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Database: UniProt
Entry: A0A221MHY0_9BACI
LinkDB: A0A221MHY0_9BACI
Original site: A0A221MHY0_9BACI 
ID   A0A221MHY0_9BACI        Unreviewed;      1047 AA.
AC   A0A221MHY0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Helicase SNF2 {ECO:0000313|EMBL:ASN07273.1};
GN   ORFNames=CFK40_02570 {ECO:0000313|EMBL:ASN07273.1};
OS   Virgibacillus necropolis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=163877 {ECO:0000313|EMBL:ASN07273.1, ECO:0000313|Proteomes:UP000204391};
RN   [1] {ECO:0000313|EMBL:ASN07273.1, ECO:0000313|Proteomes:UP000204391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 19488 {ECO:0000313|EMBL:ASN07273.1,
RC   ECO:0000313|Proteomes:UP000204391};
RX   PubMed=12710619; DOI=10.1099/ijs.0.02371-0;
RA   Heyrman J., Logan N.A., Busse H.J., Balcaen A., Lebbe L.,
RA   Rodriguez-Diaz M., Swings J., De Vos P.;
RT   "Virgibacillus carmonensis sp. nov., Virgibacillus necropolis sp. nov. and
RT   Virgibacillus picturae sp. nov., three novel species isolated from
RT   deteriorated mural paintings, transfer of the species of the genus
RT   salibacillus to Virgibacillus, as Virgibacillus marismortui comb. nov. and
RT   Virgibacillus salexigens comb. nov., and emended description of the genus
RT   Virgibacillus.";
RL   Int. J. Syst. Evol. Microbiol. 53:501-511(2003).
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DR   EMBL; CP022437; ASN07273.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A221MHY0; -.
DR   KEGG; vne:CFK40_02570; -.
DR   OrthoDB; 9760715at2; -.
DR   Proteomes; UP000204391; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR013663; Helicase_SWF/SNF/SWI_bac.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR007527; Znf_SWIM.
DR   PANTHER; PTHR10799:SF1020; BTAF (TBP-ASSOCIATED FACTOR) HOMOLOG; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF08455; SNF2_assoc; 1.
DR   Pfam; PF04434; SWIM; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50966; ZF_SWIM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:ASN07273.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000204391};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT   DOMAIN          44..84
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50966"
FT   DOMAIN          612..770
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          880..1037
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1047 AA;  121303 MW;  EC6BEB3F28153BC1 CRC64;
     MQRLFPSQVY ERGLEYFHQG RVTELLYDIN FHVWTATVYG SESYFVEVNT KRWPHELSDA
     YCDCPAFKTY NQCKHIVAVL FAIGKRHKEQ GVFRQVDKFQ KTKDFIQSIT DIQQQKRASS
     LSINRQQLQV EYVCKWTYND TLFLELKVGE KRRLVVKDIH AFLQDVFQER EHFFTKTFTY
     NPELHYFDAE DLELFESIMS IVQNERLYDG HSLYRYQSHI SEGRSISISP LLAKPLLKKL
     VERDFIVDTE RDVFRDISIV EDELPYEFKL EKNNKELALA VKGMQDAIYF TKYELMFDTG
     TFYFPKKDQV PMLEQVSEIS RDNPNLPIPA DQADVFLSEV VPSLKKVGDV QISESVASEI
     IQVPLKAKLY IDLKADWITG RLEYHYGAYQ VDPFNGKKEE DVLIIRDVEK EQQIMQLIEH
     ANFHFNGKEL YIDADEEMLY EFLYDVLPMF ESYVDLFLTS DLRKFYMENE PIPSTSVRLE
     SSNNLLEIGF SIDGINDNEI NQILNAVLEK KRYYRMDSGA LLSLESDEFT SIQELMSELD
     LKKIDIQDGS VQLPAYRGAQ VDALIETKKN YDPTFRKLLH HLKSPEEQVY EIPDNLQASL
     RNYQETGFQW FKSLSSYHLG GILADDMGLG KTIQSITYLL SLKQDLPHLI VAPSSVLYNW
     KNECEKFAPD LRVRVIAGSP LERAAMIDAN TGDEVWITSY ATLRQDIALY QDITFHTLIL
     DEAQYIKNYV TKTSRAIREI KAGHRFALSG TPIENSIDEL WAIFQVILPG LMPNQRNFKQ
     LAHSKIAMLT KPFILRRLKK DVLKELPDKI ESVHVSELTK QQKELYVGYL RELQQETAQS
     LSNQDFNKNR MKILAGLTRL RQICCHPSLF IENYEGKSGK LEQLMETVNN AVANGKRMLI
     FSQFTSMHEI IKKKLEEDGI SYFYLHGQTP SQERVQMSES FNNGEKSVFL ISLKAGGTGL
     NLTGADTVIL YDLWWNPAVE DQATGRAHRF GQKNVVQVIR MVTKGTIEDK IFALQQKKRE
     LIDQVIQPGE QMLSSLSESD IRELLSL
//
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