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419 376 LFARCWLLVEGETETWVINELARQCGHHFDAEGIKVIEFAQSGLKPLVKFARRMGIEWHVLVDGDEAGKKYAATVRSLLN 455
Cdd:cd01026    1 FFADKVILVEGDSEEILLPALAKKLGLDLDEAGISIIPVGGKNFKPFIKLLNALGIPVAVLTDLDAKRNEKKDDAGKGRN 80
                         90
                 ....*....|....*..
gi 446522419 456 NDREEEREHLTALPALD 472
Cdd:cd01026   81 KKLDSKDDVSKNLATLE 97
OLD-like_TOPRIM pfam20469
Overcoming lysogenization defect protein-like, TOPRIM domain; This entry represents the ...
376-440 9.70e-17

Overcoming lysogenization defect protein-like, TOPRIM domain; This entry represents the topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in bacterial and archaeal nucleases of the OLD (overcome lysogenization defect) family. The bacteriophage P2 OLD protein, which has DNase as well as RNase activity consists of an N-terminal ABC-type ATPase domain and a C-terminal Toprim domain. The nuclease activity of OLD is stimulated by ATP, though the ATPase activity is not DNA-dependent. The TOPRIM domain has two conserved motifs, one of which centres at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general acid in strand cleavage by nucleases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 466618  Cd Length: 67  Bit Score: 74.73  E-value: 9.70e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446522419  376 LFARCWLLVEGETETWVINELA-RQCGHHFDAEGIKVIE-FAQSGLKPLVKFARRMGIEWHVLVDGD 440
Cdd:pfam20469   1 FFADKVILVEGDTEEILLPALAeKLLGKDLDALGISIVSvGGKGNFKRFLKLLKALGIPVAVITDLD 67
 
Name Accession Description Interval E-value
DUF2813 pfam11398
Protein of unknown function (DUF2813); This entry contains YjbD from Escherichia coli, which ...
1-375 0e+00

Protein of unknown function (DUF2813); This entry contains YjbD from Escherichia coli, which is annotated as a nucleotide triphosphate hydrolase.


Pssm-ID: 431868 [Multi-domain]  Cd Length: 372  Bit Score: 522.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419    1 MILERVEIVGFRGINRLSLMLEQNNVLIGENAWGKSSLLDALTLLLSPELDLYHFVREDFWFPPGDIKGREHHLHIILTF 80
Cdd:pfam11398   1 MHLERIEVVGFRGINRLSLHFDQLTVLIGENAWGKSSLLDALSLLLNPTKELYQFTLDDFHQPYAIENEPTRHLQIIFTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419   81 RETQPGRHRVRRYRALEACWSPCEDDFHRIFYRLEGECGADGSVMTLRSFLNSDGQPLLVENINDQVRHLVRLMPVLRLR 160
Cdd:pfam11398  81 KESAPGEHKARRYRSLSALWVPHKDGYQRIYYRVEGEINEDGDVTTTRSFLDEDGEPIPLDDIEELVRELISLHPVLRLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419  161 DARfmrRIRNGTVPNVPDVEVTARQLDFLARELATRPQNLTDGQIRQGLSAMVQLLEHYFSEQGAGQARHRLMRRRSQNE 240
Cdd:pfam11398 161 DAR---RLRNGTLDVEYCNSRLERRIDNLARRLITTPQQLSEGELKSGLQAMVQLLDHYFSFQNHRRHNHRNMREILTYG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419  241 QRSWRYLDIINRMIDKPGSRSHRVILLGLFSTLLQAKGTLRLHKDARPLLLVEDPETRLHPIMLSVAWQLLNLLPLQRIA 320
Cdd:pfam11398 238 QKLWNKLKSLNQLLKQDESKSLRLLLLGLLATLLQAKGPVELRRGARPILLLEDPEGRLHPTMLAIAWELLSLLPMQKIL 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446522419  321 TTNSGELLSLTPVEHVVRLVRESSRVAAWRLGPGGLSAEDGRRIAFHIRFNRASS 375
Cdd:pfam11398 318 TTNSSELLSQVPLSSICRLVRESDRTQSYQLGRKSLSREDLRRIAFHIRFNRPLA 372
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
1-457 1.44e-68

