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Database: UniProt
Entry: F2JGE2_CELLD
LinkDB: F2JGE2_CELLD
Original site: F2JGE2_CELLD 
ID   F2JGE2_CELLD            Unreviewed;      1119 AA.
AC   F2JGE2;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=SNF2-related protein {ECO:0000313|EMBL:ADZ81837.1};
GN   OrderedLocusNames=Clole_0077 {ECO:0000313|EMBL:ADZ81837.1};
OS   Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS   RHM5) (Clostridium lentocellum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC   Cellulosilyticum.
OX   NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ81837.1, ECO:0000313|Proteomes:UP000008467};
RN   [1] {ECO:0000313|EMBL:ADZ81837.1, ECO:0000313|Proteomes:UP000008467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC   {ECO:0000313|Proteomes:UP000008467};
RX   PubMed=21398547; DOI=10.1128/JB.00239-11;
RG   US DOE Joint Genome Institute;
RA   Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA   Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA   Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA   Angert E.R., Currie C.R.;
RT   "Complete genome sequence of the cellulose-degrading bacterium
RT   Cellulosilyticum lentocellum.";
RL   J. Bacteriol. 193:2357-2358(2011).
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DR   EMBL; CP002582; ADZ81837.1; -; Genomic_DNA.
DR   RefSeq; WP_013655138.1; NC_015275.1.
DR   AlphaFoldDB; F2JGE2; -.
DR   STRING; 642492.Clole_0077; -.
DR   KEGG; cle:Clole_0077; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_000315_21_1_9; -.
DR   Proteomes; UP000008467; 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: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   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:UP000008467};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT   DOMAIN          55..94
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50966"
FT   DOMAIN          633..829
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          951..1103
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1119 AA;  128587 MW;  A551ED7E14A0C94D CRC64;
     MKITLREIKD VASSYKAYDD GLNYFKEGKV EKIHLRQDED YIEMMSCVHG DTGDYQTRVE
     LYNEKLAWCE CNCLPSFQEE GACKHVEAML LKYYYEVMPD IRRSIKGERY SQNALTYYED
     QVIKEQDLEL GEDEKINAHI KLIDEGAGSF FLGLSVGANK FYVVKDLYEF AEHMLQGNRV
     VYGKNLDFIH DLSVFDEATK PIIQFIVDKT QEYLDILRQV GMYRGFTKAD RKTLPLGPKA
     FDEFFDLVKG QNIEVENGKE IREVLFAEGN PRFEFKIEGE GDYYELSTSL AEYEPIAFSR
     YKYILLKDRL LRLDKSFGND VFPLLKYMYE ARNVHGNKQL DFSETLIKRF ILSSLAKIEK
     HVPVVMNEDI KTAITPEHVH VKTFLDLDGE GNIIGDIQFQ YKGFIFNPYK KLNESETRQL
     EQIARDTPNE YRVGNILKYY NFRTKNGGLH LSEEEDIYAF VRTGINELME LGEVHVTERL
     RHINLVKSPV GSIGLRIENN MLKVELKDVN MPLEEMAAIL NAYKMKNKYY RLRDGSFLDI
     AGGTTIGDLA NIVDGLGMKG SDLAEGEASL PKYRALYLDQ VLRQSEGIEV SRDKYFKQII
     RDVKNVEDAD YEVPKSLKAN LRTYQKTGYR WLRTMAAYGF GGILADDMGL GKTLQMIALI
     LAEKEENEAL SQNQLASQVD DKKQDDAKEA EACNKSQGSL ECLCKPSLVI CPTSLVLNWQ
     TELARFAPSL RVLVIMGTVL ERKTILEQIV GYDVVITSYE LLKRDVDSYE EIQFRYCIAD
     EAQYIKNANT LSARALKLLK SEVRFALTGT PIENSLAELW SIFDFIMPEY LFGYAEFRRH
     YEMPIVKSQD EVVTARLKKL IAPFVMRRLK KDVLKELPDK TETVIYNTME EEQQKLYTAH
     LALAKKEMEE ELKAKGVGAS HIKMLALLTR LRQLCCHPSM YLQDYTETSG KLEQCMEIVK
     DSIEAGHKIL LFSQFTTMLD ILSNRLYSEG IEHFMLTGST KAEERMRLVN EFNTSDIPVF
     LISLKAGGTG LNLTGADVVI HYDPWWNLSS QNQATDRAYR IGQKNKVQVF QMITKNSIEE
     KIKELQDKKI GLTESVLQEG EAFISKMSEE EIKALFSKQ
//
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