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hsdS

Gene
hsdS
Protein
Type-1 restriction enzyme EcoEI specificity protein
Organism
Escherichia coli
Length
594 amino acids
Function
The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. Subunit S dictates DNA sequences specificity. The EcoEI enzyme recognizes 5'-GAGN(7)ATGC-3'.
Similarity
Belongs to the type-I restriction system S methylase family.
Mass
66.344 kDa
Sequence
MAVEKLITDHIDIWSSALQTRSMAGRGSNGKIDLYGIKKLRELILELAVRGKLVPQDPNDEPASELLKRIAAEKTELVKQGKIKKQKPLLRISEDEKPFELPEGWEWITLSEIATINPKIEVTDDEQEISFVPMPCISTRFDGAHDQEIKKWGEVKKGYTHFADGDIALAKITPCFENSKAVIFKGLKGGVGVGTTELHVARPISSELNLQYILLNIKSPHYLSMGESMMTGSAGQKRVPRSFFENYPIPFPPNTEQARIVGTFSKLMFLCDQLEQQSLTSLDAHQQLVETLLATLTDSQNAEELAENWARISQYFDTLFTTEASIDALKQTILQLAVMGKLVSQDPNDEPASELLKRVEQEKVQLVKEGKIKKQKPLPPVSDDEKPFELPIGWEWCRIGEIIANMDAGWSPACSPEPSPNEDIWGVLKTTAVQSLEYREQENKTLPNSKLPRPQYEVHDGDILVTRAGPKNRVGVSCLVEKTRSKLMISDKIIRFHLISDDISAKYISLCLNRGVTADYLEASKSGMAESQMNISQENLRSAPIALPPTAIQLKVISTIEDFFKVCDQLKSRLQSAQQTQLHLADALTDAALN

Gene
hsdS
Protein
Type-1 restriction enzyme EcoAI specificity protein
Organism
Escherichia coli
Length
589 amino acids
Function
The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. Subunit S dictates DNA sequences specificity. The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'.
Similarity
Belongs to the type-I restriction system S methylase family.
Mass
66.693 kDa
Sequence
MSVEKLIVDHMETWTSALQTRSTAGRGSSGKIDLYGIKKLRELILELAVRGKLVPQDPNDEPASELLKRIAAEKAELVKQGKIKKQKPLPEISEEEKPFELPDGWEWTTLTRIAEINPKIDVSDDEQEISFIPMPLISTKFDGSHEFEIKKWKDVKKGYTHFANGDIAIAKITPCFENSKAAIFSGLKNGIGVGTTELHVARPFSDIINRKYLLLNFKSPNFLKSGESQMTGSAGQKRVPRFFFENNPIPFPPLQEQERIIIRFTQLMSLCDQLEQQSLTSLDAHQQLVETLLGTLTDSQNVEELAENWARISEHFDTLFTTEASVDALKQTILQLAVMGKLVPQDPNDEPASELLKRIAQEKAQLVKEGKIKKQKPLPPISDEEKPFELPEGWEWCRLGSIYNFLNGYAFKSEWFTSVGLRLLRNANIAHGVTNWKDVVHIPNDMISDFENYILSENDIVISLDRPIINTGLKYAIISKSDLPCLLLQRVAKFKNYANTVSNSFLTIWLQSYFFINSIDPGRSNGVPHISTKQLEMTLFPLLPQSEQDRIISKMDELIQTCNKLKYIIKTAKQTQLHLADALTDAAIN

