ID T2C1_HERAU Reviewed; 345 AA. AC P25258; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 28-JUN-2023, entry version 58. DE RecName: Full=Type II restriction enzyme HgiCI {ECO:0000303|PubMed:12654995}; DE Short=R.HgiCI {ECO:0000303|PubMed:1662609}; DE EC=3.1.21.4 {ECO:0000269|PubMed:1662609}; DE AltName: Full=Endonuclease HgiCI; DE AltName: Full=Type-2 restriction enzyme HgiCI; GN Name=hgiCIR; OS Herpetosiphon aurantiacus (Herpetosiphon giganteus). OC Bacteria; Chloroflexota; Chloroflexia; Herpetosiphonales; OC Herpetosiphonaceae; Herpetosiphon. OX NCBI_TaxID=65; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=HPG9; RX PubMed=1662609; DOI=10.1111/j.1432-1033.1991.tb16497.x; RA Erdmann D., Duesterhoeft A., Kroeger M.; RT "Cloning and molecular characterization of the HgiCI RT restriction/modification system from Herpetosiphon giganteus Hpg9 reveals RT high similarity to BanI."; RL Eur. J. Biochem. 202:1247-1256(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'-GGYRCC-3' and cleaves after G-1. CC {ECO:0000269|PubMed:1662609, ECO:0000303|PubMed:12654995}. 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 Evidence={ECO:0000269|PubMed:1662609}; 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; X55138; CAA38932.1; -; Genomic_DNA. DR PIR; S19706; S19706. DR AlphaFoldDB; P25258; -. DR REBASE; 1099; HgiCI. DR PRO; PR:P25258; -. 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. PE 1: Evidence at protein level; KW Endonuclease; Hydrolase; Nuclease; Restriction system. FT CHAIN 1..345 FT /note="Type II restriction enzyme HgiCI" FT /id="PRO_0000077311" SQ SEQUENCE 345 AA; 39170 MW; BAE97E3AFEB89EB1 CRC64; MNYQRSFEDL EFNAIKWWPQ ELSATVAEAS VLPILISSQD LFISILKLSG THPEQIFDVI NAAQISANLF LKHLVVLADY GGEMIKRLGK EFQEIFPRMD STLEYYMNYT FKGEQYTYIF KKLPIKGLDN SKLAIDGKAI IEIKPLSDLY RDMIMILLYG STTEQFNLAG LEKCEIGTIL GKNEIIYTYI TQKYLYVSRI TNGANTNSLG QIAQTYVCDI LSKYLPNDYS VTRNGKILLS DLNSQDSTKT SFDILVEFAD KKVGIEVSFQ VTTNSTIERK AGQARDRQNR MHAHYYWIAY VIDGAGNFER SGAVRAICRY SDCTVAYSES EIAVLAAFIQ EKFNA //