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Database: UniProt
Entry: D7N6M0_9FIRM
LinkDB: D7N6M0_9FIRM
Original site: D7N6M0_9FIRM 
ID   D7N6M0_9FIRM            Unreviewed;      2878 AA.
AC   D7N6M0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Helicase C-terminal domain protein {ECO:0000313|EMBL:EFI42533.1};
GN   ORFNames=HMPREF0629_01187 {ECO:0000313|EMBL:EFI42533.1};
OS   Peptoniphilus sp. oral taxon 386 str. F0131.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Peptoniphilus.
OX   NCBI_TaxID=575609 {ECO:0000313|EMBL:EFI42533.1, ECO:0000313|Proteomes:UP000004712};
RN   [1] {ECO:0000313|EMBL:EFI42533.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0131 {ECO:0000313|EMBL:EFI42533.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA   Izard J., Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Haas B.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Peptoniphilus sp. oral taxon 386 strain F0131.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL349422; EFI42533.1; -; Genomic_DNA.
DR   STRING; 575609.HMPREF0629_01187; -.
DR   eggNOG; COG0553; Bacteria.
DR   eggNOG; COG0827; Bacteria.
DR   eggNOG; COG4646; Bacteria.
DR   HOGENOM; CLU_000181_1_1_9; -.
DR   Proteomes; UP000004712; Miscellaneous, Scaffold supercont1.1.
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   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000313|EMBL:EFI42533.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000313|EMBL:EFI42533.1};
KW   Hydrolase {ECO:0000313|EMBL:EFI42533.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:EFI42533.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004712}.
FT   DOMAIN          2274..2442
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          210..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2831..2878
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2604..2652
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        213..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2831..2847
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2861..2878
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2878 AA;  330603 MW;  FF1CB09956039B55 CRC64;
     MRGQKGIPIL EDYGTYKKVD YIFDVSQTVS RNRDVNEVNL WKFDKEAHQD VLKEMIANEG
     YEESESNLEN IFSLSRIYGD EKIGSLMNEL RITDEDRISF VKFVRDSISY AVASRFKVDY
     PVDYELLREN ISRLDTISLM SVGETVSDIS GNIIDTTIQK SKELELQKGV LRNREAGYNK
     IREEIEKGEN HVLRRDDKER ISETERVFRN GEYGGDSSQN QGEYTKQLGG TDGIHQGISE
     SDLRSDEAGL SFTERGAEPL RDVSGSIQGE EADRTPDGYS ETGDSIYEDR EAEADEVLED
     RGREQSTVWG DDFSLEGNDH QGNRGNLKEN TEVEIREADK ASFSLPENSY GQIRLSIPLA
     QKDIDTVLIN GGNHDGGRLP IIAEFSKGKS NEELGEYLKN TFQGGNGYII DGNEISAWYS
     DKGLHFASGT SAREDDTQVL SWSDAANRIA ELLENGEFAT NVEISEAFDY ERDRISESLW
     YLIHDLSEEG KEQGFFEFLE KGGGFPDETK RLSEALKNPE YLVDVIKEYG RFLEAYREDR