Gene
hsdS
Protein
Type-1 restriction enzyme EcoBI specificity protein
Organism
Escherichia coli
Length
474 amino acids
Function
The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. Subunit S dictates DNA sequences specificity. The EcoBI enzyme recognizes 5'-TGAN(8)TGCT-3'.
Similarity
Belongs to the type-I restriction system S methylase family.
Mass
53.513 kDa
Sequence
MSFNSTSKELIEQNINGLLSIHDSWLRISMDSVANITNGFAFKSSEFNNRKDGVPLIRIRDVLKGNTSTYYSGQIPEGYWVYPEDLIVGMDGDFNATIWCSEPALLNQRVCKIEVQEDKYNKRFFYHALPGYLSAINANTSSVTVKHLSSRTLQDTLLPLPPLAEQKIIAEKLDTLLAQVDSTKARLEQIPQILKRFRQAVLAAAVTGRLTKEDKDFITKKVELDNYKILIPEDWSETILNNIINTQRPLCYGVVQPGDDIKDGIELIRVCDINDGEVDLNHLRKISKEIDLQYKRSKVRKNDILVTIVGAIGRIGIVREDINVNIARAVARISPEYKIIVPMFLHIWLSSPVMQTWLVQSSKEVARKTLNLKDLKNAFVPLPSIEEQHEIVRRVEQLFAYADSIEKQVNNALARVNNLTQSILAKAFRGELTAQWRAENPDLISGENSAAALLEKIKAERAASGGKKASRKKF

Gene
hsdS
Protein
Type-1 restriction enzyme StySJI specificity protein
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
469 amino acids
Function
The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. Subunit S dictates DNA sequences specificity. The StySJI enzyme recognizes 5'-GAGN(6)GTRC-3'.
Similarity
Belongs to the type-I restriction system S methylase family.
Mass
51.91 kDa
Sequence
MSGGKLPEGWATSTINEMCNLNPKLKLDDDLDVGFMPMAGVPTTYLGKCNFETKKWSEVKKGFTQFQNDDVIFAKITPCFENGKAVVIKEFPNGYGAGSTEYYVLRSINGLINPHWLFALVKTKDFLTNGALNMSGSVGHKRVTKEFLENYGVPVPPLAEQKVIAEKLDTLLAQVDSTKARLEQIPQILKRFRQSVIVAAVNGQLTKELHKKNKFKLTELNISIPSLWKISEIGQFADVKGGKRLPKGESLIAENTGFPYIRAGQLKNGTVLPEGQLYLEEYIQKSISRYTVSSGDLYITIVGACIGDAGIIPDVYNNANLTENAAKICNLNENIFNRFLSLWLRSSYLQDIINSEIKSGAQGKLALARIKSLPLILPPLQEQHEIVRRVEQLFAYADTIEKQVNNALTRVNSLTQSILAKAFRGELTAQWRAENPELISGENSAAALLEKIKAERAASGGKKTSRKKA

Gene
hsdS
Protein
Type-1 restriction enzyme EcoKI specificity protein
Organism
Escherichia coli (strain K12)
Length
464 amino acids
Function
The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. Subunit S dictates DNA sequences specificity. The EcoKI enzyme recognizes 5'-AACN(6)GTGC-3'.
Similarity
Belongs to the type-I restriction system S methylase family.
Mass
51.395 kDa
Sequence
MSAGKLPEGWVIAPVSTVTTLIRGVTYKKEQAINYLKDDYLPLIRANNIQNGKFDTTDLVFVPKNLVKESQKISPEDIVIAMSSGSKSVVGKSAHQHLPFECSFGAFCGVLRPEKLIFSGFIAHFTKSSLYRNKISSLSAGANINNIKPASFDLINIPIPPLAEQKIIAEKLDTLLAQVDSTKARFEQIPQILKRFRQAVLGGAVNGKLTEKWRNFEPQHSVFKKLNFESILTELRNGLSSKPNESGVGHPILRISSVRAGHVDQNDIRFLECSESELNRHKLQDGDLLFTRYNGSLEFVGVCGLLKKLQHQNLLYPDKLIRARLTKDALPEYIEIFFSSPSARNAMMNCVKTTSGQKGISGKDIKSQVVLLPPVKEQAEIVRRVEQLFAYADTIEKQVNNALARVNNLTQSILAKAFRGELTAQWRAENPDLISGENSAAALLEKIKAERAASGGKKASRKKS

