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Database: UniProt
Entry: A0A0Q5C2X2_9MICO
LinkDB: A0A0Q5C2X2_9MICO
Original site: A0A0Q5C2X2_9MICO 
ID   A0A0Q5C2X2_9MICO        Unreviewed;      1597 AA.
AC   A0A0Q5C2X2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=DEAD/DEAH box helicase {ECO:0000313|EMBL:KQQ25645.1};
GN   ORFNames=ASF54_14710 {ECO:0000313|EMBL:KQQ25645.1};
OS   Frondihabitans sp. Leaf304.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Frondihabitans.
OX   NCBI_TaxID=1736329 {ECO:0000313|EMBL:KQQ25645.1, ECO:0000313|Proteomes:UP000051456};
RN   [1] {ECO:0000313|EMBL:KQQ25645.1, ECO:0000313|Proteomes:UP000051456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ25645.1,
RC   ECO:0000313|Proteomes:UP000051456};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ25645.1, ECO:0000313|Proteomes:UP000051456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ25645.1,
RC   ECO:0000313|Proteomes:UP000051456};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQQ25645.1}.
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DR   EMBL; LMNV01000005; KQQ25645.1; -; Genomic_DNA.
DR   RefSeq; WP_055964745.1; NZ_LMNV01000005.1.
DR   STRING; 1736329.ASF54_14710; -.
DR   OrthoDB; 9815222at2; -.
DR   Proteomes; UP000051456; 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   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:KQQ25645.1};
KW   Hydrolase {ECO:0000313|EMBL:KQQ25645.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051456}.
FT   DOMAIN          31..224
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          273..499
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          328..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1325..1363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1325..1343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1597 AA;  171350 MW;  C69B6663EEB40AEF CRC64;
     MTDVLDRFSP ATATWFRGAF ARPTHAQEGA WEAISGGQNA LVIAPTGSGK TLASFLWSID
     KLASSPPPEE KQHRTRVLYI SPLKALGVDV ERNLRSPLVG VTQTARRLGT EAPEITVGVR
     SGDTTSSDRR LLQRTPPDIL ITTPESLYLM LTSAARENLK GVETVIIDEV HAVASTKRGS
     HLAVSLERLD ALLDKPAQRI GLSATVRPPE EVARFLGGSS PVTIVAPPSE KKFDLRVVVP
     VDDMTELGTA TPLEGSAAGA APQGSIWPHV EEGIVDLILE HRSTIVFANS RRLAERLTAR
     LNDIYVERTF GEAAEAGEQA ETELVEVGSH TQTSQTIEGA GSRPTPLTPA PAGSPPAQAV
     PAQAVPAQAV PAQVMGGSGQ TTGAEPLLAR AHHGSVSKDQ RALIEDDLKS GRLRCVVATS
     SLELGIDMGA VDLVVQVESP PSVASGLQRV GRAGHQVGEV SRGVLFPKHR ADLIHSAVAA
     ERMVSGLIEE LQMPANPLDV LAQQTVAAVA LDEIDADEWY DTVRRSAPFA NLPRSAYDAT
     LDLLSGKYPS DEFAELRPRI VWDRVHGTLS GRPGAQRLAV TSGGTIPDRG LFGVFMVGEK
     AARVGELDEE MVYESRVGDV FALGATSWRI EDITHDRVLV SPAYGQPGRV PFWKGDGIGR
     PAELGRAIGA YTRELSNSSL ADATARVVAG GLDERAAKNL LAFLTEQRDV AGHVPTDTTL
     VVERFRDELG DWRLILHSPY GMRVHAPWAL AVSARIRDQL GIDGSAMAAD DGIVVRIPDT
     DAEPPGADLF TFERDDLDAI VTEEVGGSAL FSSRFRECAA RALLLPRYNP GRRSPLWQQR
     QRASQLLDVA RKYPQFPIVL EAVREVLQDV YDLPALMSLT DALARREIRV VETETQMPSP
     FARSLLFGYV AAFLYEGDSP LAERRAAALS LDSSLLAELL GRAELRELLD ADVIDQHERE
     LQKLVPERRA RDIEGVVDLL RLLGPLATDE IVERSWLAEG AAAAPDALDA ARRELDTALG
     ELVRSTRILR FTHAGVERWA GIEDASRLRD ALGVNLPIGV PSAFVEPVDD PLGDLVGRFA
     RTHAPFGPVE VAQRLGLGTA VVLETLRRLG TQRRVMEGEF RPDRQGSEWC DAEVLRRLRS
     RSLAALRHEV EPVSHDTLGR FLPAWQHVAT GVKGSGLRGI DGVVQVIDQL SGVALPASSW
     ETLILPSRVT DYSTGMLDEL TATGEVIWSG AGSLAGNDGW VSLHLADGAQ VTLAEPSGDE
     TTELQREILS ALAGGGAYFF RQLSDSVGAT ASSPLLDTDL VTAIWDLVWQ GQITNDTFAP
     LRTQVSGKAP RTRTPTTRSR ASYRGRVPRS AMPRQAGPPT VGGRWSLLPL AEPDATVRAA
     AQAEMLLERH GVVTRGAVTN EGVRGGFSTV YKVLSTFEET GRARRGYFVE GLGAAQFATG
     PTVDRLRAFV RDDDREGSEA LASAGRGDAV PVVTLAATDP ANPYGAALPW PTAPDDAPEG
     APRGHRPGRK AGALVVLVDG RLVVYVERGG KTVLTFGDPT ERDLAVAAAS LAGVVRARLG
     KLAVERVDGE FVLGSRFGDA LREAGFAPTP SGVRLRS
//
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