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Database: UniProt
Entry: I7ZD97_9GAMM
LinkDB: I7ZD97_9GAMM
Original site: I7ZD97_9GAMM 
ID   I7ZD97_9GAMM            Unreviewed;      1467 AA.
AC   I7ZD97;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Putative ATP-dependent DNA helicase {ECO:0000313|EMBL:EIT69864.1};
GN   ORFNames=WQQ_00010 {ECO:0000313|EMBL:EIT69864.1}, WQQ_01880
GN   {ECO:0000313|EMBL:EIT70051.1};
OS   Hydrocarboniphaga effusa AP103.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC   Hydrocarboniphaga.
OX   NCBI_TaxID=1172194 {ECO:0000313|EMBL:EIT69864.1, ECO:0000313|Proteomes:UP000003704};
RN   [1] {ECO:0000313|EMBL:EIT69864.1, ECO:0000313|Proteomes:UP000003704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP103 {ECO:0000313|EMBL:EIT69864.1,
RC   ECO:0000313|Proteomes:UP000003704};
RX   PubMed=22933753; DOI=10.1128/JB.01017-12;
RA   Chang H.K., Zylstra G.J., Chae J.C.;
RT   "Genome Sequence of n-Alkane-Degrading Hydrocarboniphaga effusa Strain
RT   AP103T (ATCC BAA-332T).";
RL   J. Bacteriol. 194:5120-5120(2012).
RN   [2] {ECO:0000313|EMBL:EIT69864.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AP103 {ECO:0000313|EMBL:EIT69864.1};
RA   Park J.-H., Zylstra G.J., Chae J.-C.;
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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:EIT69864.1}.
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DR   EMBL; AKGD01000001; EIT69864.1; -; Genomic_DNA.
DR   EMBL; AKGD01000001; EIT70051.1; -; Genomic_DNA.
DR   RefSeq; WP_007183147.1; NZ_AKGD01000001.1.
DR   STRING; 1172194.WQQ_00010; -.
DR   PATRIC; fig|1172194.4.peg.1; -.
DR   OrthoDB; 9815222at2; -.
DR   Proteomes; UP000003704; 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   CDD; cd17922; DEXHc_LHR-like; 1.
DR   CDD; cd18796; SF2_C_LHR; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR013701; DEAD/DEAH_assoc.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47962:SF5; ATP-DEPENDENT HELICASE LHR-RELATED; 1.
DR   PANTHER; PTHR47962; ATP-DEPENDENT HELICASE LHR-RELATED-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08494; DEAD_assoc; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:EIT69864.1};
KW   Hydrolase {ECO:0000313|EMBL:EIT69864.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003704}.
FT   DOMAIN          41..235
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          272..424
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1467 AA;  162564 MW;  1309E456754778FA CRC64;
     MQYRLDLAAL RQGRDGPFHP AVTRWLHSRF GQPTEVQQRA WAVTSQNRHA LIAAPTGSGK
     TLAAFLAAIN DLVEEGLEQP LQDRVYVLYV SPLKALSNDI QKNLQEPLSG IRAQLAAMGL
     PDVGIRDAVR TGDTPMFERE RMRKTPPHIL VTTPESLFIL LTSQGGREML RCVRSLIIDE
     LHAVAGGKRG AHLMLTLERL AALCDRPFVR IGLSATVKPL EAMARYLIGG RDEPVTIVDT
     GHVRQRDIAM ELPKSPLTPV MSGEVWGETY DRLAELVAAH KTTLIFVNQR RIAERTARHL
     AERIGAEFVT SHHGSLSREH RLRAEQQLKN GELKALVATS SLELGIDIGD VDLVCQLGSP
     RAINAFLQRV GRAGHAIGAI PKGRLFPLTQ DDLLECTALL SAVSAGELDR IRLPQRPLDV
     LAQQIVAEIG CGEWGVDELY ALARRADPYR TLLKEDFEQV VQMLADGYVT RRGRRGAYLH
     LDAVNRRLRA RPGAKLAAVM NAGTIPDQFD YDVVLQPEGH RVGSLNEDFA FESMAGDIFQ
     LGNTSYRILK VETTRVLVED AQGLPPSIPF WFGEAPGRTD ELSAAVSKLS TQAEARLAQG
     IEACARWLAQ ELGVAEAAAQ QLAEYWASSY AMLGALPSEN CVIFERFFDE VGDTHLVIHS
     PFGSRVNRAW GLALRKRFCR TFNFELQASA LEDSIVLSLG PTHSFPLDTI QHYLKSATAR
     DVLIQALLDA PMFGTRWRWN ATVALGIRRM NGGKRVPPQF QRSDSEDLLT LVFPDQVACA
     ENLVGERQIP NHPLVQQTID DCLRETMDVE GFERVLARME SGEIRVICCD LASPSPLSQA
     ILNAKPSAFL DDGAAEERRT RTLAMQPLMD LPTAERMARL DIETIERVHG DVWPLIRNAD
     ELHDALVVHG FLLEGEMLQG RVGGVGRLDE TNWAGRAWLD TLVAQKRVTR LHPAGGEPLW
     LAAERWHEAR VVWPQATPSH PIRAVTMAEP DAGSALQELV RSRLELIGVI SLQQLARPLG
     LDVSAIEASL YALEAEGAIV RGYFTGAGIE EWCDRRLMAR IHRQTRDKRR SEIAPVPPAG
     FMRFLFAWHR LAGSAAEIRY QGDNGLLASL QQLEGYAGAT ASWEDDLLPT RVEAYNPMML
     DRLCASGRII WQRPASELDP GKKRSGPVRS TPILFCEREF LPMWQLAEEA PPGERKLSSR
     AERLLEALQQ CGASFFADLL ADSGLLGAEL EEALGELVSQ GLVSCDTFAG LRALTMSGDK
     RDRLRRHFGR GDVAFDDAGR WALTRHRRKP ASQLNVNALA DPRVEHVARV LLRRYGVVFR
     ALLERETGLP PWRELHYVYR RLEARGEVLG GRFVSGFAGE QFALSEAAGA LRRYGQQAQS
     GRGAIERVCI GASDPLNLVG VIVPGERVPR VAGNRILFED GVPVAVQSGG DTQYLKSADL
     HDQWEIRNLL LRQQKSISYL AQPRLPQ
//
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