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Database: UniProt
Entry: Q1MS02_LAWIP
LinkDB: Q1MS02_LAWIP
Original site: Q1MS02_LAWIP 
ID   Q1MS02_LAWIP            Unreviewed;      1073 AA.
AC   Q1MS02;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Superfamily II DNA/RNA helicases, SNF2 family {ECO:0000313|EMBL:CAJ54224.1};
GN   OrderedLocusNames=LI0168 {ECO:0000313|EMBL:CAJ54224.1};
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ54224.1, ECO:0000313|Proteomes:UP000002430};
RN   [1] {ECO:0000313|EMBL:CAJ54224.1, ECO:0000313|Proteomes:UP000002430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ54224.1,
RC   ECO:0000313|Proteomes:UP000002430};
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the causative
RT   agent of proliferative enteropathy.";
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AM180252; CAJ54224.1; -; Genomic_DNA.
DR   RefSeq; WP_011526250.1; NC_008011.1.
DR   AlphaFoldDB; Q1MS02; -.
DR   STRING; 363253.LI0168; -.
DR   KEGG; lip:LI0168; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_000315_21_0_7; -.
DR   OrthoDB; 9814088at2; -.
DR   Proteomes; UP000002430; 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; cd18012; DEXQc_arch_SWI2_SNF2; 1.
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   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:CAJ54224.1};
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:UP000002430};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT   DOMAIN          66..102
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50966"
FT   DOMAIN          622..781
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          911..1067
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1073 AA;  124600 MW;  DE78E9716B741E3C CRC64;
     MNFREENIAR SLIQGFIKGS IPDYIRDVGQ SIIQNNGVQK LTIRKEHDIW YIDSIVQEED
     FQNYSPQLII FIEESRVSHT CNCHEAFMGV CKHIASVAIK LHNDLDKSTD LVEEPIKHNI
     EWRQSFRNFF STSLEPEVGR HYLIFRFYPE PTRLIVAFFR GRQNKTGLSS VHQETTLEQI
     LRNPDWCEQS PQLLKVAQQI GHFLDYYGHR VEIPEGLVSW FFWAIRHEYY LLWRDTNLPC
     TIVSTPLALK LKPSLDDEGL RFYVLLQREG KMPFSLTEED TEITFHGQMP LWVNWNQSFY
     PVQTSLSPTL IKELVANTPI VPQDNISEFL DRVWTRLPSS ELYEPEEFLK IMEPIFQPAS
     YDPKLFLDEE GSLLTLEVQN TYETIHGEFT LPGPNPDFQT GSYIFEGHTF LIRRDQQEES
     ALITQLSEMH FQPRSNKLWF MEPEEAIAFL LDSYPTLVEN WRVYGEKALT RYKVRIAQPV
     ITAKVESNEK EKWFNLDIDV EYDGQHLPLE RIWKAWVRGK RYVQLKDGSY TSLPETWLQK
     LSHKLHALGF DPTKPPKHQF KQFEAPVLDT ILDELPNSET DSFWNSLRNK IRSFKEITPI
     ETPKGLNATL RSYQLQGVSY LNFLSEYGFG GILADEMGLG KTIQTLSFIQ HMVNRKYEGP
     NLIVVPTSVL PNWEREAEKF VPDLKRLTIY GTRREGMFKK VVNSDLVITT YALLRRDLEE
     LEKHYFNTII LDEAQNIKNP NTITAKSVRT IKARMRLCLS GTPIENNLFE LWSLFEFLMP
     GFLGSQHAFQ RGVIKPIRDG DNETLEYLRT RVKPFILRRT KSEVAKDLPP KIENITYCAM
     TDEQNELYTA LTKKLRSQVL ADIETKGIAK SQMSILDALL KLRQICCHPR LLKVDMPGFS
     IGSLASGKFE AFKDMIFDIV EGGHKVLVFS QFVQMLQLIK SWLQITDIPF CYLDGTSKDR
     LEQVDKFNNT PEIPVFLISL KAGGTGLNLT SADYVIHYDP WWNPAVESQA TDRTHRIGQT
     RQVFSYKLIC QNTVEEKILK LQEMKRGVAE AIIPGQDTWK SLTKEDLEML FEI
//
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