ID T2D1_HERAU Reviewed; 359 AA. AC P24599; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 28-JUN-2023, entry version 66. DE RecName: Full=Type II restriction enzyme HgiDI {ECO:0000303|PubMed:12654995}; DE Short=R.HgiDI {ECO:0000303|PubMed:2020544}; DE EC=3.1.21.4; DE AltName: Full=Endonuclease HgiDI; DE AltName: Full=Type-2 restriction enzyme HgiDI; GN Name=hgiDIR {ECO:0000303|PubMed:2020544}; OS Herpetosiphon aurantiacus (Herpetosiphon giganteus). OC Bacteria; Chloroflexota; Chloroflexia; Herpetosiphonales; OC Herpetosiphonaceae; Herpetosiphon. OX NCBI_TaxID=65; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC STRAIN=HPA2; RX PubMed=2020544; DOI=10.1093/nar/19.5.1049; RA Duesterhoeft A., Erdmann D., Kroeger M.; RT "Stepwise cloning and molecular characterization of the HgiDI restriction- RT modification system from Herpetosiphon giganteus Hpa2."; RL Nucleic Acids Res. 19:1049-1056(1991). RN [2] RP DISCUSSION OF SEQUENCE. RX PubMed=7607523; DOI=10.1016/0378-1119(94)00779-r; RA Kroeger M., Blum E., Deppe E., Duesterhoeft A., Erdmann D., Kilz S., RA Meyer-Rogge S., Moestl D.; RT "Organization and gene expression within restriction-modification systems RT of Herpetosiphon giganteus."; RL Gene 157:43-47(1995). RN [3] RP NOMENCLATURE, AND SUBTYPE. RX PubMed=12654995; DOI=10.1093/nar/gkg274; RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A., RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K., RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S., RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A., RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S., RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V., RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E., RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W., RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.; RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing RT endonucleases and their genes."; RL Nucleic Acids Res. 31:1805-1812(2003). CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double- CC stranded sequence 5'-GRCGYC-3' and cleaves after R-2. CC {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:2020544}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage of DNA to give specific double- CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4; 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; X55140; CAA38937.1; -; Genomic_DNA. DR PIR; S14028; S14028. DR AlphaFoldDB; P24599; -. DR REBASE; 1102; HgiDI. DR PRO; PR:P24599; -. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR019044; Restrct_endonuc_II_HindVP. DR Pfam; PF09519; RE_HindVP; 1. PE 4: Predicted; KW Endonuclease; Hydrolase; Nuclease; Restriction system. FT CHAIN 1..359 FT /note="Type II restriction enzyme HgiDI" FT /id="PRO_0000077313" SQ SEQUENCE 359 AA; 41204 MW; 67C9B01B88B6890C CRC64; MFEQLNQPGL FGITNSNRDF TKKEAWGKNQ FNNAFPIALA CFMFSQNIKP IYIRLEKRNI EHNYFAVDQV FQINPLEAQA FFAFEHSYHP YTELIIGKTP AIDVVISNLQ NSQIINAFEI KLTAIPDNTT ANLPDNLQGC EIVIRPDTIV YLALSIAKVF QQNPLALLDI LDPVCARIGD WEDATSIQPM IPLFCELLYT IFDRYQAVQI PILLQPIWKT QGKLSILHEN CLDLFVWSNF ALAKVFLDAS IKPSEKSITR PERTTVWLIK MLYDFAQNGK IDYKRTLDRI TFNLKNDKAF AASGMVTRKY MNSPELQNPR IKRHSIKHII INGGQRYLSP ERRLDSAIVS TPGLFEEIL //