ID   Q0A8F0_ALKEH            Unreviewed;       963 AA.
AC   Q0A8F0;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Helicase domain protein {ECO:0000313|EMBL:ABI56887.1};
GN   OrderedLocusNames=Mlg_1538 {ECO:0000313|EMBL:ABI56887.1};
OS   Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272 {ECO:0000313|EMBL:ABI56887.1, ECO:0000313|Proteomes:UP000001962};
RN   [1] {ECO:0000313|Proteomes:UP000001962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1
RC   {ECO:0000313|Proteomes:UP000001962};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S.,
RA   Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B.,
RA   Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000453; ABI56887.1; -; Genomic_DNA.
DR   RefSeq; WP_011629281.1; NC_008340.1.
DR   AlphaFoldDB; Q0A8F0; -.
DR   KEGG; aeh:Mlg_1538; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_006041_0_0_6; -.
DR   OrthoDB; 9814088at2; -.
DR   Proteomes; UP000001962; 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   CDD; cd18011; DEXDc_RapA; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF971; RNA POLYMERASE-ASSOCIATED PROTEIN RAPA; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000313|EMBL:ABI56887.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001962}.
FT   DOMAIN          49..215
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          408..597
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          357..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          873..930
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        367..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   963 AA;  110607 MW;  2BF56DE22BD13D33 CRC64;
     MTITAHHAKY YAYDLTRQAP PGAADQLSMS LFDASVDLNP HQIEAAMFAL QSPLSEGVVL
     ADEVGLGKTI EAGIVLCQRW AERRRRLLVI CPAAIRKQWA TELQEKFNLP AVVMDSRAYR
     QFQQQGQPRP FEQRAVILVS YHYAARMQDD LRMVRWELVV IDEAHKLRNA YRPSNKVGQA
     IRWATEGRRK LLLTATPLQN SLMELYGLAS LIDDHIFGDP NAFRSQYVNA GGDLAGLRQR
     LAGFCKRTLR QEVLEYVRYT ERRALTQPFR PTDAEQKLYD RISEFLQREN TYAIPDRQRH
     LIVLILRKLL ASSSNAIAGT LESLRDRLID LRDSEQLELD WSSQLIESEE METELLDEWL
     PPEENGEANG KTEDNRPEPK KLRDEISEID SLAKAARAIG VDAKSCALLT ALDVGFQEMG
     RMGAREKALI FTESRRTQDY LKDYLEQNGY AGEVLLFNGT NAGPEAKAIY ENWVGKNQES
     GRATGSRAID ARLALVEHFR DNAKIMIATE AAAEGVNLQF CSLVINYDLP WNPQRIEQRI
     GRCHRYGQQH DVIVVNFLNE RNEADQRVHE LLTEKFSLFN GLFGASDEVL GQLESGVDFE
     KRILAIYQQC RTSDEIETAF RQLQEVLEEQ IKSRIQETRQ TLLEHFDEDV HARLRLRLED
     AQAQLDRIGQ RFWQVTGHIL DGRARFDDAR LVFDLHEPPK ADIRPGRYHL ISKTRSGEQG
     ESPDYGYYLY RLSHPLGEHV IESAKQQPTP TAHLRFNITV HPGRIALVEA LKGKSGWLTL
     ARLTIESFET EEYLLFSGID DEGRSLDNET CAKLFNVAAD NRGPADLPAE VEQRLAAELA
     QHQRATANRS LEANNQHFNA ARERLEQWAE DKMLATEKTL KDTKEQIKAL RRQARQAETL
     EDQHDIQERL KQLEQRQRKQ RRDIFKVEDE IEEQRDSLIA ALEKRLARDQ RSERLFTLRW
     SVV
//