ID R9N322_9FIRM Unreviewed; 2839 AA.
AC R9N322;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0000259|SMART:SM00487};
GN ORFNames=C819_00821 {ECO:0000313|EMBL:EOS77710.1};
OS Lachnospiraceae bacterium 10-1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1235800 {ECO:0000313|EMBL:EOS77710.1, ECO:0000313|Proteomes:UP000014134};
RN [1] {ECO:0000313|EMBL:EOS77710.1, ECO:0000313|Proteomes:UP000014134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-1 {ECO:0000313|EMBL:EOS77710.1,
RC ECO:0000313|Proteomes:UP000014134};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 10-01.";
RL Submitted (APR-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:EOS77710.1}.
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DR EMBL; ASTF01000005; EOS77710.1; -; Genomic_DNA.
DR STRING; 1235800.C819_00821; -.
DR PATRIC; fig|1235800.3.peg.888; -.
DR eggNOG; COG0249; Bacteria.
DR eggNOG; COG0553; Bacteria.
DR eggNOG; COG0827; Bacteria.
DR eggNOG; COG3170; Bacteria.
DR eggNOG; COG4646; Bacteria.
DR HOGENOM; CLU_000181_0_1_9; -.
DR Proteomes; UP000014134; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR Gene3D; 3.40.1170.10; DNA repair protein MutS, domain I; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
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; PF01624; MutS_I; 1.
DR Pfam; PF04851; ResIII; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF55271; DNA repair protein MutS, domain I; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000014134}.
FT DOMAIN 2605..2834
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|SMART:SM00487"
FT REGION 285..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1614..1650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2747..2774
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 285..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1626..1650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2839 AA; 318709 MW; 02C36391E758BAAC CRC64;
MARKLQLVSE LANQTARNIT RDVDGWKQYL DTASRLYKYK FDEQLLIYAQ RPDATACAEM
ELWNEKMRRW VKAGSKGIAL IRGAETGRPH LEYVFDVADT RPVRGARMPY LWEMREEHHA
PVLAALENRY GEGSRKELGG GLMEIAAKAV EEACPEYLRE LAYDAEGSFL EGLDQLNLEV
CFRDTLTASV QYTLLTRCGL DPSDYMEDEE LAGITEFSTP AVLHHLGSAA STLSMEILQE
IGKVIRNYDR EVMAGRQKNI QKTAENSLAK STGIGYTKVT EQFNTLKRES KERSEDHGRT
DIHEERGLSD TGADAGRGGR TGGDADWEVR DAAADLPHGE PSRDVHLHAA DGEADTPLTA
DRRTGTGAGR PDSGRDDETA GSGREPERTR PDGVGAGGEQ PDGTGGGSGA SGDRLQVGQE
EQKNEKEQET AGDEPAVSAP EYFQISLFPT VEEQVERIAQ AKEERKTADS SAHGRKPVPE
VPKGVIGRAL TSGGNEKNST MRIAAFYQKS PSIEEAAAFL QKEYGTGGKG LTVAGEKYAL
