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Database: UniProt
Entry: A0A2M9R315_9FLAO
LinkDB: A0A2M9R315_9FLAO
Original site: A0A2M9R315_9FLAO 
ID   A0A2M9R315_9FLAO        Unreviewed;       631 AA.
AC   A0A2M9R315;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Recombinase RecQ {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CDL10_01065 {ECO:0000313|EMBL:PJR03242.1};
OS   Avrilella dinanensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Avrilella.
OX   NCBI_TaxID=2008672 {ECO:0000313|EMBL:PJR03242.1, ECO:0000313|Proteomes:UP000231960};
RN   [1] {ECO:0000313|EMBL:PJR03242.1, ECO:0000313|Proteomes:UP000231960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UR159 {ECO:0000313|EMBL:PJR03242.1,
RC   ECO:0000313|Proteomes:UP000231960};
RA   Leyer C., Sassi M., Minet J., Kayal S., Cattoir V.;
RT   "Description of Avrilella dinanensis gen. nov. sp. nov.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
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:PJR03242.1}.
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DR   EMBL; NIPO01000001; PJR03242.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9R315; -.
DR   OrthoDB; 9763310at2; -.
DR   Proteomes; UP000231960; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   CDD; cd17920; DEXHc_RecQ; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231960}.
FT   DOMAIN          25..193
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          213..367
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   631 AA;  72568 MW;  DF4A776284452A0E CRC64;
     MFEAEYILKK YWGFDSFRPP QEEIVKSVVS GQDVLAVLPT GAGKSVCYQV PAMMNDGITL
     VISPLVALIE DQVESLKQKG IKAVGLTGGL SQQDVFRIVD NCQYGHYKFL YLSPERLKQP
     FFLDKLAQLP VNLVAVDEAH CVSQWGHDFR PAFLDIIQLR NVLPNIPFIA LTGSANDRVQ
     QDIKQLLGLH EPEIFLKSFY RPEIIFSLHI LDNVEETLIK ILNKHPQPAI VYTRSRKYTV
     QIAQRLQSMG FACDYFHGGL TNDDKKKRLQ DWLSEKKPIM VATNAFGMGI DKPNVKNVVH
     IQIPESIENY YQEAGRAGRN GQSSFATMLI HPAEIAHFDN RFARNILSKE DLLTVYKKFV
     NDQQIAYGEG LEGFYYLNLT TFCDKYALNA THTYQAFKFL DKESVLTLYE QNNRNTTIKF
     VLSTEETLNH FKNRPKEELL FEQIVHRYAG TSVIDTKINI GTLGKGTNLD KLTIVNILKQ
     WHQAGICVFN DGDFDLMITL NEPRDDERTI NRVAKDLKVQ NQIKKEQHQA MSGYIDNSDE
     CLYRKILDYF DEKKTERCGK CSACRRQAQK DYSKNHSNEI TENIYAFLAE NRSLEEISAY
     CQLEKELIID LLSKMLEEDK IVFNPPYYHQ K
//
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