ID F0RDD1_CELLC Unreviewed; 764 AA.
AC F0RDD1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Type I site-specific deoxyribonuclease {ECO:0000313|EMBL:ADY30873.1};
DE EC=3.1.21.3 {ECO:0000313|EMBL:ADY30873.1};
GN OrderedLocusNames=Celly_3056 {ECO:0000313|EMBL:ADY30873.1};
OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS NCIMB 1423 / VKM B-1433 / Cy l20).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY30873.1, ECO:0000313|Proteomes:UP000007487};
RN [1] {ECO:0000313|EMBL:ADY30873.1, ECO:0000313|Proteomes:UP000007487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX PubMed=21677859; DOI=10.4056/sigs.1774329;
RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Ivanova N.;
RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL Stand. Genomic Sci. 4:221-232(2011).
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DR EMBL; CP002534; ADY30873.1; -; Genomic_DNA.
DR RefSeq; WP_013622616.1; NC_015167.1.
DR AlphaFoldDB; F0RDD1; -.
DR STRING; 867900.Celly_3056; -.
DR REBASE; 33134; Cly7489IP.
DR KEGG; cly:Celly_3056; -.
DR eggNOG; COG4096; Bacteria.
DR HOGENOM; CLU_018958_0_0_10; -.
DR OrthoDB; 9759819at2; -.
DR Proteomes; UP000007487; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0006304; P:DNA modification; IEA:InterPro.
DR CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR CDD; cd18799; SF2_C_EcoAI-like; 1.
DR Gene3D; 3.90.1570.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013670; EcoEI_R_C_dom.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF08463; EcoEI_R_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ADY30873.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007487}.
FT DOMAIN 165..338
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 537..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 88182 MW; 613BD4B063F2CB4A CRC64;
MTKHISESDT RANFIDPKLV DSQWEPVHIV REYYFTDGRK LLGNKRGKRL FLDYLLKYNN
TNLAIIEAKK LSDHPTKGLQ QVLDYAKKLK IKFVYATNGD QIYEFNRQTG RGDYVDNFPT
PQDLYNRLFG KKNALKEKLH KIPFLLTGNF GPRYYQEIAV NKVMESIADG EDRILLTLAT
GTGKTFISFQ IVHKLLTAKW NLDGNGRRPR VLFLADRNVL ADQAINTFNP YEKDVIKIDG
EEVRKRNGVV PTNAYIFFAI YQAIAEREDI GGFYKEYPSD FFDLIVIDEC HRGSANEAGS
WREILDHFKP AIHLGLTATP KRDDNVDTYK YFGKPIYEYS LKEGIQDGFL TPYKVKRVTT
NIDEYIHTND SKILQGEITK DRYEIDDFNK SITVKQRIEL VAQTILKQIG KMDKTIVFCA
NQDHALDLRD YINKYKTVTD INYCVRITSD EGKHGRELLE AFQDNDKDIP VILTSSKMLT
TGVDARNVRN IVLTAPIGSM VEFKQIIGRG TRVFDGKDFF TIIDFVGATN LFYDEDWDGE
PVDPTGKGGR PKTRPPRKVN EPGEPYERKE KLIISLSNGR KLKVTDIDTR YIDENGKPLT
AREFLEKLIG ELPSIYKNEE HLRKIWSNPD TRGDLLKQLG DLGFDNEQLN DLRNMIATQE
CDIFDVLSHI SFNSNLITRK QRVKFVKDEP EFFEVYKNLE ARDFLEFILK HYEDYGIEEL
QRDKLGDLVK LKLGTPKDAK TAFGDMKTLL GAYYKLQENI YRAG
//
