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Conserved domains on  [gi|491021441|ref|WP_004883140|]
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MULTISPECIES: type II restriction endonuclease [Enterobacteriaceae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EcoRII-C super family cl07580
EcoRII C terminal; The C-terminal catalytic domain of the Restriction Endonuclease EcoRII has ...
 228-392 2.32e-88

EcoRII C terminal; The C-terminal catalytic domain of the Restriction Endonuclease EcoRII has a restriction endonuclease-like fold with a central five-stranded mixed beta-sheet surrounded on both sides by alpha-helices. It cleaves DNA specifically at single 5' CCWGG sites.


The actual alignment was detected with superfamily member pfam09019:

Pssm-ID: 401096  Cd Length: 165  Bit Score: 264.64  E-value: 2.32e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441  228 FLAVEELHVLGQIAKGFAT-VNDFITLANSVSNRRKSRAGKSLELHLESLFTEHGaTSFETQATTEGKKKPDFIFPSGAA 306
Cdd:pfam09019   1 FRLYERAIVQERLRSGFGIdVDSFISFALSVLNRRKSRAGKSLENHLEEIFDAFG-LPFETQAVTENKKKPDFLFPSQAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441  307 YRDPDYPAERLRMLGVKTTCKDRWRQVLNEANRIDTVHLFTLQQGVSVAQFREMQAEGIRLVVPEGLHKAFPEEIRGELM 386
Cdd:pfam09019  80 YHDPAFPEEKLRMLAAKTTCKDRWRQVLAEADRIKDKHLLTLQPGISETQTTEMSDHGLQLVVPSEIHRSYPDAQRTELL 159


                  ....*.
gi 491021441  387 SLSAFI 392
Cdd:pfam09019 160 TFEDFI 165
BfiI_C_EcoRII_N_B3 super family cl15242
DNA binding domains of BfiI, EcoRII and plant B3 proteins; This family contains the N-terminal ...
 18-158 4.07e-59

DNA binding domains of BfiI, EcoRII and plant B3 proteins; This family contains the N-terminal DNA binding domain of type IIE restriction endonuclease EcoRII-like proteins, the C-terminal DNA binding domain of type IIS restriction endonuclease BfiI-like proteins and plant-specific B3 proteins. Type II restriction endonucleases are components of restriction modification (RM) systems that protect bacteria and archaea against invading foreign DNA. They usually function as homodimers or homotetramers that cleave DNA at defined sites of 4 to 8 bp in length, and they require Mg2+, not ATP or GTP, for catalysis. EcoRII is specific for the 5'-CCWGG sequence (W stands for A or T). EcoRII consists of 2 domains, the C-terminal catalytic/dimerization domain (EcoRII-C), and the N-terminal effector DNA binding domain (EcoRII-N). BfiI is unique in cleaving DNA at fixed positions downstream of an asymmetric sequence in the absence of Mg2+. BfiI consists of two discrete domains with distinct functions: an N-terminal catalytic domain with non-specific nuclease activity and dimerization function that is more closely related to Nuc, an EDTA-resistant nuclease from the phospholipase D (PLD) superfamily; and a C-terminal domain that specifically recognizes its target sequences, 5'-ACTGGG-3'. B3 proteins are a family of plant-specific transcription factors, involved in a great variety of processes, including seed development and auxin response.


The actual alignment was detected with superfamily member pfam09217:

Pssm-ID: 449517  Cd Length: 148  Bit Score: 189.24  E-value: 4.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441   18 VFVKRLSANDTGATKSHQSGLYMPGAVIDELFPSLRDTQLRNPEALFSVHVSSHpDCPDLNdVRAIYYNNKFFGGTRDEK 97
Cdd:pfam09217   7 WFAKRLSANDTGATGAHQAGPYIPKHFLDTLFPSLNHPEDTNPSISFKLNIDSH-SVERSE-IRAIYYNNRLRGKTRNEA 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491021441   98 RLTGFGK-QNPLQNPENTGALALLAFDHMPGTSSSYCDVWVCKDLSEEEILEPIIGEVIPGA 158
Cdd:pfam09217  85 RITGFGGgKSPLLDPENTGALLVLAFAPHKDGDQMLCHAWVCRNSSEEDLLEIFIGEILPGS 146
 
Name Accession Description Interval E-value
EcoRII-C pfam09019
EcoRII C terminal; The C-terminal catalytic domain of the Restriction Endonuclease EcoRII has ...
 228-392 2.32e-88

EcoRII C terminal; The C-terminal catalytic domain of the Restriction Endonuclease EcoRII has a restriction endonuclease-like fold with a central five-stranded mixed beta-sheet surrounded on both sides by alpha-helices. It cleaves DNA specifically at single 5' CCWGG sites.


