ID F8N7J5_9BACT Unreviewed; 977 AA.
AC F8N7J5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-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 ORFNames=Premu_2061 {ECO:0000313|EMBL:EGN57455.1};
OS Hallella multisaccharivorax DSM 17128.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hallella.
OX NCBI_TaxID=688246 {ECO:0000313|EMBL:EGN57455.1, ECO:0000313|Proteomes:UP000002772};
RN [1] {ECO:0000313|Proteomes:UP000002772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17128 {ECO:0000313|Proteomes:UP000002772};
RX PubMed=22180809; DOI=10.4056/sigs.2164949;
RA Pati A., Gronow S., Lu M., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Mavromatis K., Mikhailova N., Huntemann M., Chen A.,
RA Palaniappan K., Land M., Hauser L., Detter J.C., Brambilla E.M., Rohde M.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Ivanova N.;
RT "Non-contiguous finished genome sequence of the opportunistic oral pathogen
RT Prevotella multisaccharivorax type strain (PPPA20).";
RL Stand. Genomic Sci. 5:41-49(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; GL945017; EGN57455.1; -; Genomic_DNA.
DR RefSeq; WP_007575022.1; NZ_GL945017.1.
DR AlphaFoldDB; F8N7J5; -.
DR STRING; 688246.Premu_2061; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_1_2_10; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000002772; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 3.90.320.10; -; 1.
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; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 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}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000002772}.
FT DOMAIN 1..327
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 328..602
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 977 AA; 111488 MW; 724DA1D24D416767 CRC64;
MKNINYISAG AGSGKTYTLT HRLADHIIKG DVKPEEVILT TFTDKAATEF RERAKAALNE
EYRFDEAGRL DLAEIGTVHS IAYKMVSKYW YILGLSPQLK VMDENDVNFF ISQSLADLPT
DEEIRFLNDF RQEFDIQRRK DYGFGYISDY DYWKNYLTKI VEKSVIFNVK DFTQSEDFSV
KQVHDLYDDT KAISMHEQFI KIMFGLASRW KSRYHDYKRE QHTLDFNDME QYFLELLDKK
EVSSDISSSY KYLFVDEFQD SSPVQVQIFD KLSDLMEKSY FVGDFKQAIY GFRGTDAALT
EAVSNIISQG KNGCKMEKPL DTCWRSQPNI VRTVNSVFVK AFNALTPEAK ARIELKPCQP
MLDNENDDCL TYLDCGLNAS DKTGNIIHLA RDIAYIVAHG VKPTELAVLA RSNGELDELA
SNLSDYKLPV MRDGGSIAES KETTLLFAML RLLSNRGDQL AKAEIAYITE QGYSIGRIID
KKILFDDNKD EHKGNFLDDI PMVAKLLSRY DELHNMSVTT LVETLVLEFD LKNLSRKWDK
TSVAYSNFDA IIASAKTYEQ HCQQMTLPST IDGFMQYLTN QPPVQAGDIN GIRLFTYHGA
KGLEWNHVIV MSLQNDAVLE RTMIQKNFYG VSAFHEVEPS SVNLYPPMTI SLLPWIYGTK
QTIQNTDIKR KIIASKRYQI TLRNEIEENK RLLYVAVTRA KEHLYFAVFS GSRMKHPLQR
FETSGITVDT DADGKTSIDC LHTGISFRII ESEIEEFADN HQAELTYPAS HEYEKAIKIA
ADACQAEKRD VLPSSADSKP GAVELVTEKL PRIRLGKIRD NEMAETGSCI HQIFCSLDRH
KEDADQFITQ VINEWNQNVQ LPDRNGILVA WQNLTDWLNK QYGKPIKAYH ELPFKHFADG
QIITGNMDLV WRTSKGCVLV DYKTFPGKSA LALQPGEHYA GNYKGQFDCY THALEAAGET
VLARYVYYPV SGMVVKI
//