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 225.27  E-value: 1.44e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419   1 MILERVEIVGFRGINRLSLMLEQN-NVLIGENAWGKsslldaltlllsPELDLYHFVREDFWFppgDIKGREHHLHIILT 79
Cdd:COG3593    1 MKLEKIKIKNFRSIKDLSIELSDDlTVLVGENNSGKssilea-lrlllGPSSSRKFDEEDFYL---GDDPDLPEIEIELT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419  80 FRETqpgrhrvrryraleacwspceddfhrifyrlegecgadgsvmtLRSFLNSDGQPLLVENINDQVRHLvrlmpvlrl 159
Cdd:COG3593   77 FGSL-------------------------------------------LSRLLRLLLKEEDKEELEEALEEL--------- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419 160 rdarfmrrirngtvpnvpdvevtarqldflarelatrpqnltDGQIRQGLSAMVQLLEHYFSEQGAGqarHRLMRRRSQN 239
Cdd:COG3593  105 ------------------------------------------NEELKEALKALNELLSEYLKELLDG---LDLELELSLD 139
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419 240 EQRSW------RYLDIINRMIDKPGSRSHRVILLGLFSTLLQAKGtlrlhKDARPLLLVEDPETRLHPIMLSVAWQLLNL 313
Cdd:COG3593  140 ELEDLlkslslRIEDGKELPLDRLGSGFQRLILLALLSALAELKR-----APANPILLIEEPEAHLHPQAQRRLLKLLKE 214
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419 314 L---PLQRIATTNSGELLSLTPVEHVVRLVRESSRVAAWRLGPggLSAEDGRRIAFHIRFNRASSLFARCWLLVEGETET 390
Cdd:COG3593  215 LsekPNQVIITTHSPHLLSEVPLENIRRLRRDSGGTTSTKLID--LDDEDLRKLLRYLGVTRSELLFARKVILVEGDTEV 292
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446522419 391 WVINELARQCGHHFDAEGIKVIEFAQ-SGLKPLVKFARRMGIEWHVLVDGDEAGKkyAATVRSLLNND 457
Cdd:COG3593  293 ILLPALARKLGKDLDEEGISIIPVGGkSNLKPLAKLLKALGIPVAVLTDGDEAGK--AETIEKLKEKG 358
TOPRIM_OLD cd01026
TOPRIM_OLD: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ...
376-472 7.48e-20

TOPRIM_OLD: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in bacterial and archaeal nucleases of the OLD (overcome lysogenization defect) family. The bacteriophage P2 OLD protein, which has DNase as well as RNase activity, consists of an N-terminal ABC-type ATPase domain and a C-terminal Toprim domain; the nuclease activity of OLD is stimulated by ATP, though the ATPase activity is not DNA-dependent. Functional details on OLD are scant and further experimentation is required to define the relationship between the ATPase and Toprim nuclease domains. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general acid in strand cleavage by nucleases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 173776  Cd Length: 97  Bit Score: 84.64  E-value: 7.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522419 376 LFARCWLLVEGETETWVINELARQCGHHFDAEGIKVIEFAQSGLKPLVKFARRMGIEWHVLVDGDEAGKKYAATVRSLLN 455
Cdd:cd01026    1 FFADKVILVEGDSEEILLPALAKKLGLDLDEAGISIIPVGGKNFKPFIKLLNALGIPVAVLTDLDAKRNEKKDDAGKGRN 80
                         90
                 ....*....|....*..
gi 446522419 456 NDREEEREHLTALPALD 472
Cdd:cd01026   81 KKLDSKDDVSKNLATLE 97
OLD-like_TOPRIM pfam20469
Overcoming lysogenization defect protein-like, TOPRIM domain; This entry represents the ...
376-440 9.70e-17

Overcoming lysogenization defect protein-like, TOPRIM domain; This entry represents the topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in bacterial and archaeal nucleases of the OLD (overcome lysogenization defect) family. The bacteriophage P2 OLD protein, which has DNase as well as RNase activity consists of an N-terminal ABC-type ATPase domain and a C-terminal Toprim domain. The nuclease activity of OLD is stimulated by ATP, though the ATPase activity is not DNA-dependent. The TOPRIM domain has two conserved motifs, one of which centres at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general acid in strand cleavage by nucleases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 466618  Cd Length: 67  Bit Score: 74.73  E-value: 9.70e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446522419  376 LFARCWLLVEGETETWVINELA-RQCGHHFDAEGIKVIE-FAQSGLKPLVKFARRMGIEWHVLVDGD 440
Cdd:pfam20469   1 FFADKVILVEGDTEEILLPALAeKLLGKDLDALGISIVSvGGKGNFKRFLKLLKALGIPVAVITDLD 67
 
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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