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Conserved domains on  [gi|1113584791|gb|OJY44287|]
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restriction endonuclease [Rhizobiales bacterium 64-17]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SgrAI-like cd22360
Restriction endonuclease SgrAI and similar nucleases; The type II restriction endonuclease ...
21-292 2.18e-173

Restriction endonuclease SgrAI and similar nucleases; The type II restriction endonuclease SgrAI binds and cleaves the target sequence CR|CCGGYG (| denotes the cleavage site, R stands for a purine and Y stands for a pyrimidine). 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: 411764  Cd Length: 272  Bit Score: 479.97  E-value: 2.18e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113584791  21 TFGEYLGQFRSNAHGALSVLYGAGFAFSGSALAKVEGDVFELMEAGAIWNAFAAWNKFMDGLPWPSKVFTTPNGTVATPS 100
Cdd:cd22360     1 PFREYLRQPISNADTAGELLFGGDFNVDSNAKAKVEGDIYETLEAAALWNAAAAWNSFMDTGNWPSSPFYAPPGAVPSPR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113584791 101 RKAAILKLPRGYDTTRLFKSEVRTRIQAHEQALKLRGMELGLSSPDIVGIRIPDPMPPEFAPFLDPLPNLGEQARLILEK 180
Cdd:cd22360    81 RQVAIVNLPRGYDWTRLLNPEARAAIEAFRAALRLRGLELPLSTPDIAGVRLPDPMPEGDDPFRTPLPDLTRPNQRILEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113584791 181 THEKLEGTLEGRSFLFAIAVKRTTRSDRLYQPLFEANVLKYLIEEVLRGAAFRFHVHMGSFEGADVEGHYNAASLVSLMR 260
Cdd:cd22360   161 AHQLLEGTVEPGEFLLAIAVKRSLRSDRLYQPLFEANVLKYLLEEVLRGPAVRFEVHTLSFEGADVEGIYKAASLISLAR 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1113584791 261 GGEPTKAVTSTYLAERPVECAQTILNDLPLFP 292
Cdd:cd22360   241 GGTPHKAIDELYLAETPLARAQFALNDQPLFP 272
 
Name Accession Description Interval E-value
SgrAI-like cd22360
Restriction endonuclease SgrAI and similar nucleases; The type II restriction endonuclease ...
21-292 2.18e-173

Restriction endonuclease SgrAI and similar nucleases; The type II restriction endonuclease SgrAI binds and cleaves the target sequence CR|CCGGYG (| denotes the cleavage site, R stands for a purine and Y stands for a pyrimidine). 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: 411764  Cd Length: 272  Bit Score: 479.97  E-value: 2.18e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113584791  21 TFGEYLGQFRSNAHGALSVLYGAGFAFSGSALAKVEGDVFELMEAGAIWNAFAAWNKFMDGLPWPSKVFTTPNGTVATPS 100
Cdd:cd22360     1 PFREYLRQPISNADTAGELLFGGDFNVDSNAKAKVEGDIYETLEAAALWNAAAAWNSFMDTGNWPSSPFYAPPGAVPSPR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113584791 101 RKAAILKLPRGYDTTRLFKSEVRTRIQAHEQALKLRGMELGLSSPDIVGIRIPDPMPPEFAPFLDPLPNLGEQARLILEK 180
Cdd:cd22360    81 RQVAIVNLPRGYDWTRLLNPEARAAIEAFRAALRLRGLELPLSTPDIAGVRLPDPMPEGDDPFRTPLPDLTRPNQRILEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113584791 181 THEKLEGTLEGRSFLFAIAVKRTTRSDRLYQPLFEANVLKYLIEEVLRGAAFRFHVHMGSFEGADVEGHYNAASLVSLMR 260
Cdd:cd22360   161 AHQLLEGTVEPGEFLLAIAVKRSLRSDRLYQPLFEANVLKYLLEEVLRGPAVRFEVHTLSFEGADVEGIYKAASLISLAR 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1113584791 261 GGEPTKAVTSTYLAERPVECAQTILNDLPLFP 292
Cdd:cd22360   241 GGTPHKAIDELYLAETPLARAQFALNDQPLFP 272
 
