ID B1KS08_CLOBM Unreviewed; 1350 AA.
AC B1KS08;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=DNA helicase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=CLK_3276 {ECO:0000313|EMBL:ACA55297.1};
OS Clostridium botulinum (strain Loch Maree / Type A3).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498214 {ECO:0000313|EMBL:ACA55297.1, ECO:0000313|Proteomes:UP000000722};
RN [1] {ECO:0000313|EMBL:ACA55297.1, ECO:0000313|Proteomes:UP000000722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Loch Maree / Type A3 {ECO:0000313|Proteomes:UP000000722};
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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DR EMBL; CP000962; ACA55297.1; -; Genomic_DNA.
DR RefSeq; WP_012343299.1; NC_010520.1.
DR KEGG; cbl:CLK_3276; -.
DR HOGENOM; CLU_000738_1_0_9; -.
DR Proteomes; UP000000722; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049468; Restrct_endonuc-II-like_dom.
DR InterPro; IPR047187; SF1_C_Upf1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF8; HELICASE WITH ZINC FINGER 2; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF18741; MTES_1575; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 266..393
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1011..1194
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT DOMAIN 1237..1329
FT /note="Restriction endonuclease type II-like"
FT /evidence="ECO:0000259|Pfam:PF18741"
SQ SEQUENCE 1350 AA; 159631 MW; 32ADDAC3D720ED76 CRC64;
MKCSEKIKNI FYYLLRIKRM NKCSSDVRTY EALYTKKDIL NNSYCNVSRD KEDNVTIKIS
KEAGKIYDKI YKQYLDGGNE NEIILGQAIL ALRKNKNIIH PVITSKVKVD FIDKENVLSL
KIPSNIKLEI EVCDCLNKTL FKKIISRKNY WEKEKIDIMN YDNIKDKIQL LLNNDSEIVF
KDIEDLNKIE ITEEPVIYNC PILVIRKTDN SLWSKEFESI AEEIDNGYDI PKTIEALVEE
KEIEDDYIHK DQWKECKEDI LFPLDANEEQ ISIVKKICEN EAILVQGPPG TGKSHTIANL
ICHFLAHGKK VLITSETSRA LRVLINKIPK DIKPLCVNLL DDNNGEYELE QCIKNISDNL
CKNPSEIIDD IYILNNERKE CKKNQQVLYN KLKEIEFMEN KKIHCKGNYY KLIHIGSWLN
ENEYKYGWIR DNIRYEDIKP VNEEQFNKLI ELLKNNGKEY IGNINELIFI CNKIPSYNEV
ENKLDRMIYL ESNLNFYKDK IKGWYIPAEC KCNYDILSDF LYDCIEKMKN ITKDPMLGKM
FELYYSSEIF RDSINNFTLN LNSSKEKLIK IRANINRYSI EIKEIKDMDM FIKDYERVYS
KIKGKKKISK IFKVINSKYD YIFKNCYING ENIKSIEQLN IINDYIEERK IYNFLNRLWE
NIINSYIQED SNYNIDNLIS IERITNNLDT IMNWNREYRD KIIKLLGRIR IPININWYEI
NTYEYFIQCI ECIKAINEYN DLKAFMEIIK KQVRNFESLN PIIKGIDKEN IDYIKEAYSY
IEKIMSMKSD MDEINYIYKK LEESCPRTLE FILENYKKNY KFNSWENAWK WAQYNNLFKK
LEKIDEKTLQ GQLIEEKNKE KEIINQIISK KAWKNIILNI NEGEKRSLFS WVQAVKRIGK
GRGKFVLQYS NIAKEEMEKC KSIIPVWIMP LEKVIENIKP SKEQFDVVIF DESSQSNIFA
ISALMRAKKA IIVGDDKQIS PEIVGMDQGM ISNFIDKYLD GIPHNQWFDL QTSLYDTALR
TFKDRIMLKE HFRSVPEIVQ FSNKLCYGDL IVPLRYPKIK EAFNSPIKCI KVEDGYREKT
KQININEAKA LVNKLLECCR DSKYNGMTMG VISLLGDAQS EFIENLLKNN LSKEEIKIRK
LVCGDAYSFQ GDERDIIFLS MVVGDNMKYT ALTKETDIKR FNVAASRARN QIFLFYSIDY
KNINNDCVRY KLIDYCNNYK NYKSKLPDIN YVMQSKFQKD IYNNIRNLKC DIKSNIKLGK
YIIDFILEGE HNRIAIICDD GNLYENNNVE KVLNLEMDLT RLGWAFYKIR GSKFYRNPEV
EVEKLHKFLI ESGLYKDDSK EILKNNLLVV
//