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P07989

- T1M_SALPO

UniProt

P07989 - T1M_SALPO

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Protein

Type I restriction enzyme StySPI M protein

Gene

hsdM

Organism
Salmonella potsdam
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Methylation of specific adenine residues; required for both restriction and modification activities.By similarity

Catalytic activityi

S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei216 – 2161S-adenosyl-L-methionineBy similarity

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. N-methyltransferase activity Source: InterPro
  3. site-specific DNA-methyltransferase (adenine-specific) activity Source: UniProtKB-EC

GO - Biological processi

  1. DNA restriction-modification system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

S-adenosyl-L-methionine

Protein family/group databases

REBASEi3518. M.StySPI.

Names & Taxonomyi

Protein namesi
Recommended name:
Type I restriction enzyme StySPI M protein (EC:2.1.1.72)
Short name:
M.StySPI
Gene namesi
Name:hsdM
Synonyms:hsdT
OrganismiSalmonella potsdam
Taxonomic identifieri597 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Type I restriction enzyme StySPI M proteinPRO_0000088025Add
BLAST

Interactioni

Subunit structurei

The type I restriction/modification system is composed of three polypeptides R, M and S.

Structurei

3D structure databases

ProteinModelPortaliP07989.
SMRiP07989. Positions 4-527.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni148 – 1536S-adenosyl-L-methionine bindingBy similarity
Regioni178 – 1803S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Belongs to the N(4)/N(6)-methyltransferase family.Curated

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR022749. D12N6_MeTrfase_N.
IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view]
PRINTSiPR00507. N12N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07989-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNNNDLVAKL WKLCDNLRDG GVSYQNYVNE LASLLFLKMC KETGQEADYL
60 70 80 90 100
PEGYRWDDLK SRIGQEQLQF YRNLLVHLGA DEKKLVQAVF QNVNTTITQP
110 120 130 140 150
KQLTELVSSM DSLDWYNGDH GKSRDDFGDM YEGLLQKNAN ETKSGAGQYF
160 170 180 190 200
TPRPLIKTII HLLKPQPREV VQDPAAGTAG FLIEADRYVK SQTNDLDDLD
210 220 230 240 250
GDAQDFQIKK AFVGLELVPG TRRLALMNCL LHDIEGNLDH GGAIRLGNTL
260 270 280 290 300
GSDGENLPQA DIVATNPPFG SAAGTNITRT FVHPTSNKQL CFMQHIIETL
310 320 330 340 350
PPGGRAAAVV PDNVLFEGGK GTDIRRDLMD KCHLHTILRL PTGIFYAQGV
360 370 380 390 400
KTNVLFFTKG TVANPNQDKN CTDDVWVYDL RTNMPSFGKR TPFTEQHLQP
410 420 430 440 450
FETVYGEDPH GLSPRTEGEW SFNAEESEVA DSEENKNADQ HQATSRWRKF
460 470 480 490 500
SREWIRTAKS DSLDISWLKD KDSIDADSLP EPDVLAAEAM GELVQALGEL
510 520
DALMRELGAG DEADAQRQLL EEAFGGVKA
Length:529
Mass (Da):58,906
Last modified:February 1, 1995 - v2
Checksum:i07895A9ADA4FA249
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02507 Genomic DNA. Translation: AAA27143.1.
M14984 Genomic DNA. Translation: AAA27144.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02507 Genomic DNA. Translation: AAA27143.1 .
M14984 Genomic DNA. Translation: AAA27144.1 .

3D structure databases

ProteinModelPortali P07989.
SMRi P07989. Positions 4-527.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

REBASEi 3518. M.StySPI.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR022749. D12N6_MeTrfase_N.
IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view ]
PRINTSi PR00507. N12N6MTFRASE.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS00092. N6_MTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Roles of selection and recombination in the evolution of type I restriction-modification systems in enterobacteria."
    Sharp P.M., Kelleher J.E., Daniel A.S., Cowan G.M., Murray N.E.
    Proc. Natl. Acad. Sci. U.S.A. 89:9836-9840(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Two DNA recognition domains of the specificity polypeptides of a family of type I restriction enzymes."
    Fuller-Pace F.V., Murray N.E.
    Proc. Natl. Acad. Sci. U.S.A. 83:9368-9372(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 455-529.

Entry informationi

Entry nameiT1M_SALPO
AccessioniPrimary (citable) accession number: P07989
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1995
Last modified: October 1, 2014
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and Mg2+ as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases.

Documents

  1. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3