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Database: UniProt
Entry: A0A0J1CPP2_9BURK
LinkDB: A0A0J1CPP2_9BURK
Original site: A0A0J1CPP2_9BURK 
ID   A0A0J1CPP2_9BURK        Unreviewed;      1104 AA.
AC   A0A0J1CPP2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Helicase {ECO:0000313|EMBL:KLU22632.1};
GN   ORFNames=EOS_29570 {ECO:0000313|EMBL:KLU22632.1};
OS   Caballeronia mineralivorans PML1(12).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU22632.1, ECO:0000313|Proteomes:UP000035963};
RN   [1] {ECO:0000313|EMBL:KLU22632.1, ECO:0000313|Proteomes:UP000035963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX   PubMed=26205858;
RA   Uroz S., Oger P.;
RT   "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT   Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT   Ability.";
RL   Genome Announc. 3:e00798-15(2015).
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:KLU22632.1}.
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DR   EMBL; AEJF01000175; KLU22632.1; -; Genomic_DNA.
DR   RefSeq; WP_047895749.1; NZ_AEJF01000175.1.
DR   AlphaFoldDB; A0A0J1CPP2; -.
DR   PATRIC; fig|908627.4.peg.6600; -.
DR   OrthoDB; 9760715at2; -.
DR   Proteomes; UP000035963; 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   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd18012; DEXQc_arch_SWI2_SNF2; 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   InterPro; IPR007527; Znf_SWIM.
DR   PANTHER; PTHR10799:SF1020; BTAF (TBP-ASSOCIATED FACTOR) HOMOLOG; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF04434; SWIM; 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.
DR   PROSITE; PS50966; ZF_SWIM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:KLU22632.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT   DOMAIN          52..90
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50966"
FT   DOMAIN          647..807
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          935..1092
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          232..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1104 AA;  123366 MW;  D178511177464E98 CRC64;
     MPAFAYDTAQ IIKWLGSHTV AKARTYVDEV TRLHWDEDVL RANVQGTQRR PYTVEVMFHD
     HHGLLSAQGH CSCPVGFGCK HAAAVLLASA SDRPRESEAV RPEVAGWLEG FRSRFASTRN
     ASAKKPGEAN GALGLVYVLG ASRIMRTAEV ALHKVRLSPD GSFQTLDRPW TNLDAALVKQ
     PKFVSDEDMT IVRALVIGRT RNDFGGFGLH GEEGADLLHR MMATGRLFSA MPTSQDVAEP
     RRPLGEGAMR PGRIEWTPDL DDRVRPVLQT EPAATLIIPT EPLWFADAET REAGIVDMPQ
     PARQLADYLS MPPISLAEAP LVSAMLREVA SDLPPPPEQE TLNLHVVDTE PVPVLVLDTR
     PVNGSWRPRD ERTAANVLDF ALVSFDYDGF SIDPTRATTV MRAASGEMVQ VNRRHDVEAR
     YLASLYDLGF RQIPSHQRFG PKPIPNGVIG LPAPAAWASF TNDALPALRE DGWRVSMSPE
     FRFDFIEIDD IQGTARQAAD GWFDLELGIV VGERSVRLEP LLADLFQRDR RWLAGAIDSI
     PDDEGIELKT DLGERLRVRA ARIKPVVRVL IDLFDTIGSH PLRVSEQDAG RLEALSDTGR
     WQFHGDVSIR ELAQRLQEGP GLREVPVPHG LQAELRVYQR EGLNWMQYLR ERNLSGVLAD
     DMGLGKTVQT LAHILVEKES GRLDRPALVV LPTTLIHNWR EEARKFAPAL RVLDLHGPQR
     KERFDQIGEH DLVLTTYPLL WRDQAMLSLH EYHLLILDEA QIVKNVATKA AKGIRDLRAR
     HRLCLTGTPL ENHLGELWAQ FDFLLPGFLG SQKDFTKRWR TPIEKYDDPV RRDLLVRRIR
     PFMLRRRKDE VAKELPQKTT IVRTVALEGA QRDLYETVRI AMQEKVRMAV ADQGLARSHI
     VVLEALLKLR QVCCDPALVK LARAGRVEES AKLDLLLDML PELLEEGRRV LLFSQFTGML
     AIIAAALDKA GLPYVTLTGD TTDRVMPVKR FQDGEVPLFL ISLKAGGVGL NLTAADTVIH
     YDPWWNPAAE NQATDRAHRI GQLKPVFVYK LIVAGSIEER IVAMQDRKAA LADSILREDK
     AGAAKFSAED IEALLAPMPE MLAG
//
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