     DVLRFDYHKV DSLYQKLQEL ALPRKEYTSN LTELPKVKAF ITEDEVLATL SMGSGADRGK
     ERITEFFKEN HTLQEKADFL KDEYGTGGRS HAVSGLTGSG EWHDAKGIKL EKNDCNDVFL
     TWSRVAKHID EILSKNLYLE EKKIESKAER EEAKELQYYS KDEPENLMTD EMIERVPELY
     AQEDVELADK EVHAAYIIPF RSNWTWYMTE YDRESGDAFG LVLGIEPEWG YFNLNELKEL
     NAQRLVLEDF PKTFQEIKDT ELVKQMSEEE IDRVFNGQLS SKDNQKEQDI FYLSDEMGIS
     LEESEGIIDD RSRLSGVSTE DTDNKDNLLD EKSPVQSTLF DYIQQKEEVE LNEKEESLAE
     QFAVKQGDTV YFDHEAYIAR DIEKNKVNGK PEVWLYPARD GNRQIAIVPF MDNEELLKKI
     SLERPNFLVG DEVRYKDKDC TITRFDNMGN NLKTVTVMDN TEYLGGMITG SDVIPYRLES
     DLERIFENLT YTKAKDTIQD IDEKAEKPKI EAHNFKIIEE ILPEKLTPSE RLNQNLEAIS
     MLKRVESGQR ELDNTAQEVL VKYVGWGGLS EVFDEERGGQ WKKARSFLKE NLSQAEYEAA
     RESTLTSFYT PKTVIDSIYS TLSGMEFKNG NILEPSMGIG NFIGNLPDEM KKSKFYGVEL
     DSVSGRIGKL LYPESDIQIK GLEETSFSNN FFDVVIGNVP FGEYKVNDRE YNKNNFLIHD
     YFFAKSIDKV RNGGIIAFIT SSGTMDKKDE SVRRYLAARA GFLGAIRLPN DTFKGVAGTE
     VTSDIIFLKK RDSIRERDED WIHLSEDEKG LTYNKYFVEN PQMVLGSMEE VSGKFGNTLA
     CLPRENADLK ELLARASEEI SKGATYEEIE LLEDEISTMP ATDDVKNFSY TIIDDEVYYR
     ENSLFVKKEI TEKNKEKIKD YLELNTALKD VIYKQKEDFS DDEVKKSQEK LNEVYDGFSK
     KHGFVNNLSN TRALKEDSNF PLVSSIEILD EEENFKEKGD IFSKRTITKA KTIDHVDTSL
     EALVLSMSEK GYVDFDYMES LTGKDRPTLI EELRGEIYLN IREEQNFYRP LSFNPEDGDL
     PFACASGSDS YKYGYVTKDE YLSGNIRDKI AIVDSYLSKL RQTERELPHL GYAEDGKEKE
     LISYEMNRLE YQKAELTKVL PKALEASEIS VRLGATWIPM KDIEKFIFET LKTPGYAKWD
     IKVKFSNLTS EWNVEGKSAD RGNDLAEMTY GTSRVNAYKL IEDALNLKET KVFDQIENPD
     GSKSSVLNKK ETLLAGQKQE LLKEEFKNWI FSDQERRNRL VKLYNERFNS IRNREYDGSN
     LSFEGMNTEI ELRPHQRNAI ARSLYGGNTL LAHVVGSGKT FEMVASAMES KRLGMCSKSL
     FVVPNHLTGQ IGREFMQLYP SANIMVADKK DFEPKNRKRF IGKIATGEYD AVVIGHTQFE
     KIPMSKEYQE KHIQDQIDEI LNYIEEYKHD RNQNFTVKQL EKTKKKLEAR LEKLNDDFKK
     DDVITFEELG VDKLFVDEAH GFKNLYLHTK MRNVAGIGQS EAFKSSDMFM KCRYMDEMTN
     GKGIVFATGT PVSNSMTELY TMQRYLQYEN LKKNHLEHFD AWASTFGETQ SAFELAPEGT
     GYRVKTRFSK FYNLPELMSM FKEVADIQTA DTLDLPTPEA HYEVIKTLPS EEQKEILKGL
     SERADKVRNR VVEPDEDNML KITNDGKKLA LDQRLLNPLL PDNSDSKVNV CVKNVFAIWD
     KTKDDRSTQL LFSDMSTPKG DGEFNIYDDI REKLVAMGIP KEEIAFIHEA NSDKQKDELF
     AKVRKGDVRI LLGSTQKMGA GTNVQNKLIA LHDLDVPWRP ADLEQRAGRI VRQGNENKEV
     NIYRYVTENT FDAYLWQTIE NKQKFISQIM TSKTPVRVAE DVDESSLNYA EIKALATGDP
     KIKEKMDLDN EVTKLKMLEA NYKSNRYRLE DKVAKNYPEE ITRTEKLIEA VKNDISEVEP
     KAEGEEKFTS ITILGEKITD KKLAGEKLLE AISKIKINES KMIGKYRNMD LEVSYNFFTN
     EHNFSLNGAA KHSGELGTSA DGNITRLDNA LEKMPEKLKR LEEKLISTKE QLENAKEELK
     KPFEKADELK TKVLRLAELN KLLDMGEVEE KRNDNPLVED VKRAIIDFCN REYEENHSYD
     EFDTLYPDLK HIGIAYTDTP DERHGIQYEL NLEDYTWTQY IDDTPIKTES FDYENKGENE
     ALKNMKNEIE LSSFEDLVYV DSEDLRAATG LDIDDEGNFY DPLAKDLDND GIPDRYDNDF
     RDSDYFESTY DVEDNLHTKE ETAQRTDDKP SILGQIRAYQ SESKTEEKQT TKEQEYAR
//
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