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Database: UniProt
Entry: I9L7D5_9FIRM
LinkDB: I9L7D5_9FIRM
Original site: I9L7D5_9FIRM 
ID   I9L7D5_9FIRM            Unreviewed;      1082 AA.
AC   I9L7D5;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=SNF2 helicase associated domain protein {ECO:0000313|EMBL:EIW16284.1};
GN   ORFNames=FB4_0795 {ECO:0000313|EMBL:EIW16284.1};
OS   Pelosinus fermentans B4.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW16284.1, ECO:0000313|Proteomes:UP000004324};
RN   [1] {ECO:0000313|EMBL:EIW16284.1, ECO:0000313|Proteomes:UP000004324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:EIW16284.1,
RC   ECO:0000313|Proteomes:UP000004324};
RX   PubMed=22933770; DOI=10.1128/JB.01174-12;
RA   Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K.,
RA   Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J.,
RA   Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.;
RT   "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans Strains
RT   Isolated from a Cr(VI)-Contaminated Site and for Type Strain R7.";
RL   J. Bacteriol. 194:5147-5148(2012).
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:EIW16284.1}.
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DR   EMBL; AKVJ01000066; EIW16284.1; -; Genomic_DNA.
DR   RefSeq; WP_007937214.1; NZ_AKVJ01000066.1.
DR   AlphaFoldDB; I9L7D5; -.
DR   PATRIC; fig|1149862.3.peg.3797; -.
DR   OrthoDB; 9760715at2; -.
DR   Proteomes; UP000004324; 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   Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT   DOMAIN          51..92
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50966"
FT   DOMAIN          633..793
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          918..1072
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1082 AA;  124334 MW;  281409CE23447945 CRC64;
     MLTDAKIQER AATSSSYVKG CQYYRNGNVK DIKYSQHEQA YKAQVVGSEV YTVRVNFNNY
     HEVDGYECDC PAFSSYYHGM CKHIVAVLKV MQAHWEIYFG KGKTTILTHA AQELLDFFNH
     DMLEPSSYQS VPIRMIPTYG FSLESRGKRS WLEFSLGNEK LYVMKNIPQL LDALDTQEEI
     IYGKNFILKP REALFDEQAK SLLHLLQSAY ADDKQLADWN PYASTVSAFG DARRLKMTNS
     NMLKFFTIME EVPFCVEINH EKVSGVQIVK ERPAVNLSVK AVVGGLKLRM ETGNDVFYGL
     DTDFQYIYHQ KTIYKVDPLF ASCIRPLMKC FYENKKSEVY IPEEEAANFF SSVVPALENI
     GTVHISSTLL KKFHKEPLEI EIYFDRFTDG IRARVGFKYG DLTIDPLAPS EGTLHTISGK
     MLLRLKKEEN RILTLFQRYG FVIMEGQLVQ ADEEKTYDFL QEGLHQLQNL AEVFYSDDFK
     NSRITYTGRV SAGVKLNTKT DMLEFSLHYE DMQPSELFAL LASYKLKKRY HRLENGAFIP
     LDSTDLQIVN TLLEQLDLNP ADIENKVIEL PKYRAMYIDS LARESSDFHL GRDHSFKKMV
     QDILEPQDVE YPIPEGIQGK LRDYQKVGFK WLKSLASYGF GGILADDMGL GKTLQVITFL
     MSEKESENIP SLVVAPTSLV YNWQQEVERF APALKVMIIS GNQEERQEQL NHIDEVDLAV
     TSYALMKRDI EFYESRIFKY CFIDEAQHIK NPNTLNAKSV KKIRAKGYFA LTGTPIENTL
     TELWSIFDFI MPGYLKTHKF FSNQFEIPIS KNREGEALTE LGRCIKPFIL RRMKKAVLKE
     LPEKIESRMV NEMTEEQAKL YAAWILQVKT EFENEVQNHG FAKSQIKILS LLTRLRQLCC
     HPSLFIANYH GGSGKLEMLT ELLEDAVSGG HRILLFSQFT GMLAIIKQEL ESRNIGYYYL
     DGSTKAEERI KLVNSFNGGE KDVFLISLKA GGTGLNLTGA DMVIHYDPWW NPAVEEQATD
     RAYRIGQKNS VQVCKLITKN TIEEKIYELQ QKKREMIDAL IQPGENFLAK MSEEEIRKLF
     EA
//
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