ID A0A0C1U4R7_9CLOT Unreviewed; 965 AA.
AC A0A0C1U4R7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=DEAD/DEAH box helicase family protein {ECO:0000313|EMBL:KIE46643.1};
GN ORFNames=U732_3308 {ECO:0000313|EMBL:KIE46643.1};
OS Clostridium argentinense CDC 2741.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE46643.1, ECO:0000313|Proteomes:UP000031366};
RN [1] {ECO:0000313|EMBL:KIE46643.1, ECO:0000313|Proteomes:UP000031366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE46643.1,
RC ECO:0000313|Proteomes:UP000031366};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
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:KIE46643.1}.
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DR EMBL; AYSO01000016; KIE46643.1; -; Genomic_DNA.
DR RefSeq; WP_039632984.1; NZ_AYSO01000016.1.
DR AlphaFoldDB; A0A0C1U4R7; -.
DR STRING; 29341.RSJ17_19400; -.
DR OrthoDB; 9802848at2; -.
DR Proteomes; UP000031366; Unassembled WGS sequence.
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 GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR CDD; cd09204; PLDc_N_DEXD_b2; 1.
DR CDD; cd18799; SF2_C_EcoAI-like; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR021835; DUF3427.
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; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF11907; DUF3427; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50035; PLD; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:KIE46643.1};
KW Helicase {ECO:0000313|EMBL:KIE46643.1};
KW Hydrolase {ECO:0000313|EMBL:KIE46643.1};
KW Nucleotide-binding {ECO:0000313|EMBL:KIE46643.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031366}.
FT DOMAIN 123..153
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 237..387
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 432..633
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 965 AA; 112452 MW; 61752892995CCC70 CRC64;
MKEILDGISE KVISESLDLE ISPKSIIEDK YIIRNKLIVN SQRGNLLNEL KQSLSECKSF
YFSIAFINFS GLQLLLDSFK ELQEEGIKGK IITSTYLNFT EPKALDRVRK FENIDLKVFV
ADKERGFHTK AYIFENEDDY KIIIGSSNIT QRALKSNVEW NVMVISKKET EFVQEVLEEY
QDLWDTTGFV DDEFLEKYEK FINSIRQKED KSIVEFNDYK IITPNIMQKE ALENLDRLRR
TGEDKALVIA ATGTGKTYMS AFDVMQFNPK KLLFLVHRED ILRSAEQTYK SLCKNKNITM
GFYTGNVKEL ESDYLFATVQ TIERNLENFK NDEFEYIVID EAHHSTSPTY EKILEYFNPK
FLLGITATPE RCDTGNIFDV FDNNTALEVR LNEALENELI VPFHYFGITD IDVVDYEGVN
LDNISEVSKR LMINSRVNFI KEKMDFYGFD GIKQKTVGFC VNKEHAYYMA EEFRKLGIDS
IALTGEDSID KRQAFMKKLE DNNDLLKVIF TVDIFNEGVD IPSINQVLML RPTNSPIVFI
QQLGRGLRKH ESKSFLTVLD FIGNHKKAFL IAVALKGGRY YDKDSLRVSV ATEFTNIPGC
SNIQMDRIVQ ERILEQLNTE NFNSLKYLKE EYNEFKSLLG GKIPYRLMDY VKYDGAPDPL
KFINYSKTYQ GFLKKVETGY DGEEVDNKEL NKILKELSNK LPVKRPHEFA IIKHLLNVNV
IDSDTVKKVI LKYLDTVDES TIIHGFRNLN QEFYDTRQKD ENIKLFDYTN GKLIRLISFE
RILANKQYKN ILLDLLNYGL ITYEKRYGSK NFGVPFFKLY EQYQMIDAAL LSNYEKIHSS
FRGSGLITNG KEYFLFVDLH KDEDIKESIN YKDEFINKST FQWQTPNSTS QTSDRGKNII
FNKENKVNLH LFVRKYKEID NKVQPYIYMG KGDTIRFEGE KPITVILKLQ NKVPESLYTE
FIKKV
//