Pssm-ID: 401096  Cd Length: 165  Bit Score: 264.64  E-value: 2.32e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441  228 FLAVEELHVLGQIAKGFAT-VNDFITLANSVSNRRKSRAGKSLELHLESLFTEHGaTSFETQATTEGKKKPDFIFPSGAA 306
Cdd:pfam09019   1 FRLYERAIVQERLRSGFGIdVDSFISFALSVLNRRKSRAGKSLENHLEEIFDAFG-LPFETQAVTENKKKPDFLFPSQAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441  307 YRDPDYPAERLRMLGVKTTCKDRWRQVLNEANRIDTVHLFTLQQGVSVAQFREMQAEGIRLVVPEGLHKAFPEEIRGELM 386
Cdd:pfam09019  80 YHDPAFPEEKLRMLAAKTTCKDRWRQVLAEADRIKDKHLLTLQPGISETQTTEMSDHGLQLVVPSEIHRSYPDAQRTELL 159


                  ....*.
gi 491021441  387 SLSAFI 392
Cdd:pfam09019 160 TFEDFI 165
EcoRII-like cd22322
Restriction endonuclease EcoRII and similar endonucleases; Restriction endonuclease EcoRII ...
 187-394 7.38e-69

Restriction endonuclease EcoRII and similar endonucleases; Restriction endonuclease EcoRII recognizes the sequence 5'-CCWGG-3' (W stands for A or T); it requires binding of a second target site as an allosteric effector in order to be active. EcoRII belongs to a superfamily of nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI.


Pssm-ID: 411726  Cd Length: 211  Bit Score: 216.41  E-value: 7.38e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441 187 EWNHYFPSGREIIGFAACHYDKKtSDPDTQLTRRRKIEFEIFLAVEELHVLGQIAKGFAT----VNDFITLANSVSNRRK 262
Cdd:cd22322    1 DPFEIKPPGDAIFKITRDIEVKF-LNFSLLLRDMQRVEYALFLLIEEATGQDAIRSVIEVltidFDELDRVFLSASQSRK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441 263 SRAGKSLELHLESLFTEHGAtSFETQATTEGKKkPDFIFPSGAAYRDPDYPAERLRMLGVKTTCKDRWRQVLNEANRIDT 342
Cdd:cd22322   80 SRAGKSFELHIEALLKAGGI-PFEEQAVIEGKR-PDFVLPSLDAYKDPTRNPEDALILSAKTTLRERWRQVVTEAKRICQ 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491021441 343 VHLFTLQQGVSVAQFREMQAEGIRLVVPEGLHKAFPEEIRGELMSLSAFINE 394
Cdd:cd22322  158 FYLATVDEKVSSAQLDEMREHGIYLVVPESLKKSYYTAERANVISFEDFFDE 209
EcoRII-N pfam09217
Restriction endonuclease EcoRII, N-terminal; The N-terminal effector-binding domain of the ...
 18-158 4.07e-59

Restriction endonuclease EcoRII, N-terminal; The N-terminal effector-binding domain of the Restriction Endonuclease EcoRII has a DNA recognition fold, allowing for binding to 5'-CCWGG sequences. It assumes a structure composed of an eight-stranded beta-sheet with the strands in the order of b2, b5, b4, b3, b7, b6, b1 and b8. They are mostly antiparallel to each other except that b3 is parallel to b7. Alternatively, it may also be viewed as consisting of two mini beta-sheets of four antiparallel beta-strands, sheet I from beta-strands b2, b5, b4, b3 and sheet II from strands b7, b6, b1, b8, folded into an open mixed beta-barrel with a novel topology. Sheet I has a simple Greek key motif while sheet II does not.


Pssm-ID: 430469  Cd Length: 148  Bit Score: 189.24  E-value: 4.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441   18 VFVKRLSANDTGATKSHQSGLYMPGAVIDELFPSLRDTQLRNPEALFSVHVSSHpDCPDLNdVRAIYYNNKFFGGTRDEK 97
Cdd:pfam09217   7 WFAKRLSANDTGATGAHQAGPYIPKHFLDTLFPSLNHPEDTNPSISFKLNIDSH-SVERSE-IRAIYYNNRLRGKTRNEA 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491021441   98 RLTGFGK-QNPLQNPENTGALALLAFDHMPGTSSSYCDVWVCKDLSEEEILEPIIGEVIPGA 158
Cdd:pfam09217  85 RITGFGGgKSPLLDPENTGALLVLAFAPHKDGDQMLCHAWVCRNSSEEDLLEIFIGEILPGS 146
EcoRII_N cd10016
N-terminal domain of type IIE restriction endonuclease EcoRII and similar proteins; N-terminal ...
 15-162 5.02e-50