Name Accession Description Interval E-value
SgrAI-like cd22360
Restriction endonuclease SgrAI and similar nucleases; The type II restriction endonuclease ...
21-292 2.18e-173

Restriction endonuclease SgrAI and similar nucleases; The type II restriction endonuclease SgrAI binds and cleaves the target sequence CR|CCGGYG (| denotes the cleavage site, R stands for a purine and Y stands for a pyrimidine). 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: 411764  Cd Length: 272  Bit Score: 479.97  E-value: 2.18e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113584791  21 TFGEYLGQFRSNAHGALSVLYGAGFAFSGSALAKVEGDVFELMEAGAIWNAFAAWNKFMDGLPWPSKVFTTPNGTVATPS 100
Cdd:cd22360     1 PFREYLRQPISNADTAGELLFGGDFNVDSNAKAKVEGDIYETLEAAALWNAAAAWNSFMDTGNWPSSPFYAPPGAVPSPR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113584791 101 RKAAILKLPRGYDTTRLFKSEVRTRIQAHEQALKLRGMELGLSSPDIVGIRIPDPMPPEFAPFLDPLPNLGEQARLILEK 180
Cdd:cd22360    81 RQVAIVNLPRGYDWTRLLNPEARAAIEAFRAALRLRGLELPLSTPDIAGVRLPDPMPEGDDPFRTPLPDLTRPNQRILEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113584791 181 THEKLEGTLEGRSFLFAIAVKRTTRSDRLYQPLFEANVLKYLIEEVLRGAAFRFHVHMGSFEGADVEGHYNAASLVSLMR 260
Cdd:cd22360   161 AHQLLEGTVEPGEFLLAIAVKRSLRSDRLYQPLFEANVLKYLLEEVLRGPAVRFEVHTLSFEGADVEGIYKAASLISLAR 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1113584791 261 GGEPTKAVTSTYLAERPVECAQTILNDLPLFP 292
Cdd:cd22360   241 GGTPHKAIDELYLAETPLARAQFALNDQPLFP 272
Bse634I-like cd22314
Restriction endonuclease Bse634I and similar endonucleases; Bacillus stearothermophilus ...
4-273 5.15e-16

Restriction endonuclease Bse634I and similar endonucleases; Bacillus stearothermophilus restriction endonuclease Bse634I recognizes the nucleotide sequence R|CCGGY (R = A or G, Y = T or C, with | designating the cleavage site) and is an isoschisomer of Citrobacter freundii restriction endonuclease Cfr10I; it is active as a homotetramer and 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: 411718  Cd Length: 281  Bit Score: 76.14  E-value: 5.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113584791   4 TFGDFMPGTDNDPDPTRTFGEYLGQFRSNA---HGALSVlygagfafSGSALAKVEGDVFELMEAGAIWNAFAawnkfmd 80
Cdd:cd22314    19 AFRNLYSSIVLPNGSISEILDEIQNFVKKAakeKGLQNP--------SQGALNNCRGDWYEWIIAIIAWNYFI------- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113584791  81 glpwpskvfttpngtvaTPSRKAAILKLP--RGYDTTRLFKSEVRTRIQAHEQALKL-RGMELGLSSPDIVGIRIPDPmp 157
Cdd:cd22314    84 -----------------KNENNYLIIKLPniSSFDFAKLYDPELFEYINDLRAKLKSsSDVELITSNPDFVIIDIKDL-- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113584791 158 pEFAPFLDPLPNLGEQARLILEKTHEKLEGTLEGRSFLFAIAVKRTTRSDRLYQPLFEANVLKYLI------EEVLRGAA 231
Cdd:cd22314   145 -ELSLPDKPITNLSLDTLSDLDNLYKDFIGKCELDDIKGYISLKTSLRPDRRLQIVHEGSLLKALYahlqtrSWIINPKG 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1113584791 232 FRFHVHMGSFEGADVEGHYNAA--SLVSLMRggEPTKAVTSTYL 273
Cdd:cd22314   224 IKYYAASSKVSNADREALKTAAthSIVNVES--LPERAVDELFE 265
 
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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