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Database: UniProt
Entry: S2ZM78_BIFBR
LinkDB: S2ZM78_BIFBR
Original site: S2ZM78_BIFBR 
ID   S2ZM78_BIFBR            Unreviewed;      2533 AA.
AC   S2ZM78;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1482_01544 {ECO:0000313|EMBL:EPD75475.1};
OS   Bifidobacterium breve HPH0326.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1203540 {ECO:0000313|EMBL:EPD75475.1, ECO:0000313|Proteomes:UP000014395};
RN   [1] {ECO:0000313|EMBL:EPD75475.1, ECO:0000313|Proteomes:UP000014395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPH0326 {ECO:0000313|EMBL:EPD75475.1,
RC   ECO:0000313|Proteomes:UP000014395};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dover J., Dai D.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bifidobacterium breve HPH0326.";
RL   Submitted (MAY-2013) 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:EPD75475.1}.
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DR   EMBL; ATCB01000003; EPD75475.1; -; Genomic_DNA.
DR   PATRIC; fig|1203540.3.peg.1539; -.
DR   HOGENOM; CLU_000181_8_5_11; -.
DR   Proteomes; UP000014395; 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:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
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; IPR003356; DNA_methylase_A-5.
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; N6_MTASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF02384; N6_Mtase; 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; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
FT   DOMAIN          1363..1618
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1761..1938
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          92..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2140..2183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2494..2533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2142..2180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2503..2533
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2533 AA;  280663 MW;  389546A43A640DBC CRC64;
     MVRKRLYAKQ TASVEYEQID LFSLLEEEQR QTDRTAEQVR GYEITVGHAA VQRLRARGAD
     DETIAAVAAE YRENRLRGLG RRDARIAAEN KLGVGAATPG ETTPQPVVKR FTQSSGTENN
     TEERNNDGRD DMDRPAAQGA LREEPQGDGT APGGASGTVQ QVGAAVQGVH PQQPARDPEH
     AHQLADGQPS AAVQGDDDGQ RARGASAGHR EADEGTPGAD HGPADGVQAP AQPDGLPEGG
     TPDDRPGPAQ RDERGASGVD EHGDPRDRGK LLASLDSQRA RSPRERAEAN IAAIRTLKTL
     DGNGDEPLSA EQTDTLRGYS GWGGCADAFS DKPEWADLNA EIRELLDDDE YTQARASTLT
     AYYTPGPVVK AMWDALDIGS APIQVLEPGC GTGNFMAGIP ENIKANVSGV ELDPISARIA
     AALNPDATIL NADLADCTIH PGFDLTIGNV PYSGDISLDY RTTDGGTSRL PLHDYFIERS
     VDALRPGGVA MLLTSRYTLD KRSETMRADL ARKAELVGVV RLPSSTFARQ AGTEAVTDVL
     VLRRRERTLD RTPDEAWIHS NPVAVPGYQD VTVNVNQAVA NDMTAHAVGD IRPVIGRFGG
     DFDVVFQGDA EQVGERLQEL LSTQITHGPA LSLGEAEPAG RAEITVRPDH VAPFEYSVDQ
     RGVVWYGDGT TVTEIAHGQG DEARRLRGMI RLRDLARELQ RLELDPARVD DPDVEAKRAE
     LDRAYDRFTS EFGRLCDRAN QRAYSGEESG HHLVMALEET DEKGRFAGKA KCLSQRTISP
     VPPMPAHADS LDDALSISLD RDGRVDLELI ARLADTTVEE TEAGLGDRII RDPDTGDVMP
     AEDYLTGDVG TKLGHVTAMA EHLRHRAGTE AMTQFAASTY ATPEDMPAME QAREWINTAG
     TDVWRSLTDP YAAESYRDPA PVIERINDGR YGWTMGWNRN PGLVLALAWR AVEELPERHA
     RVTLERSDAE ERKPWHAPAW HQSHGTSPLW DAFCWTWRDG DAPQDYAPIL ADRRMPVRDL
     ALFVHKIAHT DRLETADKTA ILSNLFESYS AHDVHGSTIW TDTTIGAMAR QLMPGTDDPM
     RLAERLATDM SVSEWIWGIT RELPGLRQGA SHDAYSTPPR TVDARPDDYQ AFRARREEQL
     GQWREQPEHA EAAHADQADA ERLEHVAGLL ERVQPIPLET EQIKAPLGAP WIPAKDIHDF
     MMETFNVRGH GLTPGKLAQY SVDWIPQLGQ WRVGYSGGGD IDYKAAKTYG TEDRNPFQLL
     EACLNNAQIT VTKDSPTETT PAGKPKRVKD QKATMAAIEK ANAIRDTWNQ WVFKDPARAR
     RLTALYNRRF NSLRPRHVDG SYLTTPGIAH DVALRPHQKD AVARALRSDE GTLIAHVVGA
     GKTFEGVTLS HEAKRLGKAS KPMLVVPNHL VNQWAGDVLR LYPASRILVM DKDAQRNPES
     VRRFWGRVAT GDWDAVIVPE SRFSQLHVSK ERRLRNMRAR VEEFTLAVKA AAQARGDKDP
     TVKRLEAARK SAETAMQRLR DGKESRDDKA LAGIEFESLG VDMLIVDEAH HFKNLGVPVA
     SADLGMQLSS AAKCEDLLDK CEWLREAGHG GNIAFMTGTP VSNSMSELYN MQRYLAPETL
     KAQGLDTFAA WAGAYGQVVP TVELKPEGNG FQVKQRFARF QNLPELMNAV KQFTDMITND
     DIQLPLPELE QVPVPVPITD RQKEEMEELS DRADRVRDGD VPPEIDNLLR ITGDGRKIAL
     DPKLLKGHEN DRPLENGKIQ ACAENVARIW HEETPRLGTQ LVFCDSSTPA SGGWNAYQDL
     KDRLIQLGVP AEQIAFVHDA GDNPAKREKL FAKVRSGEIR VLMGSTQKLG TGTNVQERLA
     AIHDLDCPWR PADLEQRLGR IQRQGNMYGH VRDYRYVTEG TFDAYSYQTV ERKQRFISQL
     MSSKSPAREA ADLDADVVTL ANIKALATGD PDIQRRMTLE NEINQLKLLR ASWAQQKADT
     RRDINQQLQP RIERIRQAIR EKTDDKPLAS KALGIHQTAR MNGRWEGMTI NGQPIGDRQT
     ACRLIHQAAH QAHDGDTIAE YDGLPVIARR AATTGRITLA VKAVHEHESG TEMPGPYLTG
     PSSIVSQLDR IVRNMATDPG KLTERLADAE RELAAAQETL AEPFAHEDEY RRKQAELEQL
     TSKPDESRKT ESRDQETKER SAGMPLTMEN ARRLLEQDPD VAGITQGGNA MGHYLEARLT
     DGRAVQIDFH DNPAWKDTDR LAGRIEVSYA NRPQAEWQYD DNDIADREHT VIDPADPAAK
     KTIAKAVKDW ERAGGLHAAR TTETSHLAAQ QPPEEYAYRW RKPGDPDRHI AYLSTAFDRD
     QAMKAREDAG YLVTKVNEDP AVLYEQHRKA SCMRASHILE RYESPDQDAV RILHGIVGEV
     NAHDPENDIA TYLAYPSDKA VQITGDGLTS ADIAEKREMG GWDPRKDPLM RINAQGDWTG
     ITQQQADQIV WDNRDEILTR ASYDSELSTW TLHQLDQLKE PQPAQSLDRD RPEPDHKAPA
     QADSTTKRHG PRL
//
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