N-terminal domain of type IIE restriction endonuclease EcoRII and similar proteins; N-terminal domain of type IIE restriction endonuclease EcoRII and similar proteins. Type II restriction endonucleases are components of restriction modification (RM) systems that protect bacteria and archaea against invading foreign DNA. They usually function as homodimers or homotetramers that cleave DNA at defined sites of 4 to 8 bp in length, and they require Mg2+, not ATP or GTP, for catalysis. EcoRII is specific for the 5'-CCWGG sequence (W stands for A or T). EcoRII consists of 2 domains, the C-terminal catalytic/dimerization domain (EcoRII-C), and the N-terminal effector DNA binding domain (EcoRII-N). To be catalytically active, EcoRII has to form a dimer.


Pssm-ID: 197382  Cd Length: 142  Bit Score: 165.24  E-value: 5.02e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441  15 NVWVFVKRLSANDTGATKSHQSGLYMPGAVIDELFPSLRdTQLRNPEALFSVHVSSHPDcpDLNDVRAIYYNNKFFGGTR 94
Cdd:cd10016    2 SIQVYCKRLSANDTGATGGHQAGIYIPKSAAELLFPSNH-PDEKNPNPDLTAKISSHDG--PTTESRFIYYNNGLFGGTR 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491021441  95 DEKRLTGFGKQNPLQNPENTGALALLAFdhmpgtSSSYCD---VWVCKDLSEEEILEPIIgEVIPGATIFG 162
Cdd:cd10016   79 NEYRITRFGKGFPFLDPDNTGALLVLAF------QSSDCDlysVWVCRSDEEEDEFEAEI-EVLPGALNLL 142
 
Name Accession Description Interval E-value
EcoRII-C pfam09019
EcoRII C terminal; The C-terminal catalytic domain of the Restriction Endonuclease EcoRII has ...
 228-392 2.32e-88

EcoRII C terminal; The C-terminal catalytic domain of the Restriction Endonuclease EcoRII has a restriction endonuclease-like fold with a central five-stranded mixed beta-sheet surrounded on both sides by alpha-helices. It cleaves DNA specifically at single 5' CCWGG sites.


Pssm-ID: 401096  Cd Length: 165  Bit Score: 264.64  E-value: 2.32e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441  228 FLAVEELHVLGQIAKGFAT-VNDFITLANSVSNRRKSRAGKSLELHLESLFTEHGaTSFETQATTEGKKKPDFIFPSGAA 306
Cdd:pfam09019   1 FRLYERAIVQERLRSGFGIdVDSFISFALSVLNRRKSRAGKSLENHLEEIFDAFG-LPFETQAVTENKKKPDFLFPSQAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441  307 YRDPDYPAERLRMLGVKTTCKDRWRQVLNEANRIDTVHLFTLQQGVSVAQFREMQAEGIRLVVPEGLHKAFPEEIRGELM 386
Cdd:pfam09019  80 YHDPAFPEEKLRMLAAKTTCKDRWRQVLAEADRIKDKHLLTLQPGISETQTTEMSDHGLQLVVPSEIHRSYPDAQRTELL 159


                  ....*.
gi 491021441  387 SLSAFI 392
Cdd:pfam09019 160 TFEDFI 165
EcoRII-like cd22322
Restriction endonuclease EcoRII and similar endonucleases; Restriction endonuclease EcoRII ...
 187-394 7.38e-69

Restriction endonuclease EcoRII and similar endonucleases; Restriction endonuclease EcoRII recognizes the sequence 5'-CCWGG-3' (W stands for A or T); it requires binding of a second target site as an allosteric effector in order to be active. EcoRII belongs to a superfamily of nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI.


