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Database: UniProt
Entry: A0A1M6M9F6_9CLOT
LinkDB: A0A1M6M9F6_9CLOT
Original site: A0A1M6M9F6_9CLOT 
ID   A0A1M6M9F6_9CLOT        Unreviewed;       802 AA.
AC   A0A1M6M9F6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Rad3-related DNA helicase {ECO:0000313|EMBL:SHJ80074.1};
GN   ORFNames=SAMN05444401_3901 {ECO:0000313|EMBL:SHJ80074.1};
OS   Clostridium amylolyticum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121298 {ECO:0000313|EMBL:SHJ80074.1, ECO:0000313|Proteomes:UP000184080};
RN   [1] {ECO:0000313|EMBL:SHJ80074.1, ECO:0000313|Proteomes:UP000184080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21864 {ECO:0000313|EMBL:SHJ80074.1,
RC   ECO:0000313|Proteomes:UP000184080};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC       {ECO:0000256|ARBA:ARBA00038058}.
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DR   EMBL; FQZO01000008; SHJ80074.1; -; Genomic_DNA.
DR   RefSeq; WP_073010760.1; NZ_FQZO01000008.1.
DR   AlphaFoldDB; A0A1M6M9F6; -.
DR   STRING; 1121298.SAMN05444401_3901; -.
DR   OrthoDB; 9765586at2; -.
DR   Proteomes; UP000184080; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.275.40; -; 1.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 1.10.30.20; Bacterial XPD DNA helicase, FeS cluster domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR006554; Helicase-like_DEXD_c2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR   InterPro; IPR042493; XPD_DNA_FeS.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   PANTHER; PTHR11472:SF47; FANCONI ANEMIA GROUP J PROTEIN; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF06733; DEAD_2; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00488; DEXDc2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:SHJ80074.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184080}.
FT   DOMAIN          185..472
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
SQ   SEQUENCE   802 AA;  93749 MW;  877B24CA4A59F83A CRC64;
     MSEREVNISV RNLVEFILRE GSIDSKFMSS KRAQEGTKAH QKLQKINSKE FEKYSSEVYI
     KQRVQYENLS IVVEGRIDGI IEEGGKKIIE EIKSTNKELS LIEEDYNLLH WAQAKCYAFM
     YAEEQGLSEI SVMLRYFSLT TEEVKEFIKD YKKEELAEFF FGVLDKYYIW AENTLKWESI
     RDHSIEKTPF PFPYYRSGQR ELAVASYGTI KEGKKLFVQA PTGIGKTIST IFPAVKAMGE
     GKVSRIFYLT AKTITRSVAE EAFQKLKEKG LDLKVLTLTA KDKICFCKGE SCAPESCPYA
     DGHFNRVNDA IFQIITKEQY FTREIIEKYA EMHRVCPFEF SLDIALWSDC IICDYNYAFD
     PRVYLKRFFL EASSSERYAF LVDEAHNLVD RAREMFSSEL VKSDFLKMKK LMKGKAPNLY
     KAANSINSYF IDLRHLCEDD NTTFIVQKKP PEDIYMPIRI FMKEAEEYLT KNANTEGYEE
     LLDLFFKCNG FINITDLYDD HYVTYVDTED RDVKLKIFCL DPSKNLKEAM KRARGEVVFS
     ATLTPLNYFQ EILGGNEEDY RLKLPSPFPK DNIDIMVAPI STRYKDRQDT YDIITDYIYS
     FVTMKKGNYL VFFPSYAYMK EITQRFNERF NDINSIVQQG EMSEEERENF LKEFKEEPSE
     TLVGFCVLGG IFSEGIDLTG DRLIGAVVIG VGLPQICLER NIMKDYFNEE KGRGYEYAYM
     YPGMNKVLQG VGRIIRTEKD KGAALLIDDR FLTPAYERLM PPEWQPYKLI KNREELRDNL
     REFWNKDHEE GFHNDVKEHY VY
//
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