ID   I0AM18_IGNAJ            Unreviewed;      1043 AA.
AC   I0AM18;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   OrderedLocusNames=IALB_2322 {ECO:0000313|EMBL:AFH50025.1};
OS   Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS   Mat9-16).
OC   Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC   Ignavibacteriaceae; Ignavibacterium.
OX   NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH50025.1, ECO:0000313|Proteomes:UP000007394};
RN   [1] {ECO:0000313|EMBL:AFH50025.1, ECO:0000313|Proteomes:UP000007394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC   {ECO:0000313|Proteomes:UP000007394};
RX   PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA   Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA   Bryant D.A.;
RT   "Complete genome of Ignavibacterium album, a metabolically versatile,
RT   flagellated, facultative anaerobe from the phylum Chlorobi.";
RL   Front. Microbiol. 3:185-185(2012).
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; CP003418; AFH50025.1; -; Genomic_DNA.
DR   RefSeq; WP_014561174.1; NC_017464.1.
DR   AlphaFoldDB; I0AM18; -.
DR   STRING; 945713.IALB_2322; -.
DR   GeneID; 78243916; -.
DR   KEGG; ial:IALB_2322; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_010384_0_0_10; -.
DR   OrthoDB; 9762792at2; -.
DR   Proteomes; UP000007394; Chromosome.
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:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR049035; ADDB_N.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   PANTHER; PTHR30591; RECBCD ENZYME SUBUNIT RECC; 1.
DR   PANTHER; PTHR30591:SF1; RECBCD ENZYME SUBUNIT RECC; 1.
DR   Pfam; PF21445; ADDB_N; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007394}.
FT   DOMAIN          19..272
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21445"
FT   DOMAIN          282..628
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13361"
FT   DOMAIN          741..1038
FT                   /note="PD-(D/E)XK endonuclease-like"
FT                   /evidence="ECO:0000259|Pfam:PF12705"
SQ   SEQUENCE   1043 AA;  121888 MW;  EC390EDC495BB688 CRC64;
     MILSKKNLKQ IDIDFILNEK IQNEKLNETL IVVPTNRKVR SLKRELISLS PNGATANLHI
     HTLSTLSLSI FKLTNLSEFF LLDDATAVVL LNKAFHKIKP TYFANYQDEV PAGTLDRIKN
     VISEYKRNGV SPDLLYEQAK NLTGSEKNKA NDIAKIYADY FNECSQNNLF EIGDIYKFLN
     ELSDKDFQKA FDELFNEVNF VLVNGFDEFS NPEIELLNRI SECREDFFIQ FDYYKYNPAL
     FGHLDECFSK FEKRGFKEIT DLSESQNLHF HSVIREKLFD FQKHKPQSVN EKIFIVNPAT
     PEKEIEFIAK EIKRLLFEEK VQPEKICVAF NLISEHSKVV RDIFTEYGLP FNLTDRFALS
     ESQPIIALIN LLEIIENNFF YKNIFRTLSG RWIELDGIDL SNLLQVASNL KITAGYNNWI
     ESIDNALEEI KNLNEDDERN FLPEENYLKA KEDIISIAEM LNPFKSKLTV DEFRNELDNL
     IVRLQLIPKA INDHKDYAEK NVRAITSFVQ TVHNLFELMR IELGEKPKHS VSFYLKNIKT
     ALQFARYNLR EKIDSGILVT SINEIRGLNF DYLFIGGMTD GEFPTRYQPE IFLSGSFRKE
     DYKHILEERY HFYQALCAVK KVLYLTYPNS DERKQFTAST FIKDLKNVIN TLEINAGNYD
     KLIASEKELL SAINKNDLNS DQVNQNLIEA GFNPENILED IKIDELRIQN PFDEIPYNGF
     LSEQLSKESL EKLKALSDRT YSATQLEEYA KCPFQYFLRR ILLIETIEEP TEEIEAFELG
     SIIHSILYTF YKTIKEQKRK IENCSEEEFA EFVQLIFSIA RKKTEHIKFS SPYSFFEYEK
     IFGINGNIKH SILYKFLEEE RKDKEGFEPL FFEISFGKRT NSSIEVKLNE INFSGKIDRI
     DVNEEDKLYQ VIDYKLSGRK PTREDFNLGI SLQLPLYLYA SKLLLKAEFK KEYQPASAEI
     YSLKIFNEEF GRKIAHNLPG RKFTQEDYLK ASEDLIKIFE EVVPKYIDNI RKGVFNLSLL
     EKREDKVCGF CEFSSICRIR ELG
//