ID   Q112D5_TRIEI            Unreviewed;      1119 AA.
AC   Q112D5;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   SubName: Full=Type III restriction enzyme, res subunit {ECO:0000313|EMBL:ABG51639.1};
GN   OrderedLocusNames=Tery_2422 {ECO:0000313|EMBL:ABG51639.1};
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG51639.1};
RN   [1] {ECO:0000313|EMBL:ABG51639.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101 {ECO:0000313|EMBL:ABG51639.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000393; ABG51639.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q112D5; -.
DR   STRING; 203124.Tery_2422; -.
DR   REBASE; 13423; TerORF2418P.
DR   KEGG; ter:Tery_2422; -.
DR   eggNOG; COG4096; Bacteria.
DR   HOGENOM; CLU_009326_0_0_3; -.
DR   OrthoDB; 9802848at2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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; IPR025285; DUF4145.
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; PF13643; DUF4145; 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; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}.
FT   DOMAIN          364..523
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          599..764
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   COILED          155..203
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1119 AA;  128751 MW;  06579322A2E6B76E CRC64;
     MTSNFDFLKP HYPKLHQTAT QAETLINNAP RASCFYTRYT LEQAVIWLYE NNPYLELPKT
     YNLGALIHEQ TFKDNLQNNL FPKLRIIHKI GNAAAHDPKP ITSKDARYLI QELYHFLYWL
     TRYYSPDGKN LPNLKFNPDL IPTSTTKSDL TLDKLQQLET QLSTAQEMQR IAEQKEKQTT
     AELETAKAEL AQLKQQNQTK SDRHDYNEAD TRTYLLDILL KEAGWPIHLP ESTEYQVTGM
     PNETGKGKID YVFWGDDGNP LAIVEAKRTR KSPQTGQHQA KLYADCLQAE FNHRPVIFYS
     NGYEHWIWDD FNYPPRPIQG FLKKDELERL IFRRSHRQPL HTLDVNPDIA GRCYQKEAIC
     CIKEIFDNKQ RKALLVMATG TGKTRTAVSI VELLERANWV KRVLFLADRN VLLTQAQGVF
     NSNLNSITTA NLTEKKQDAE NATIVFSTYP TISNRINATD GDKRLFSPGY FDLVIVDEAH
     RSIYRKYRQI FQYFDALLLG LTATPRNEVD RDTYSIFDLE PGVPTFAYEL DSAIKDGYLV
     PPSGVEVPFK FMRAGIRYSE LQPEEKTAYE ERFADAETGE VPDKINATAL NTWLFNISTV
     DQALQLLMER GLKVEGGDRL GKTIIFARNH KHAEFISERF NANYPHYKGQ FAQIIDSQSS
     YSQSLLDDFS NADKQPIIAV SVDMLDTGVD VREVVNLVFF KPVYSRIKFN QMIGRGTRLC
     PNLFAPGDDK TEFLVFDLCS NFSYFEQQID EKNVKIPDSL TTKLVKSRLE LSQLVPTGEL
     KNNLLDELHQ YINSMPKDNF LVRPHLQQVE EFSQRERWNE LGESDQEIIG ESLASLPNGL
     PKESHLNKRF DLICVKLQLA LLKQSTDFIR LRDNIRDICS QLAQKSNIPM IAAKLQVIEE
     VQAEEWWRDI TVEMVSILQQ DLRELVKFID SQEQKIMYVN FADEMGEVQN VNVPTQTSGF
     SPLQYKKKVE AYIRSNENNV AVAKLKRNIP LTDADLTALE EMLFNSEVIE DREIFAEVYG
     QNISLKLFIR KLVGLDRNAA KELFSKYLNS KFNTSQIRFV ENIIDYLTQN GVMSPELLYE
     PPFTDLHTEG LDGIFADKEA DNIIEILTEI NESVDYDVA
//