Pssm-ID: 411726  Cd Length: 211  Bit Score: 216.41  E-value: 7.38e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441 187 EWNHYFPSGREIIGFAACHYDKKtSDPDTQLTRRRKIEFEIFLAVEELHVLGQIAKGFAT----VNDFITLANSVSNRRK 262
Cdd:cd22322    1 DPFEIKPPGDAIFKITRDIEVKF-LNFSLLLRDMQRVEYALFLLIEEATGQDAIRSVIEVltidFDELDRVFLSASQSRK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441 263 SRAGKSLELHLESLFTEHGAtSFETQATTEGKKkPDFIFPSGAAYRDPDYPAERLRMLGVKTTCKDRWRQVLNEANRIDT 342
Cdd:cd22322   80 SRAGKSFELHIEALLKAGGI-PFEEQAVIEGKR-PDFVLPSLDAYKDPTRNPEDALILSAKTTLRERWRQVVTEAKRICQ 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491021441 343 VHLFTLQQGVSVAQFREMQAEGIRLVVPEGLHKAFPEEIRGELMSLSAFINE 394
Cdd:cd22322  158 FYLATVDEKVSSAQLDEMREHGIYLVVPESLKKSYYTAERANVISFEDFFDE 209
EcoRII-N pfam09217
Restriction endonuclease EcoRII, N-terminal; The N-terminal effector-binding domain of the ...
 18-158 4.07e-59

Restriction endonuclease EcoRII, N-terminal; The N-terminal effector-binding domain of the Restriction Endonuclease EcoRII has a DNA recognition fold, allowing for binding to 5'-CCWGG sequences. It assumes a structure composed of an eight-stranded beta-sheet with the strands in the order of b2, b5, b4, b3, b7, b6, b1 and b8. They are mostly antiparallel to each other except that b3 is parallel to b7. Alternatively, it may also be viewed as consisting of two mini beta-sheets of four antiparallel beta-strands, sheet I from beta-strands b2, b5, b4, b3 and sheet II from strands b7, b6, b1, b8, folded into an open mixed beta-barrel with a novel topology. Sheet I has a simple Greek key motif while sheet II does not.


Pssm-ID: 430469  Cd Length: 148  Bit Score: 189.24  E-value: 4.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441   18 VFVKRLSANDTGATKSHQSGLYMPGAVIDELFPSLRDTQLRNPEALFSVHVSSHpDCPDLNdVRAIYYNNKFFGGTRDEK 97
Cdd:pfam09217   7 WFAKRLSANDTGATGAHQAGPYIPKHFLDTLFPSLNHPEDTNPSISFKLNIDSH-SVERSE-IRAIYYNNRLRGKTRNEA 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491021441   98 RLTGFGK-QNPLQNPENTGALALLAFDHMPGTSSSYCDVWVCKDLSEEEILEPIIGEVIPGA 158
Cdd:pfam09217  85 RITGFGGgKSPLLDPENTGALLVLAFAPHKDGDQMLCHAWVCRNSSEEDLLEIFIGEILPGS 146
EcoRII_N cd10016
N-terminal domain of type IIE restriction endonuclease EcoRII and similar proteins; N-terminal ...
 15-162 5.02e-50

N-terminal domain of type IIE restriction endonuclease EcoRII and similar proteins; N-terminal domain of type IIE restriction endonuclease EcoRII and similar proteins. Type II restriction endonucleases are components of restriction modification (RM) systems that protect bacteria and archaea against invading foreign DNA. They usually function as homodimers or homotetramers that cleave DNA at defined sites of 4 to 8 bp in length, and they require Mg2+, not ATP or GTP, for catalysis. EcoRII is specific for the 5'-CCWGG sequence (W stands for A or T). EcoRII consists of 2 domains, the C-terminal catalytic/dimerization domain (EcoRII-C), and the N-terminal effector DNA binding domain (EcoRII-N). To be catalytically active, EcoRII has to form a dimer.


Pssm-ID: 197382  Cd Length: 142  Bit Score: 165.24  E-value: 5.02e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441  15 NVWVFVKRLSANDTGATKSHQSGLYMPGAVIDELFPSLRdTQLRNPEALFSVHVSSHPDcpDLNDVRAIYYNNKFFGGTR 94
Cdd:cd10016    2 SIQVYCKRLSANDTGATGGHQAGIYIPKSAAELLFPSNH-PDEKNPNPDLTAKISSHDG--PTTESRFIYYNNGLFGGTR 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491021441  95 DEKRLTGFGKQNPLQNPENTGALALLAFdhmpgtSSSYCD---VWVCKDLSEEEILEPIIgEVIPGATIFG 162
Cdd:cd10016   79 NEYRITRFGKGFPFLDPDNTGALLVLAF------QSSDCDlysVWVCRSDEEEDEFEAEI-EVLPGALNLL 142
BfiI_C_EcoRII_N_B3 cd10015
DNA binding domains of BfiI, EcoRII and plant B3 proteins; This family contains the N-terminal ...
 18-123 3.63e-18