WFDKEGIKIA PGRTANVPGA TLVTWEQAAG QVSELLEEGI YATQEILDTA RGNEYQELAA
KLWYLRQDLS EEAASSGFLP HVSELYGGFP DSTEKIAGLL EGKESRDIFV SELTDFVRAY
EADRDLMRFH FHNPQEILNG LLNLDIEPRQ FRGTEGFEPA KGSFITEDEI DRMFMRGSGV
SEGKMRIYSF FCQGHDARER ADFLKNEYGD GGYGSQGYNE WHDSKGIKFT RSDEASGFDG
YDTVKMNWNQ AQKRIGELIE AGRYLNPKEM AYTSEYEKIR LARSIYAFYF YCPGTPNPSN
SIEWDVDAAE RDFKPMLDDA KISAALYEDM LESFATVTPE ESRSYGIMQR AIEDMGAYQR
GEYSLFTPLP EETLRAERQK REAAKKEAKE KQNVSKKEKE PLGELEAAAR ALAQKQKNLA
KEQPGKVKER PDGQLTFDFM AVNEEDAGQA DTASSKTGSD LEQIKEQEEA VLAHYDIGYG
FLGNGLTVWN RLEEEHGDYK TVAHIDADRS VTFYDEGLPE AVKEQIRKVA AETQMNISAT
QEAPVFSTPT QAEPEIRAEK DTKASPAGKS AAELYREALS MLSDVVRQSS FYSYLRDRET
DYDSAAAELD NELGFFINEI VESQPDLYDA FQSLPMFRAW MVEDILERTY QDVVTDSRDA
IERHAGEPDV PEWAKETEAA SVQRQAAPED AEPIESGNTD NLLTEENSGQ EKAGAGEPET
QGKKKGRTLP ELNYRAFMRL FPDFTSQHYT AMQMRAGESM MPLHIEAVGS DEISIAHYYR
QNGDSMADPE MTFRIDHEKG TLEPLTYQQD SMGMYQQVYP EPGRWIPKLR KDLNRFANQW
FHNIEEQRYR PERAVMEADG DRKEIFYQDG KPVIKEEPAP VLEGTEKDTG TVQAETDLAP
NVEEYLNLKA EHPDKLVGVQ VGEYILFYGK DAEAAAPALS AKLLTREIDG LGETSVTGGR
VWQAVVKDLL EHGQSVVIAR PDPERGENAP YEIVKERDIA DYIPLGMKLT IDGRHMEVDS
IDYENGRVSL KDLDMQGWFP IFREESVPFV RECVKQEWEN DLEHGNFPED MAQAGMDAGG
QAEEAHTAPE PEKDAVYREE AETQVPDSRD MEEAKRLIED FCLEEYNEDS VDFTNLEEVG
IAYGTTENGG FEVQVNVDLI HFSLSQFVDG KCVEKRQYDS LRELIDGELA FLDYDQLIYV
EPHIEEQLEA GLNEKIWREE MQGAREGVFP TEPESADREE EKLPEMVEIE GGQVITAETV
GVYSKGLPYE IVVEKLHTGP DRSNFRITDD ALGEGGQKTK YQNNIAAIRT LKQIEAENRL
ATPQEQEVLS KYVGWGGLYQ AFDADNQKWG KEYGELKELL TPEEYESARS TVLNAHYTSP
VVIKAMYEAV KRMGFKPGNI LEPSCGIGNF FGLVPEEFEK SNLYGVELDS LTGRIAKQLY
QKADITVGGF ETTDHPNDFF DLAVGNVPFG EYKVHDRQYD KQNLLIHDYF LTKTLDKVRP
GGVVAFITSK GTMDKANGRV REALAQKADL LGAVRLPNNA FKANAGTEVT ADILFFQKRG
SAPEKLPDWV NVGQTEDGVP LNNYYLQHPE MVLGRMAFWE NMYGNATETA CIPLEGADLK
EQLAEAVTHI GTPDQELLHM DAPEQEGKEK EETIPADPQV RNFSFAEKDG KLYFRENSRM
KRMEVGKMPA ARIRGMIAIR DSARQLIDLQ LNGADDAQIG KEQERLNTLY DNFQKKYGLL
NSAGNRLAFR QDSSYPLLCS LEVLDEEGNL KRKADMFTKR TIKHRQSVTS VDTAVEALGV
SIGERACVDL GFMASLMGGS DKIPQIISDL KGIIFKDPDS GPAVISEENT DWHKGWQTAD
EYLSGNVRKK LERAKKAAEE YPEFAANVEA LTAVQPKDLT APEISVRIGA PWIDTRYYRQ
FLFELLQTPG RLQNGRIDVM YSDVTGEWRI KGKSEDSITN TRVHTTYGTK RINAYEIFEA
SLNQRSVQIF DTHTDIEGKE TRVLNEKETA IAQQKQDAMK EAFHDWIFKD PDRRADLCGI
YNKLFNSTRP REYDGKHINF IGMNPEIKLE PHQRNAVARI LYGGNSLLAH VVGAGKTYEM
IAAAMESKRL GLCKKSIMVV PNHLTEQWGG DFLTLYPGAK VLVATKKDFE PKNRKKFCAR
IATGDYDAVI IGHSQFEKIP ISPERQAAII QGQIDEIVDA IAEAKANKEE KFTVKQMEKT
KKNLEAKIKK LYDKKKDDTV TFEELGVDRL FVDEAHSFKN LYMHTKMRNV AGISQTDAQK
SSDMFAKCRY MDDVICCEL
//