Gene
hsdS
Protein
Type-1 restriction enzyme StySPI specificity protein
Organism
Salmonella potsdam
Length
463 amino acids
Function
The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. Subunit S dictates DNA sequences specificity. The StySPI enzyme recognizes 5'-AACN(6)GTRC-3'.
Similarity
Belongs to the type-I restriction system S methylase family.
Mass
51.19 kDa
Sequence
MNRGKLPEGWATAPVSTVTTLIRGVTYKKEQALNYLQDDYLPIIRANNIQNGKFDTTDLVFVPKNLVKESQKISPEDIVIAMSSGSKSVVGKSAHQRLPFECSFGAFCGALRPEKFISPNYIAHFTKSSFYRNKISSLSAGANINNIKPASFDLINIPIPSLAEQKIIAEKLDTLLAQVDSTKARLEQIPQILKRFRQAVLAAAVSGTLTTALRNSHSLIGWHSTNLGALIVDSCNGLAKRQGLNGNEITILRLADFKDAQRIIGNERKIKLDSKEENKYSLENDDILVIRVNGSADLAGRFIEYKSNGDIEGFCDHFIRLRLDSNKIMSRFLTYIANEGEGRFYLRNSLSTSAGQNTINQTSIKGLSFLLPPLKEQAEIVRRVEQLFAYADTIEKQVNNALTRVNSLTQSILAKAFRGELTAQWRAENPDLISGKNSAAALLEKIKAERAVSGGKKTSRKKA

Gene
hsdS
Protein
Type-1 restriction enzyme EcoDI specificity protein
Organism
Escherichia coli
Length
444 amino acids
Function
The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. Subunit S dictates DNA sequences specificity. The EcoDI enzyme recognizes 5'-TTAN(7)GTCY-3'.
Similarity
Belongs to the type-I restriction system S methylase family.
Mass
49.894 kDa
Sequence
MSAGKLPVDWKTVELGELIKLSTGKLDANAADNDGQYPFFTCAESVSQINSWAFDTSAVLLAGNGSFSIKKYTGKFNAYQRTYVIEPILIKTEFLYWLLRGNIKKITENGRGSTIPYIRKGDITDISVALPSPSEQTLIAEKLDTLLAQVESTKARLEQIPQILKRFRQAVLTFAMNGELTKEWRSQNNNPAFFPAEKNSLKQFRNKELPSIPNNWSWMRFDQVADIASKLKSPLDYPNTIHLAPNHIESWTGKASGYQTILEDGVTSAKHEFYTGQIIYSKIRPYLCKVTIATFDGMCSADMYPINSKIDTHFLFRWMLTNTFTDWASNAESRTVLPKINQKDLSEIPVPTPPLPEQHEIVRRVEQLFAYADTIEKQVNNALARVNNLTQSILAKAFRGELTAQWRAENPDLISGENSAAALLEKIKAERAASGGKKASRKKS

Gene
hsdS
Protein
Type-1 restriction enzyme EcoR124II specificity protein
Organism
Escherichia coli
Length
404 amino acids
Function
The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. Subunit S dictates DNA sequences specificity. The EcoR124/3i enzyme recognizes 5'-GAAN(6)RTCG-3'.
Similarity
Belongs to the type-I restriction system S methylase family.
Mass
46.179 kDa
Sequence
MSEMSYLEKLLDGVEVEWLPLGEITKYEQPTKYLVKAKDYHDTYTIPVLTAGKTFILGYTNETHGIYQASKAPVIIFDDFTTANKWVDFDFKAKSSAMKMVTSCDDNKTLLKYVYYWLNTLPSEFAEGDHKRQWISNYSQKKIPIPCPDNPEKSLAIQSEIVRILDKFTALTAELTAELNMRKKQYNYYRDQLLSFKEGEVEWKTLGEIGKWYGGGTPSKNKIEFWENGSIPWISPKDMGRTLVDSSEDYITEEAVLHSSTKLIPANSIAIVVRSSILDKVLPSALIKVPATLNQDMKAVIPHENILVKYIYHMIGSRGSDILRAAKKTGGSVASIDSKKLFSFKIPVPNINEQQRIVEILDKFDTLTNSITEGLPREIELRQKQYEYYRDLLFSFPKPETVSN