ID B1VHI3_CORU7 Unreviewed; 411 AA. AC B1VHI3; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 68. DE SubName: Full=Type I restriction-modification system, specificity subunit {ECO:0000313|EMBL:CAQ05224.1}; GN Name=hsdS4 {ECO:0000313|EMBL:CAQ05224.1}; GN OrderedLocusNames=cu1264 {ECO:0000313|EMBL:CAQ05224.1}; OS Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=504474 {ECO:0000313|EMBL:CAQ05224.1, ECO:0000313|Proteomes:UP000001727}; RN [1] {ECO:0000313|EMBL:CAQ05224.1, ECO:0000313|Proteomes:UP000001727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43042 / DSM 7109 {ECO:0000313|Proteomes:UP000001727}; RX PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009; RA Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A., RA Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J., RA Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M., RA Puehler A.; RT "The lifestyle of Corynebacterium urealyticum derived from its complete RT genome sequence established by pyrosequencing."; RL J. Biotechnol. 136:11-21(2008). CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase CC family. {ECO:0000256|ARBA:ARBA00010923}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AM942444; CAQ05224.1; -; Genomic_DNA. DR AlphaFoldDB; B1VHI3; -. DR STRING; 504474.cu1264; -. DR REBASE; 17666; S.CurORF1265P. DR KEGG; cur:cu1264; -. DR eggNOG; COG0732; Bacteria. DR HOGENOM; CLU_021095_0_0_11; -. DR Proteomes; UP000001727; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.1120; Bipartite methylase S protein; 1. DR Gene3D; 3.90.220.20; DNA methylase specificity domains; 2. DR InterPro; IPR000055; Restrct_endonuc_typeI_TRD. DR InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf. DR PANTHER; PTHR30408:SF12; TYPE I RESTRICTION ENZYME MJAVIII SPECIFICITY SUBUNIT; 1. DR PANTHER; PTHR30408; TYPE-1 RESTRICTION ENZYME ECOKI SPECIFICITY PROTEIN; 1. DR Pfam; PF01420; Methylase_S; 1. DR SUPFAM; SSF116734; DNA methylase specificity domain; 2. PE 3: Inferred from homology; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}; KW Reference proteome {ECO:0000313|Proteomes:UP000001727}; KW Restriction system {ECO:0000256|ARBA:ARBA00022747}. FT DOMAIN 220..400 FT /note="Type I restriction modification DNA specificity" FT /evidence="ECO:0000259|Pfam:PF01420" SQ SEQUENCE 411 AA; 45698 MW; FE6CDC6DF43CC6A2 CRC64; MHSHNVPALR LDGFEDEWEE KTVQQISVPV ARVNPDSTAP VMMISAADGF INQSEKYSSD NAGKSLSKYI ELHQGELAYN HGASKIRPFG SCFELRESAA RVPFVYHCFR VPEEHPTFTS YSLNRKSVQS QLERLVSSGA RMDGLLNISF PQYGTVTAYF PTLEEQQAIG AIFTNLDAAI NQHSKKHQAL QQAKTALMQR MFPQEGQTVP ELRLEGFDGE WKTTTLGELG SFKSGVGFPE REQGGDTGLP FYKVSDLSAP GNELQLRSAN HYVTEEQIVR NHWIPVTAVP AILFAKVGAA VFLGRKRLAT DTFLLDNNLM AFSLDTKSWD VQFADTYLKT VDLTRFTQSG ALPSLNARHL AEAAATIPPT LEEQQAIGAV FTRLDTLIAT EAKYIESLKQ TKTALLQRMY I //