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Database: UniProt
Entry: C8W1L6_DESAS
LinkDB: C8W1L6_DESAS
Original site: C8W1L6_DESAS 
ID   C8W1L6_DESAS            Unreviewed;       209 AA.
AC   C8W1L6;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Resolvase domain protein {ECO:0000313|EMBL:ACV61661.1};
GN   OrderedLocusNames=Dtox_0751 {ECO:0000313|EMBL:ACV61661.1};
OS   Desulfofarcimen acetoxidans (strain ATCC 49208 / DSM 771 / KCTC 5769 / VKM
OS   B-1644 / 5575) (Desulfotomaculum acetoxidans).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61661.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61661.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S., Chen F.,
RA   Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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DR   EMBL; CP001720; ACV61661.1; -; Genomic_DNA.
DR   RefSeq; WP_015756379.1; NC_013216.1.
DR   AlphaFoldDB; C8W1L6; -.
DR   STRING; 485916.Dtox_0751; -.
DR   KEGG; dae:Dtox_0751; -.
DR   eggNOG; COG2452; Bacteria.
DR   HOGENOM; CLU_082093_0_1_9; -.
DR   OrthoDB; 3575335at2; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000150; F:DNA strand exchange activity; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd04762; HTH_MerR-trunc; 1.
DR   Gene3D; 1.10.1660.10; -; 1.
DR   Gene3D; 1.10.287.2170; -; 1.
DR   Gene3D; 3.40.50.1390; Resolvase, N-terminal catalytic domain; 1.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR000551; MerR-type_HTH_dom.
DR   InterPro; IPR006118; Recombinase_CS.
DR   InterPro; IPR006119; Resolv_N.
DR   InterPro; IPR036162; Resolvase-like_N_sf.
DR   InterPro; IPR048046; Transpos_IS607.
DR   NCBIfam; NF033518; transpos_IS607; 1.
DR   PANTHER; PTHR36172; -; 1.
DR   PANTHER; PTHR36172:SF1; TRANSPOSASE IS605 ORFB C-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00376; MerR; 1.
DR   Pfam; PF00239; Resolvase; 1.
DR   SMART; SM00422; HTH_MERR; 1.
DR   SMART; SM00857; Resolvase; 1.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR   SUPFAM; SSF53041; Resolvase-like; 1.
DR   PROSITE; PS50937; HTH_MERR_2; 1.
DR   PROSITE; PS00397; RECOMBINASES_1; 1.
DR   PROSITE; PS51736; RECOMBINASES_3; 1.
PE   4: Predicted;
KW   DNA integration {ECO:0000256|ARBA:ARBA00022908};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN          4..48
FT                   /note="HTH merR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50937"
FT   DOMAIN          61..209
FT                   /note="Resolvase/invertase-type recombinase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51736"
FT   ACT_SITE        69
FT                   /note="O-(5'-phospho-DNA)-serine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606118-50,
FT                   ECO:0000256|PROSITE-ProRule:PRU10137"
SQ   SEQUENCE   209 AA;  23907 MW;  FD89E230436376BF CRC64;
     MENYISIGKA AKYLGVSINT LRVWEKKKIL VPERTPTGHR RYKMSQVESF EGKKYSRIQN
     TVFLYARVST QKQADAGNLD RQIGRLTEYA SNNKYAIQAV FRDIASGLNE NRKGLQKLLK
     AVKETNNALV IIEYKDRLAR FGYAYLEKYI SDFGGHIVVI EKKDVDEQQE LVEDLIAVTT
     SFSARIYEKR GGRVAKKLSK VIESEVMEA
//
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