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Database: UniProt
Entry: A0A376BMI8_9NEIS
LinkDB: A0A376BMI8_9NEIS
Original site: A0A376BMI8_9NEIS 
ID   A0A376BMI8_9NEIS        Unreviewed;      1375 AA.
AC   A0A376BMI8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   Name=recQ_2 {ECO:0000313|EMBL:SSY70855.1};
GN   ORFNames=NCTC10283_00970 {ECO:0000313|EMBL:SSY70855.1};
OS   Alysiella crassa.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Alysiella.
OX   NCBI_TaxID=153491 {ECO:0000313|EMBL:SSY70855.1, ECO:0000313|Proteomes:UP000254209};
RN   [1] {ECO:0000313|EMBL:SSY70855.1, ECO:0000313|Proteomes:UP000254209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10283 {ECO:0000313|EMBL:SSY70855.1,
RC   ECO:0000313|Proteomes:UP000254209};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) 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=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
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DR   EMBL; UFSO01000002; SSY70855.1; -; Genomic_DNA.
DR   STRING; 1120980.GCA_000745955_01174; -.
DR   Proteomes; UP000254209; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
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   CDD; cd17932; DEXQc_UvrD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 6.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF13245; AAA_19; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF13361; UvrD_C; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000254209}.
FT   DOMAIN          52..230
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          260..407
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          825..1154
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   BINDING         846..853
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1375 AA;  156657 MW;  2013EDDE3205BA0C CRC64;
     MASILRQIRG TPCAEHCPYC QTHLNAERHL QKYFAYPSFR EYNGKPLQAQ AAQAAIAHQS
     LLAIFPTGGG KSVTFQVPAL MAGEHSKALT VIISPLQSLM KDQVDNLEQR GITEAVTING
     LLDPIERQKA VQRVQDGSAS LLYISPESLR SRTIEHLILG RNVARFVIDE AHCFSAWGQD
     FRVDYLYIAE FIQRIQTHKQ HAIPVSCFTA TAKPQVVEDI KQYFKKNLDL DLQVFAADVG
     RKNLHYQVLP QKNDDERYQT LRHLIQQHNC PTIVYVSRTR KTQELAQQLM QDGFAALPYH
     GKMENEQKIA NQNAFMTGEA QIMVATSAFG MGVDKKDVGL VVHYEISDSL ENYVQEAGRA
     GRDEQIQAAC FVLFQLEDLD KHFILLNQTK ISQKEINQIW KAIKDLCGKR SQITESALNI
     AKQAGWQDEH IDEIETRVKT AIAALENAGY VKRGQNMPCV YANSILAKNA QEAIEKIAQS
     QIIHPDQKSH AVRVIKKLFS QRSQIHATDE QAESRVDYMA DVLGLKTETV VKIVSWLRME
     GILADQQDLR AFIRHNGRSQ DVITRLSHLA DLERALLAQF KEHDGVLHTS YKALNQLFSG
     SLKFSNPKII KSLLAFWKIK NWLGRAETQY DEIALAMKLP LPDVAQWLER KHFLAQFAVR
     YLHDLRDLSH QAAAENPDLA YVEFSLGGLQ KAFAQQNLSD IATLEEWEDV LFYLVRMDLL
     KIEGGFLVVY QRLHVQRLIA DNRKQYTKDD YTQLAHYYQM RQEQIHIVGK YAQTMMNDVQ
     AALKLVRDYF SLDYRQFLRH YFPAQESESL KRNMTAARFE QWFGNLSPEQ RQIIQDNQSQ
     HIVVFAAPGS GKTRVLVHKL ASLYQLEDVK HEQLLMLTFS RAAAHEFKSR LFDLIGNAAA
     YVEIKTFHSY CFDLLGRVGD LQQSDDIIAQ AIAKIQSGEV ESTRIAKLVL VLDEAQDINA
     TQFELVKTLM AHNEDMRVIA VGDDDQTIYD FMGASPHYMQ TLLRDFGATK YELLANYRSK
     SEIVRFCNHF ASHISQRLKE NDVAAVQTET GQVEYVAFSG SVLPLLLDKV QAAQGHSVAV
     LTHTNEEAIW LAGELKQAQI PCKLVQGNDG FRVHDLLEVR VFEHFLALHG KAVIDEIAWQ
     TAKQRAQTHF SRSQHLSLLN NLLGDFEHTH PKTKYVSDWY NFVQESALEN FDRAHQASVH
     VSTIHKAKGR EYDDVLVYLN QAACERDEQK RLLYVAFSRA KSHLCIFANH AHLHKMCANV
     GAEIPFYRGE AIAPARELAL YLNHGDVNLG RFAACARAVR ALQAGDKLLA DGEKCCDLSG
     NAVLYFSKKF REKLAHYQQS YYQISHAEVN FIVLWHNKEN DETSRIVLPI VYLRR
//
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