DNA binding domains of BfiI, EcoRII and plant B3 proteins; This family contains the N-terminal DNA binding domain of type IIE restriction endonuclease EcoRII-like proteins, the C-terminal DNA binding domain of type IIS restriction endonuclease BfiI-like proteins and plant-specific B3 proteins. Type II restriction endonucleases are components of restriction modification (RM) systems that protect bacteria and archaea against invading foreign DNA. They usually function as homodimers or homotetramers that cleave DNA at defined sites of 4 to 8 bp in length, and they require Mg2+, not ATP or GTP, for catalysis. EcoRII is specific for the 5'-CCWGG sequence (W stands for A or T). EcoRII consists of 2 domains, the C-terminal catalytic/dimerization domain (EcoRII-C), and the N-terminal effector DNA binding domain (EcoRII-N). BfiI is unique in cleaving DNA at fixed positions downstream of an asymmetric sequence in the absence of Mg2+. BfiI consists of two discrete domains with distinct functions: an N-terminal catalytic domain with non-specific nuclease activity and dimerization function that is more closely related to Nuc, an EDTA-resistant nuclease from the phospholipase D (PLD) superfamily; and a C-terminal domain that specifically recognizes its target sequences, 5'-ACTGGG-3'. B3 proteins are a family of plant-specific transcription factors, involved in a great variety of processes, including seed development and auxin response.


Pssm-ID: 197381  Cd Length: 109  Bit Score: 79.60  E-value: 3.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441  18 VFVKRLSANDTGATKSHQSGLYMPGAVIDELFPSLRDTQLRNPEALFSVHVSShpDCPDLNdVRAIYYNNKffggtRDEK 97
Cdd:cd10015    2 VLIKRLSANDTGATGGHQVGLYIPKGIVEKFPPSINHTREANPSIFLTMHDIS--DCRDWE-ARAIFYNSN-----RNEK 73

                         90       100
                 ....*....|....*....|....*.
gi 491021441  98 RLTGFGKQNPLQNPENTGALALLAFD 123
Cdd:cd10015   74 RLTRGGRGFVKQNPLNTGDLTLIAFD 99
Ecl18kI-like cd22320
Restriction endonuclease Ecl18kI and similar endonucleases; Restriction endonuclease Ecl18kI ...
 250-398 7.65e-10

Restriction endonuclease Ecl18kI and similar endonucleases; Restriction endonuclease Ecl18kI recognizes the sequence |CCNGG and cleaves it before the outer C (| designates the cleavage site) to generate 5 nt 5'-overhangs. It belongs to a superfamily of nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI.


Pssm-ID: 411724  Cd Length: 262  Bit Score: 59.19  E-value: 7.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441 250 FITLANSVSNRRKSRAGKSLELHLESLFtEHGATSFETQA-------TTEG-KKKPDFIFPSGAAYRdpdypAERLR-ML 320
Cdd:cd22320  105 IYELSLSNTQSRRSRAGKEFEAIIELLL-IGAGIPFDSQGnigkkifEEKGlGKLVDSVSPGVIEYE-----INKRKtVL 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441 321 G-VKTTCKDRWRQVLNEANR--IDTVHLFTLQQGVSVAQFREMQAEGIRLVVPEGlHKAFPEEIRGELMSLSAFINEIKE 397
Cdd:cd22320  179 IsMKTTLRERWQEVPEEINRtgAPEMYLLTLDEKISKNKIDTLYEHNIILVVTKS-VKEKYYKNNNRVLTFEELLEELID 257


                 .
gi 491021441 398 L 398
Cdd:cd22320  258 I 258
PspGI-like cd22350
Restriction endonuclease PspGI and similar nucleases; PspGI is an isoschizomer of EcoRII, it ...
 253-337 9.41e-03

Restriction endonuclease PspGI and similar nucleases; PspGI is an isoschizomer of EcoRII, it recognizes and cleaves the DNA sequence 5'-|CCWGG-3' (| denotes the cleavage site, W stands for A or T). It belongs to a superfamily of nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI.


Pssm-ID: 411754  Cd Length: 239  Bit Score: 37.31  E-value: 9.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491021441 253 LANSVSNRRKSRAGKSLELHLESLFTEHGATSFETQAT------TEGKKkPDFIFPSGAAY-RDPDYPAerlrMLGVKTT 325
Cdd:cd22350   69 LEQSFQQARFSRGGKAFEIIFTKLLNKFGIRYEHDRVIkiydyiTEGEK-PDFIIPSVRTFlNDPSSAI----LITVKRK 143

                         90
                 ....*....|..
gi 491021441 326 CKDRWRQVLNEA 337
Cdd:cd22350  144 VRERWREAVGEA 155
 
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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