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Database: UniProt
Entry: A0A059KMJ7_9BURK
LinkDB: A0A059KMJ7_9BURK
Original site: A0A059KMJ7_9BURK 
ID   A0A059KMJ7_9BURK        Unreviewed;       667 AA.
AC   A0A059KMJ7;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Helicase c2 {ECO:0000313|EMBL:KDB52429.1};
GN   ORFNames=X805_20440 {ECO:0000313|EMBL:KDB52429.1};
OS   Sphaerotilus natans subsp. natans DSM 6575.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Sphaerotilus.
OX   NCBI_TaxID=1286631 {ECO:0000313|EMBL:KDB52429.1, ECO:0000313|Proteomes:UP000026714};
RN   [1] {ECO:0000313|EMBL:KDB52429.1, ECO:0000313|Proteomes:UP000026714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6575 {ECO:0000313|EMBL:KDB52429.1,
RC   ECO:0000313|Proteomes:UP000026714};
RX   PubMed=24965827; DOI=10.1111/1574-6941.12372;
RA   Park S., Kim D.H., Lee J.H., Hur H.G.;
RT   "Sphaerotilus natans encrusted with nanoball-shaped Fe(III) oxide minerals
RT   formed by nitrate-reducing mixotrophic Fe(II) oxidation.";
RL   FEMS Microbiol. Ecol. 90:68-77(2014).
CC   -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC       {ECO:0000256|ARBA:ARBA00038058}.
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:KDB52429.1}.
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DR   EMBL; AZRA01000050; KDB52429.1; -; Genomic_DNA.
DR   RefSeq; WP_037481359.1; NZ_AZRA01000050.1.
DR   AlphaFoldDB; A0A059KMJ7; -.
DR   STRING; 34103.SAMN05421778_11523; -.
DR   PATRIC; fig|1286631.3.peg.2010; -.
DR   eggNOG; COG1199; Bacteria.
DR   Proteomes; UP000026714; 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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR027417; P-loop_NTPase.
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; PF13307; Helicase_C_2; 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:0000313|EMBL:KDB52429.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          25..309
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
SQ   SEQUENCE   667 AA;  72552 MW;  E867E656E24E5107 CRC64;
     MSEPFSDDAF ALRAEVARAF AEDGDLARLD PRFRPRPGQT RLADAVAQAL DSRDVLVAEA
     GTGVGKTYAY LVPLLLSGLR AMVSTATKGL QDQLFLRDLP RLARLFGLPV QVALLKGRAS
     YLCLHRLTLA RQAPEPLDVF ALRQLARIEV WAQGTRSGDL AEVEGLDERS AVIPLVSSTR
     DNCLGADCPS WRQCHVVQAR REAMQADIVV VNHHLFFADL TLRDTGMAEL LPSVDAVVFD
     EAHQLNEAGV QFLGRTLASA QLMDFGRDLL AAGLTQARGF GPWQELAARC ELAARELRLA
     CAGPGRASVR LRWEERAGQA PFDEALERVA RVAAEAADHL EAVEAAGPDL QRLLERARSL
     LSRAEAFGAE LEPGRVRWID AGAHQARLTE SPLDVRETLR AQVESGRRAW IFTSATLGDE
     PSLAWFTRRA GLDEARTLQV VSPFDYAGRA RLLVPRPFPR PAEPQHPDEV AALAGRCARA
     LGGRTFVLTT TLRALQRIGE RLRALLRPGG IEVLIQGEGP KRALLSRFLE RPRAVLVGSH
     SFWEGIDVPG DALQCVVIDK LPFPPPGDPL AEARSRAIEA EGGSAFNDLF VPETAIALKQ
     GAGRLIRSES DRGLLVICDT RLVQMGYGRR LLAALPPMRP VADEAEALAW LAQLGEPSAP
     ASPPEPV
//
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