ID E4SC14_CALK2 Unreviewed; 756 AA.
AC E4SC14;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=Calkro_0020 {ECO:0000313|EMBL:ADQ44939.1};
OS Caldicellulosiruptor kronotskyensis (strain DSM 18902 / VKM B-2412 / 2002).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=632348 {ECO:0000313|EMBL:ADQ44939.1, ECO:0000313|Proteomes:UP000006835};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=2002;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Blumer-Schuette S.E., Kelly R.M., Woyke T.;
RT "Complete sequence of Caldicellulosiruptor kronotskyensis 2002.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ44939.1, ECO:0000313|Proteomes:UP000006835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18902 / VKM B-2412 / 2002
RC {ECO:0000313|Proteomes:UP000006835};
RX PubMed=21216991; DOI=10.1128/JB.01515-10;
RA Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A.,
RA Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., Woyke T.,
RA Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., Detter J.C.,
RA Walston-Davenport K., Han S., Adams M.W., Kelly R.M.;
RT "Complete genome sequences for the anaerobic, extremely thermophilic plant
RT biomass-degrading bacteria Caldicellulosiruptor hydrothermalis,
RT Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor kronotskyensis,
RT Caldicellulosiruptor owensenis, and Caldicellulosiruptor lactoaceticus.";
RL J. Bacteriol. 193:1483-1484(2011).
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; CP002330; ADQ44939.1; -; Genomic_DNA.
DR AlphaFoldDB; E4SC14; -.
DR KEGG; ckn:Calkro_0020; -.
DR PATRIC; fig|632348.3.peg.23; -.
DR HOGENOM; CLU_008504_0_0_9; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000006835; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 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}.
FT DOMAIN 12..351
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 378..627
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 756 AA; 88991 MW; 7153920CC150A593 CRC64;
MNIMHYAEKF SKSPLTETQQ NILKVNFPFY LKAGAGTGKT ELLVELIIKC LNENPKASIS
NFVVITFTNK ATSEVKRRLV ERLYFDYSLN HKKLSSLSSL LADNRNIMNR QEDEKRKFVD
LTSMLNVYTI HGFCEIILRQ YGYLIGISPK FEIKSVTWKL NEIIRKAIDN YAENEFLNVL
PSYRLHQLVR TLYEECDNKG DEITEKDIKN KFRKNQEQYF WSNFKDSFLD LFLEVGREIE
NFKKENNILT PNDLIKYASK LVKGNDFVAT KLASKYKYLF IDEFQDTNRS QFELVNTLLE
KGVNIFLVGD EKQSIYSFRG ADIQSSIEMG NIIANKCNSP LIEMTDNFRS NKNVIEVINK
IFSQSYSATY KGKLYQIKFD NYQPLIFPQI NKSYVDQRSF PQYKWKGKTS KIENTLTIEE
MDISTIIKKI KNEMCYSDNS DIKYSDIAVL CRKNRQVEKI ADELKKNKIP VKIYGGGGFF
QSNAIISTCK LFEYISYPSE ITKHEVKNTD YYFAMLSTGR NDLEKFLNEL SLYARSNIVA
DILNFVFENT NIEEYYISTS QHQELYNLYK LREIVRNIHN QEFLHPLSFF EYLNNMILTG
QKEENADFIE DKQQDSIQVM TIHKSKGLAF NIVIIPFIDE PIVISDTEPL ITYRKTEKEM
MIGFNKHKLK IYNNIEDDLD FSSMVTDEIK KQFEEELRVY YVAITRAREL IILKTNNRRE
NNIYRNTITS FLDWIKQIDN FNFYNKHFKL LEKGKL
//
