ID   Q21QG4_ALBFT            Unreviewed;      1726 AA.
AC   Q21QG4;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=Helicase-like {ECO:0000313|EMBL:ABD71981.1};
GN   OrderedLocusNames=Rfer_4295 {ECO:0000313|EMBL:ABD71981.1};
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OG   Plasmid pDSM15236 {ECO:0000313|Proteomes:UP000008332}.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969 {ECO:0000313|EMBL:ABD71981.1, ECO:0000313|Proteomes:UP000008332};
RN   [1] {ECO:0000313|Proteomes:UP000008332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118
RC   {ECO:0000313|Proteomes:UP000008332};
RC   PLASMID=Plasmid pDSM15236 {ECO:0000313|Proteomes:UP000008332};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of plasmid 1 of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000268; ABD71981.1; -; Genomic_DNA.
DR   RefSeq; WP_011458758.1; NC_007901.1.
DR   KEGG; rfr:Rfer_4295; -.
DR   eggNOG; COG0553; Bacteria.
DR   eggNOG; COG0827; Bacteria.
DR   eggNOG; COG4646; Bacteria.
DR   HOGENOM; CLU_000181_8_7_4; -.
DR   OrthoDB; 9151960at2; -.
DR   Proteomes; UP000008332; Plasmid pDSM15236.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR41313; ADENINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR41313:SF1; DNA METHYLASE ADENINE-SPECIFIC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000313|EMBL:ABD71981.1};
KW   Helicase {ECO:0000313|EMBL:ABD71981.1};
KW   Hydrolase {ECO:0000313|EMBL:ABD71981.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:ABD71981.1};
KW   Plasmid {ECO:0000313|EMBL:ABD71981.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008332}.
FT   DOMAIN          868..1141
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|SMART:SM00487"
FT   REGION          1696..1719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1704..1718
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1726 AA;  191284 MW;  45F465B4C5B91189 CRC64;
     MTQTNLWLPG FEFADALFGL TPIQTEVPIE PVSITQQEPQ STEIQEVPCF DASSTEDTLT
     QAESLPENAA PSLVMAQPAT AQDVGLSEPP WPLLAKDVHE DLRGQVTKFD ANVEAIELLR
     VLEAEMTPPT LAQRQTLNRY TGWGGIKHPF DSPYHLAQEW VNRAKQLKSL LSEDEFESAK
     ESTLNAHFTP IPVIDQLWTI LRQIGFTGGR IIEPAGGIGF MLGAMPSDIA QRSSVTAVEI
     DDLSARFLKV LYGSHANVLH MGFEKTNLPE QYFDLVIGNV PFGNYSVGDL RRKTYSDWAI
     HNYFVGRSLD LVRPGGLVAV ITSAYFMDNS NDKVRDVIAR KAKLLGAIRL PAGTFSEIAN
     TDVVADLVIL QKRSSTETLT REERENWVET TLLLDEDGTK MRVGNYTQGQ NVNSYWMKNP
     QAVVGVWTEI SRNQGQSIVP KLPKGADLMV EMERASKVIP QGVYAPATQQ VKEVLLAVAD
     GSNAVLPGSY VIEGGDIYRF NGHSLEKTGV KGKKAERIAG MALIRDTAQA LIKEQCKSDA
     AESVMSTLRF QLNVRYDSFI AKHGFISTKG NRQAMGSDPT WPLLLSLEMY NLEEETASKA
     DIFFERTIFS TAIPKSADNA EDALAICVAE LGCIDVDFIG QLLAADGKRA LDGLAAIGAV
     FVDPMTMAYQ TATEYLSGNV RDKLVIAQSA GLAFDRNVRA LEESLPPDLN PTDIDVIPGA
     AWIPIDVTEA FLRELVAEEW KGSNWASVNI GYELTTGTWS VKSSGPTGTA MCVTWGTSRI
     NGFALFEKCM NQIDAEVFDS FGDSPVLNAS ETAQARMKQD ELRAEYARWI WSDDDRAKQL
     CRLYNDKYNC WAIRKYDGSN LRLPGYSQSL ALRQFQLNAI ARIATGCNTL LAHVVGAGKT
     ITMVCGSMEL RRLGIAKKPF HVVPNHCLEQ YCAEFMRAYP NASVLMATKA DFEKDKRQTF
     VAKCATGNWD AVVLTHSMFE RIAADQVIVE DYLKRILSEL RAAKDAGALD RTAARAVNKF
     IKDWEARLEK LQASWKKDQL ISLSETGCDW VFFDECHVAK NLFRISSMKN IAGLSNSNSQ
     RSFDLLLKCV QLMRLHGDRE RGLCFASGTV ISNTMAELHV AQRYLQPYAL EKAGLEKFDA
     WAAQFGRAVS SMEVSPDGSS FRLNKRFKQF VNMPELMGLF RQVADIQTKE MLDLPVPKLV
     TGSYQICAVE PSNEVKEYVA DLVERVEAIR DRQVKPAEDN MLAITGDGQK VALDMRLIRP
     RTPFDPKGKV AMCIDNVYRI WEMTASFKGA QIIFSDMGTP TGHSLNLYED MRTRLVAKGI
     PHHEIAFIHE AQTHHAKSAL FAKVRAGTIR VLIGSTSKCG MGTNVQTRLY AVHHLTTPWR
     PSDLQQRDGR IERQGNTCEA IEIWRYVTSG TFDAYMWQTL TAKAGFIAQV LSGNAEVRSV
     EDAMMATLSY DEVKAIACGN PAVREKATID AEIMGLSLKL KHHRDSVWNS KEELWRLPIK
     IAEHKRQAVE YAKFHEQVLA SDGQGRGFGM VVNGKKFSDP EKIEKIITLS IRELKELQKA
     GLISEERLIG TLCGVDIFYG RSYGDFKITA RSSNGGASID IGTYSTGDSV IRKLGEIEQR
     LLAVVQDNEN RANYLTQQLP ILERIAQSEF ADTGKLESLR ARSKEIAIEL GLLKAMAGTD
     GQADGTEISS ELAATLAGED ESTQDGTEAS EENEEHDECL LTEAFC
//