ID J6IL10_9FLAO Unreviewed; 1967 AA.
AC J6IL10;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Eco57I restriction-modification methylase {ECO:0000313|EMBL:EJU34685.1};
GN ORFNames=HMPREF1154_2130 {ECO:0000313|EMBL:EJU34685.1};
OS Capnocytophaga sp. CM59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=936370 {ECO:0000313|EMBL:EJU34685.1, ECO:0000313|Proteomes:UP000003140};
RN [1] {ECO:0000313|EMBL:EJU34685.1, ECO:0000313|Proteomes:UP000003140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM59 {ECO:0000313|EMBL:EJU34685.1,
RC ECO:0000313|Proteomes:UP000003140};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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:EJU34685.1}.
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DR EMBL; ALNN01000003; EJU34685.1; -; Genomic_DNA.
DR RefSeq; WP_009640579.1; NZ_ALNN01000003.1.
DR PATRIC; fig|936370.3.peg.149; -.
DR Proteomes; UP000003140; 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:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.1360.10; -; 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; IPR002052; DNA_methylase_N6_adenine_CS.
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 Pfam; PF13155; Toprim_2; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF56731; DNA primase core; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000313|EMBL:EJU34685.1};
KW Transferase {ECO:0000313|EMBL:EJU34685.1}.
FT DOMAIN 1221..1463
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1602..1774
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 318..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1967 AA; 224486 MW; B0DDF45056E76005 CRC64;
MPLFSPEEIE EICNSVSLID YFRDLDRRGI VRYDRKRGKD EYFLTDNNKF SVTDDQYYDF
KAGQGGKIIK AVMEMENKNW REAIEFLRDF SNTYIVNNDI GAEKKQTPQP TSEPTIAEPR
NVFTMAITPN NEKLIAYFEG RGIPKDILQT YTQQVHYRNR TSGKSFFGIG LKNQSGGYDV
KSLLDKPYDK AKVGRSDMSV IPGSSKEMVV FEGMTDMLSY LRLCRDTNKP NTRTLVVLNS
TTNTGAFIDQ FRTYEGKIHL VLDGDKAGND ATDKILNSLP NSTDQRHRYN ISETGNNDLN
DYLINKIKNS LQVQEKSRTL AEENKNQLSE NETVTIEPNR VSSLEPMGGK SLDPNYREPL
QGSQSQQEGD NPGRQAVGSN HAGNGLSSSE RSDLGGRTGG SQVDTNSGEQ QEVLSGVGGT
GENPNVSRTR NTGGSDTGSP QTTAEGQKDE GNIQSTQTGE RDSTRQDIPN GDRPRSERDS
KTAITGFERV TLINKVAHLS KLAKGNKVSN EQIKDLVDLL TFVDKDNTIQ LKEGATITDS
IKDIVNHYKS GGITKDGRGV LDEYYTDEKL VNAVRNLIKD NFQGKQDIKV LEPSVGTGNF
LHAATDLGIN THITAFEINE TTAKIAKILH PDTQINLRSF ETEFVTDNGT KKAFTPSYDL
VIGNPPYGTH RGLYLGLGEE SKLSRYEDYF VKRSLDVMNE GGTLAMVLPS SWLDRQKSLS
NGELIDAYRL PNGAFKATGV GTDIVVLRKN SQAQAKDITQ FFKEHPNKVL GDTIMKKNRF
GREEEYIKGN LEDALTRLAE VKPNKAVEAV KPIKPIAQTQ EVKQLSIFDL LQEQEQEQKK
NAEEKTPISH DSSDKVEIPI AEVQDKLNKA LDSLEKIKFK SLAVMQEIEN YNILLIEIEK
EPEKFSKEYK EDLVKKAENI INVHNGKNTN NRKVKSSEKS EYTLQYTPNI SKKVLKYQFS
KDDMVVNTSL QNSSNLTEEQ IKAFSATNYD GELLSNDEAI LNKYGNHYKG KIIHDFYYAE
GNIYEKLDQL EKDFSDRFGD ENKKAQYEKQ KALLESVLPP KKQLEDIVVA PNHEFVHNFW
LGKVEKETYN HYMKRHETIT VDYSLADKFK DFVDSLPREA LSPSSPWEVS QFVDNQTVTG
SDKERNALVR ERRKEVANKL FQKFLQEELT PEQKRDFVNE FNRKYNNIHI PDYSQFPLFS
KINQNFKGKP LQLTEVQKAG IGRLTTKGVG LLAHEVGFGK TLSGILAMHE AMERGNAKRP
LIVVPNDNIL KQWVDTIYET IPHAKVNVLG NLGKDYDLSH FDNKDGEITL VTYEGFNNIG
FNKEITQSLS NRFSYINEKD VNGLDNPTQR DIEKGIADRY KIEGKMKQGK VYDWEDFGFD
HLTFDEVHNA NHIVDKVRIE DKRFNSDFRN QNQRPSKLGL NTWVAAQYIQ ERYDGRNVTL
LSATPFTNRP LEYYSILSLV ANDRLEKSGY FNVNNFFETF MEADNDMEID AKGDVKFKTN
VRRFKNNALF QQLLSEFIDI KGEEDNPQLK RPNRINKEYK IEQNSLTEQM YDKLNSLLDE
SKDGAILTHI LNARKIAISP YLYEGYDGDK PTTKEFVENS PKLKTTMDLI RQNKADKPEA
GQIIYSELGV SEFPQLKEYL IKEVGYKDDE VGIITGATSK AQRLDIQEKF NEGKIKVVIG
SEAIQEGMNL QENTSDMYLL TLPYNFTSLR QTEGRMWRQG NKWENVRVNY MLTNDSIDVF
MLQKLQAKQA RYMEAIKKGA SVVDVSDVDT QEMKTAIITN PETRARIEVE LLKKRLENEK
TKHAADLGFI SRKYEDYNKA LGEYLYVKKS YEEMQKYAQE ENGGYWVDRL PDKKVQVDMA
QRNLNMVTEK LMKKGINVED FKIQQESTQA IIEDLDKRIK EELPILENNL IAQYKAEKAE
RLSRPQTDFV QERAQENKTF YKLIPDKEIA KIAEEKPQES TYKAFKR
//
