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Database: UniProt
Entry: U2CLX1_9FIRM
LinkDB: U2CLX1_9FIRM
Original site: U2CLX1_9FIRM 
ID   U2CLX1_9FIRM            Unreviewed;      1080 AA.
AC   U2CLX1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Protein, SNF2 family {ECO:0000313|EMBL:ERI91534.1};
GN   ORFNames=HMPREF1982_03179 {ECO:0000313|EMBL:ERI91534.1};
OS   Clostridiales bacterium oral taxon 876 str. F0540.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1321778 {ECO:0000313|EMBL:ERI91534.1, ECO:0000313|Proteomes:UP000016490};
RN   [1] {ECO:0000313|EMBL:ERI91534.1, ECO:0000313|Proteomes:UP000016490}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0540 {ECO:0000313|EMBL:ERI91534.1,
RC   ECO:0000313|Proteomes:UP000016490};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:ERI91534.1}.
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DR   EMBL; AWSZ01000063; ERI91534.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2CLX1; -.
DR   STRING; 1321778.HMPREF1982_03179; -.
DR   PATRIC; fig|1321778.3.peg.3140; -.
DR   eggNOG; COG0553; Bacteria.
DR   eggNOG; COG4715; Bacteria.
DR   HOGENOM; CLU_000315_21_1_9; -.
DR   OrthoDB; 9760715at2; -.
DR   Proteomes; UP000016490; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
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   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   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:UP000016490};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT   DOMAIN          59..105
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50966"
FT   DOMAIN          633..790
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          910..1074
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1080 AA;  124800 MW;  C7300FC81AAA8954 CRC64;
     MLKEDILLQL FKESTSGKNY DMGYKIIDND LVSSVNVNSE GELICIDGFV ISENLFNEYT
     TKIELDASKK EVFSTFCSCA DYEKNEFKKK NYVCKHVAAT FYKALEELIN HPLFNEEETT
     NEVGINNGRL LEMLLGEKKD KEELKLDVYI NRKEWNDDIS AEFRLGIKSM SSNSLYILKD
     IEQFLVSLYN NMPVTYSKNF TFDTKYQKLS TKDKKLIDFI EMLKTIEGSN KYINRSSAGA
     VEGKYLNIPK YLVREFFSII KDHRVYLNEG FFHRPVEAEI LYEAPPIDFD LKLIKNEYVL
     KSPNGMPQSL GSKKDVFVYG SDIYIPDYEF CYKISPYLQV FAGQKVVLFP IEDEETVLRR
     LIPQLNFLSS KVTLSKVIKD KIVMGSCNFS FYFDREEEQI TLVVKVSYEG CEFNIFEDYK
     EKIVYRDSLK EAEVISVLRG FGFEDIGNRF YFNKEDDYIF RFFKYEISKL QEIGEVYYSD
     NFKGLKSIGS KGIKGDIKAG KFNYFEMDFK IGDIPPKETA DILRAFRDNL KFYKLKSGEY
     IDLEELELNK LLKLIDAVAM KGIEDNHIEI AKNRAAYIES FIEENEVRFI KGKTELKKVS
     DKLKNIASLK FEQPKGLLAD LREYQKTGYN WFKTLDYLGF GGILGDEMGL GKTLQTIAFI
     LSNEGSKSLI AAPTSLVYNW VSEFEKFAPT VRVAAVNGTK EEREEIIKKL DKYDVFITTY
     NLLKRDLDSY ASIEFDYFVL DEAQYIKNSG SQNALAVKEI KAKTRFALSG TPIENSLMEL
     WSIFDFIMPG YLYDEKRFSV RYHKRLREEP VVIEEINRLI KPFILRRRKK DVIKELPDKI
     EKTVAVDMDE DQKKVYKAYA NYAVELIEKK VEDYEFQNSR IEILSYITKL RQLCLDPSVL
     MGNYKGESAK IEALVELLQQ SIEEGHRVLI FSQFTSVLKN IGKRISKEGI NYSYLDGSIP
     SEKRMNMVKA FNEGENSVFL ISLKAGGTGL NLTSADVVIH FDPWWNPAVE EQATDRAHRI
     GQKNVVEVIK LIAKGTIEEK ILKLQEDKRK LISEVMGDEL SSGEGFASLS EEELLELFSM
//
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