ID   N8WJV9_9GAMM            Unreviewed;      1077 AA.
AC   N8WJV9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=F970_01961 {ECO:0000313|EMBL:ENU95497.1};
OS   Acinetobacter sp. CIP 102082.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1144663 {ECO:0000313|EMBL:ENU95497.1, ECO:0000313|Proteomes:UP000018448};
RN   [1] {ECO:0000313|EMBL:ENU95497.1, ECO:0000313|Proteomes:UP000018448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 102082 {ECO:0000313|EMBL:ENU95497.1,
RC   ECO:0000313|Proteomes:UP000018448};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. CIP 102082.";
RL   Submitted (FEB-2013) 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:ENU95497.1}.
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DR   EMBL; APPD01000052; ENU95497.1; -; Genomic_DNA.
DR   RefSeq; WP_004777597.1; NZ_KB849372.1.
DR   AlphaFoldDB; N8WJV9; -.
DR   PATRIC; fig|1144663.3.peg.1936; -.
DR   HOGENOM; CLU_008466_2_0_6; -.
DR   Proteomes; UP000018448; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   CDD; cd18011; DEXDc_RapA; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45766:SF3; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A-LIKE PROTEIN 1; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          241..402
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          661..879
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1077 AA;  121664 MW;  3B050906E8676ED8 CRC64;
     MLLDNKNKGY VGAELKKHSF EGSKLAVLSS LFTLYGFSSL KKELSKVDQT RLYLTDWQEQ
     GLQSLIGTTH EVRLLNQLDQ KQIAAECAKW IRGKVEVKAS LTKQITQNLI HLQSKQGSFA
     IHGSATFSPI GLGDIGSNIL QMNMGLTDTE SSQQLLTWFD SIWADEISSK SIKKELIEKL
     DYIAADQPAN FIYFLTLFNL FKDFLEDIDE ENIIRSKTGF KDTIVWNKLY KFQKDGVLGA
     IDKLEKHNGC IIADSVGLGK TFEALAVIKY YELRNDRVLV LCPKKLRDNW TMYTINDKRN
     LLASDRFNYD VLNHTDLSRS KGYSGEINLE TLNWNNYDLI VIDESHNFRN NPNKAEGKTR
     YERLLNDVIR SGVKTKVLML SATPVNNRMN DLKNQVAFIT EGQDTAFNEV GIKSIESTLK
     LAQKQFNQWV SEPVENRTTA TLLDSMSFDY FKLLDIVTIA RSRKHIEKYY GTADIGRFPT
     RLPPKNIYSD IDLSNEFPPL KEVNKTIRKL SLAGYSPLKF VRIDKKEEYA RRYDKAVGGG
     KGVFRQVDRE ESLIHLMRVN LLKRMESSIH SFTLTVSKLL NQVESLLSKI DAHDSDLIDA
     LNIEELQDIE LESTELEQFM IGNKTKVLLQ DMDLIRFKQE LEADKIFLSS IVEAAKGVTA
     QRDAKLELLK QTIAAKVCNP LNSDNKKVIV FTAFADTAQY LYSHIAQWAS LELGIHSALI
     TGGGTNKTTL SGLGIDLNNI LTTFSPVSKE RHKLDPNATT QLDLLIATDC ISEGQNLQDC
     DTLINYDIHW NPVRIIQRFG RVDRLGSKNT RIQLVNFWPN MELDEYINLE AKVSGRMMLL
     DISATGEENV IDENAKEMND LEYRRKQLQQ LKDAVVDLED MTGGVSITDL TLNDFRMDLS
     GYMNQKENLA KLENAPFGFY SVTPIDKVLA AEGIKPGVVF CLKNIRTGTE AIQVDSNYPL
     APYFLVYVSD NAVVELNFTQ SKKIIDLLKR QAFTHTTVAS QAVALMESRT RHGQDMEHYQ
     HLLAVAVDNI AGKSEEKGIE SLFIRGGTVL SATSSQGIED FAVVSYLILT DHLGSES
//