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Database: UniProt
Entry: G6B1Q6_9BACT
LinkDB: G6B1Q6_9BACT
Original site: G6B1Q6_9BACT 
ID   G6B1Q6_9BACT            Unreviewed;       784 AA.
AC   G6B1Q6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Putative type-I restriction enzyme {ECO:0000313|EMBL:EHJ36161.1};
GN   ORFNames=HMPREF0673_02831 {ECO:0000313|EMBL:EHJ36161.1};
OS   Leyella stercorea DSM 18206.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Leyella.
OX   NCBI_TaxID=1002367 {ECO:0000313|EMBL:EHJ36161.1, ECO:0000313|Proteomes:UP000004407};
RN   [1] {ECO:0000313|EMBL:EHJ36161.1, ECO:0000313|Proteomes:UP000004407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18206 {ECO:0000313|EMBL:EHJ36161.1,
RC   ECO:0000313|Proteomes:UP000004407};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHJ36161.1}.
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DR   EMBL; AFZZ01000248; EHJ36161.1; -; Genomic_DNA.
DR   RefSeq; WP_007903042.1; NZ_JH379471.1.
DR   AlphaFoldDB; G6B1Q6; -.
DR   GeneID; 78338210; -.
DR   PATRIC; fig|1002367.3.peg.2284; -.
DR   eggNOG; COG4096; Bacteria.
DR   HOGENOM; CLU_018958_0_0_10; -.
DR   Proteomes; UP000004407; Unassembled WGS sequence.
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; IPR013670; EcoEI_R_C_dom.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR029464; HSDR_N.
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; PF13588; HSDR_N_2; 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.
PE   4: Predicted;
FT   DOMAIN          182..346
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          560..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   784 AA;  89948 MW;  869AB57DB0495926 CRC64;
     MIDILQLSEE DIKLRYITPS IVDKGWSVDN ITMETKVKLT DGKINLRGNL VSRGKAKYAD
     YVLYYNRATP IAIVEAKDAS HAVAHGLQQA KEYAQMMDVP FAFSSNGMGY QEYDFLTGKE
     RYFSMDQFPT KEDLYARFIS ESNGGAGLSD NQMKVIDQPF CTGWDIFPPR YYQRNAVNRT
     VNSVAQGKKR LLLVMATGTG KTYTAFQIVY RLLKAGLVKK VLYLADRNIL VDQSIQQDFK
     PLDKTIHKVS YQKDKGPGNT AYEVYFALYQ QLIGQGGKQQ YKELFKPEFF DMVIVDECHR
     GSAKDDSNWR EILDYFDGAI QLGMTATPKE TKYQSSITYF DEPIYTYSLK EGIEDGYLAP
     FKVVNITTNI GDEWRPTKGQ KDINGNLIED RIYNNTDYDY NIVIEDRIRE VAHEITCYLK
     NTDRMAKTIV FCADEEHADR MRTALVNENS DMCRKNPDYV VRITGSDPYG QSKLDYFISV
     ASKYPVIATT SKLLSTGVDC KMVKLIVLDQ RINSMTEFKQ IVGRGTRIRE KDGKTHFTIM
     DFRNITRLFA DPDWDGPIEV DESYSKQKPK PYPEYKDDPT IIHEPDPKPR PNPKPIVDKD
     GCRVEVINKV VSVYDANGKL LRTESITDYT RKNINDTYVN LDDFINHWNA AEKKAEITDL
     MRESGIDLQA LKIERNMENV DDFDFICHIA YGKKPLTRKE RAENVKKRDV FNRYGAEARK
     VLEALLDKYA NDGISQLENR MVLKLDPFRQ MGSPANIAKL FGGNKQYFSA VKELENLIYN
     NSIA
//
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