ID A0A221W9C2_9PSEU Unreviewed; 1812 AA.
AC A0A221W9C2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=ATP-dependent Lhr-like helicase {ECO:0000313|EMBL:MBB5923779.1};
DE EC=3.6.4.- {ECO:0000313|EMBL:MBB5923779.1};
DE SubName: Full=Putative ATP-dependent helicase Lhr {ECO:0000313|EMBL:ASO22139.1};
GN ORFNames=AHOG_22630 {ECO:0000313|EMBL:ASO22139.1}, FHR81_004852
GN {ECO:0000313|EMBL:MBB5923779.1};
OS Actinoalloteichus hoggarensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinoalloteichus.
OX NCBI_TaxID=1470176 {ECO:0000313|EMBL:ASO22139.1, ECO:0000313|Proteomes:UP000204221};
RN [1] {ECO:0000313|EMBL:ASO22139.1, ECO:0000313|Proteomes:UP000204221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45943 {ECO:0000313|EMBL:ASO22139.1,
RC ECO:0000313|Proteomes:UP000204221};
RA Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA Kalinowski J., Zotchev S.B.;
RT "Complete genome sequence of Actinoalloteichus hoggarensis DSM 45943, type
RT strain of Actinoalloteichus hoggarensis.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB5923779.1, ECO:0000313|Proteomes:UP000541573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8639 {ECO:0000313|EMBL:MBB5923779.1,
RC ECO:0000313|Proteomes:UP000541573};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP022521; ASO22139.1; -; Genomic_DNA.
DR EMBL; JACHJM010000009; MBB5923779.1; -; Genomic_DNA.
DR KEGG; ahg:AHOG_22630; -.
DR OrthoDB; 9815222at2; -.
DR Proteomes; UP000204221; Chromosome.
DR Proteomes; UP000541573; 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 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:ASO22139.1};
KW Hydrolase {ECO:0000313|EMBL:MBB5923779.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000204221}.
FT DOMAIN 45..238
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 481..637
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 258..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1812 AA; 189531 MW; F38C95F530A6A40B CRC64;
MSPGRVVVPT ADGDAQRGLE LFSPATRDWF AAAFPAPTAA QTGAWRAAAR GGHALVIAPT
GAGKTLAAFL WALDRLAVVG PPADPRARCR VLYVSPMKAL AVDVERNLRG PLAGIGRSAT
RLGLPAPDIT VGMRTGDTDS AARRGFNRTP PDVLVTTPES LFLLVTSAAR ESLRGVETVI
VDEVHAVAGG KRGAHLALSL ERLDALLPKP AQRIGLSATV RPVEEITTFL AAGTEVAVVR
PAHPKEVAVR VEVPVADMSR LDEQQAPAPP SGSRRRGDAA GAGQAEAASA VDPASIQPAG
STVSDGSGTA RPPETPEPEA VPSASIWPAV ERRVLDLVRA HRSTIVFVNS RRLAERLTAR
LNELVAEEAA AEWHGQAGAL PDTASAGRPG VPAAGVDGLR TDVEPVDLDE MQAAESDTVA
GEADKDAEAA APGPDPLHRR DSARADEADS RTAGAADDGH SAGRGGVPAS NRAAETGEAA
TADQHTGLGG TVGAAPRESG PLAGAARFPA EAVGQSGVAA GAPPVIAKAH HGSMARAQRT
EVEEELKAGL LPCVVATSSL ELGIDMGAVD LVVQVEAPPS VAAGLQRVGR AGHHVDAVST
GVVLPKFRGD LVSCAVVAER MRGGAIEEVR FPRNPLDVLA QHVVAMAAME PWPVDALATL
VRRAAPFTDL PDSALHAVLD MLAGRYPSEE FGELRARIVW DRTADVLHAR PGAQRLAVTS
GGTIPDRGLF TVTTPGGEGE PGTRVGELDE EMVYESRVGD TFLLGTTSWR VQEITHDRVI
VTPAPGVPAR MPFWKGDAPG RPLELGVALG GFVREIVAAD PASARRRAET AGLDVWACDN
LLAYLADQRA ATGRVPDDRT VLLERFRDEV GDWQWVVHSP FGDRVNAPWA LLIAARLRDR
LGVDPQIVHS DDGIVLRLPA ELAEEHGEHT VAAEDVLFDP DEVERLVAQE VGSSALFAAR
FRECAARSLL LPRWDPRRRS PLWRQRQRSA QLLAVAARYE RFPVMLETMR ECLRDVYDLP
GLITVLRDAS ARRIEVVEVQ TSTPSPFARA LLVGYVAMFL YGEDVPLAER RAAGLTLDAT
LLGELLGSEA VRDLLDVAVL AEVEAALQRT DPEQHVSDAE GVADLLRFLG DLSRAELAAR
GGLAEWAAEL VTAGRAVPVV VAGEPRWIAV EDAARYRDAL GTELPGGLPA ALLEPVSDAL
GDLLIRYARG RGPFRADEAA TRFGLGVGPV TERLDRLCAG GRLVRGELRP VEAQSVLPGG
LGTPTEYCDA EVLRRLRRGS LARLRAQVEP VEPAALGRFL PDWHGVLPAP QAPAVPIEAA
DGTRAGAGDP NSPDDDERRD GAGDRGGMGA GGDGGRGAGV RDDTGPGGDT GEVRAHRGGV
AEHAAGGRAD FGLRSGVAAA GPDEVSAVIE QLAGTPMPAS AVESMILGAR LPGYQPAALD
ELTAAGEVVW CGCGPLGAGD GWVALAPADL AELILPPPSA DDPALDTELH RALLTALASG
GLFFRGIVDR IAAWSAERAE PRQSEADLVA ALWQLVWAGL VTNDTLAPLR ALLGGGSATH
RPRRQAPRGR RAALRIGGRG RPSPAASGPP TVAGRWSLVP LRETDPTRRA HAQAEALLAR
HGVLTRGAVE GERVPGGFAG VYRVLRAMEE SGRCRRGLLL RGAGGAQFAV PGAVDGLRAW
SREAGRLDAP PAAVVLAAAD PAQPYGAALP WPVSIGAGGH RPGRKAGALV SLVDGEPVLY
VERGGKSLLS FTEDESALRS ATAALVDVVR TGRSEPLVVS RADGEQALGS RLASVLQAAG
FRATPKGLRL RG
//
