ID A0A2A9DV91_9MICO Unreviewed; 1592 AA.
AC A0A2A9DV91;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Lhr family ATP dependent helicase {ECO:0000313|EMBL:PFG30513.1};
GN ORFNames=ATJ78_1446 {ECO:0000313|EMBL:PFG30513.1};
OS Microbacterium agarici.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=630514 {ECO:0000313|EMBL:PFG30513.1, ECO:0000313|Proteomes:UP000221369};
RN [1] {ECO:0000313|EMBL:PFG30513.1, ECO:0000313|Proteomes:UP000221369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21798 {ECO:0000313|EMBL:PFG30513.1,
RC ECO:0000313|Proteomes:UP000221369};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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:PFG30513.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDJE01000001; PFG30513.1; -; Genomic_DNA.
DR Proteomes; UP000221369; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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 Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR009351; AlkZ-like.
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 InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR47962:SF5; ATP-DEPENDENT HELICASE LHR-RELATED; 1.
DR PANTHER; PTHR47962; ATP-DEPENDENT HELICASE LHR-RELATED-RELATED; 1.
DR Pfam; PF06224; AlkZ-like; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08494; DEAD_assoc; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00382; AAA; 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:PFG30513.1};
KW Hydrolase {ECO:0000313|EMBL:PFG30513.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000221369}.
FT DOMAIN 31..229
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 289..498
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 252..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1592 AA; 172016 MW; 2CC28E4A4715AF14 CRC64;
MSGVLDKFSP ATRDWFAGAF TAPTRAQEGA WNSISHGKHT LVVAPTGSGK TLSAFLWSID
RLMDAAAHSP EPASKLRRGT RVLYISPLKA LGVDVERNLR APLVGITQTA KRLGVEPPEV
TVGVRSGDTP AKDRRTLISK PPDILITTPE SLFLMLTSQA RETLRTVDTV IIDEVHAVAA
TKRGAHLAVS LERLDALLEN PAQRIGLSAT VRPREEIARF LGGTSPVEIV APPAEKTFEL
DVVVPVDDMT DLTVGQPPRA EPTEGGSAAG PVRDDGERAG SIWPHVEEAI VDRILAHKST
IVFANSRRLA ERLTARLNEI HEARLDADVL VNDPLPDNWP GQPGREPAST SEPAHIASQS
TTPTRAPAAL MGGSGQTHGL NDESAILARA HHGSVSKEQR AQVEDDLKSG RLRCVVATSS
LELGIDMGEV DLVIQVEAPP SVASALQRVG RAGHQVGEIS HGVLFPKHRA DLVNTAVTSE
RMLQGAIESM QVPANPLDIL AQQTVAATAL DVIDVEQWFE QLRRTAPFSS LPRSAYEATL
DLLAGRYPSD EFAELRPRIV WDRDAGTIEG RPGAQRLAVT SGGTIPDRGM FAVYMVGGEE
GKPGARVGEL DEEMVYESRV GDVFALGTTS WRIQEITFDR VLVTPEFGMP GRLPFWSGDA
LGRPFELGEA LGRFTRTIDK ASETDAATRL SAAGLDERSI RNLRAYLTEQ RQATGHLPTD
RTLVVERSRD ELGDWRVILH SPFGMQVHAP WALAVNARVQ ERLGIDGASI ASDDGIIVRI
PDTTDDPPGA ELFVFDADEL EVIVTNEVGG SALFASRFRE CAARALLLPN YKPGRRSPLW
QQRQRSAQLL EVASKFPQFP ILLETVRECL QDVYDVPALL DLARRIESRK IRLVDTTTDE
PSPYAKSLLF GYVGAFMYEG DSPLAERKAA ALALDSSMLS ELLGQVELRE LLDPGIIEDT
ERELQRLTES RRMRGLEGVA DLLRMLGPLD ADEVAARLQP LEDTEPRDST GEVENAEHQS
ERHATPGEAA ALLDELVTAK RALRVPVAGV ERVIAIEDAP RVRDALGVPL PIGVPSAFIE
PVPDPLGDLV ARYARTHGPI RTGDVAARLG LGTAIVTQVL GRLADEGRVV RGEFLPEGEG
AGSPIDSAEW CDKEVLRRLR LRSLAALRHE VEPVDTATFA RFLPAWQNVG GSLRGVDGVA
AVIEQLEGCH LPASAWETLI LPQRVRDYSP AMLDELTALG EVIWSGRGSL PGRDGWVGLH
LAESAPLTLA PADDLPMGQL EDDILVALSS GGAYFSAQVA QATGSADDES LQQALWNLVW
AGLITNDTFT PLRMLVSGTG AHKTRRATPR SRLYGRRGYA RPSGASGPRL GGRWSLLPLA
EQDATVRAAA TVETLLDRYG VVTRGSVMAE DYPGGFALAY RVLSSFEEKG RARRGYVIDG
LGASQFSTSA TIDRLRGHVF TDDQRPLRAI ALAATDPANP YGAALPWPPA ELTGTRHRPG
RKAGGIVVLV DGELTCYLER GGKTWLAFSG DESTLDAAAA SVGDLVRAGR IDKVAVEKVN
GEFVYGSALE HPLRRAGFTE TPRGLRIRTS HA
//
