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Database: UniProt
Entry: A0A3D9LF62_9MICC
LinkDB: A0A3D9LF62_9MICC
Original site: A0A3D9LF62_9MICC 
ID   A0A3D9LF62_9MICC        Unreviewed;      1693 AA.
AC   A0A3D9LF62;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Lhr family ATP dependent helicase {ECO:0000313|EMBL:REE05079.1};
GN   ORFNames=C8E99_2938 {ECO:0000313|EMBL:REE05079.1};
OS   Citricoccus muralis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Citricoccus.
OX   NCBI_TaxID=169134 {ECO:0000313|EMBL:REE05079.1, ECO:0000313|Proteomes:UP000256727};
RN   [1] {ECO:0000313|EMBL:REE05079.1, ECO:0000313|Proteomes:UP000256727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14442 {ECO:0000313|EMBL:REE05079.1,
RC   ECO:0000313|Proteomes:UP000256727};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (JUL-2018) 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:REE05079.1}.
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DR   EMBL; QREH01000001; REE05079.1; -; Genomic_DNA.
DR   Proteomes; UP000256727; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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   CDD; cd18796; SF2_C_LHR; 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:REE05079.1};
KW   Hydrolase {ECO:0000313|EMBL:REE05079.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256727}.
FT   DOMAIN          55..258
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          305..501
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1147..1166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1384..1444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1540..1560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1389..1408
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1693 AA;  180772 MW;  D399058A8EF951F9 CRC64;
     MTSGSRRSMA AMAQDSRPDA AEPAADEVLA RFTPATREWF EGAFAAPTTA QLGAWDAISS
     GQHALVVAPT GSGKTLSAFL WALDGFLRVP SATSIQDSEK TEKQAKKQTR VLYISPLKAL
     GVDVERNLRA PLIGITQTAK RLGEAAPDVR VGVRSGDTPA RERRQLASHP PDILITTPES
     LYLMLTSQAR STLAGVQTVI VDEVHAVAGT KRGAHLAISL ERLDTLLAKP AQRIGLSATV
     EPKEEVARFL GGVQPVRIVA PASTKSWDVH VTVPVPDMTE LPSASSAHDL GPGSGLQTNA
     SIWPHVEERI VDLVEANRST IVFANSRRLA ERLTGRLNEI WEERQVAEPP PEVPQELPDA
     GRSGSPAQLM GGAGQSAGHA SQGTGTEFAR AHHGSVSKEQ RALIEDALKS GQLRCVVATS
     SLELGIDMGA VDLVIQVESP PSVASGLQRV GRAGHQVGET SSGWFFPKHR GDLVDTTVVV
     ERMLSGRIES MSIPANPLDI LAQQTVAACA LDELDVEAWF DLLRRSAPFA TLPYSAFESV
     LDLLSGRYPS DEFAELRPRV VWDREAGTLA GRNGSQWLAV TSGGTIPDRG LFGVFLAGTE
     NETTSDAGTA GGAKASAGTA RTGGRRVGEL DEEMVYESRV GDVIVLGATS WQIQDITHDR
     VLVIPAFGQP GRLPFWRGDA EGRPVELGEA VGAFRREVSA GLGGGEAGVG NPMSERLAAA
     GLDAWAQDNL TAYLAEQREA TGQLPTEKTL VVERFHDELG DWRVVLHSPF GMPVHAPWAL
     AVGARLHARY GMDGSAMAAD DGIVLRVPMM EDEPPGADLF LFTAEELEEL VTAEVGGSAL
     FAARFRENAA RALLLPRRDP GKRTPLWQQR QRSAQLLEVA RKYPQFPIIL ETVRECLQDV
     YDLPALKDLA TRIEAKSLRL VETTTQTPSP FAQSLLFGYV AQFIYEGDSP LAERRAAALS
     LDPGLLNELL GRAELRDLLD PDVMATVEAD LQRLSPDRRV KGTEGLADLL RLLGPLTAEG
     AASRLRPAVE TDEETHEHAE ATGLLDQLVT ANRALRVRIN GQTRYAAVED AARLRDALGV
     ALPMGIPVAF IEPVEDPLAD LVSRYARTHG PFTAAEAGVA LGLGAAVVLQ VLQRLAAEQR
     VTEGQFRPTA GHGVDGDGSR PSGPHETEWC EVEVLRRIRR RSLAVLRAEV EPVEQSAYAR
     FLADWQHLSP APGGGSPATL SGIDGVATVL DQLSGVPVPA SGWESHVLPS RVRDYTPALL
     DELLASGEFL WSGTAAASGD DGWVAFHSAE SADLSLTRRE DLEPGPVHRA LLEVLDAGGA
     WFFGQLAERA RTVLAAAETT ETRRDEPAPR VSSGDLLRAL WDLVWAGLVG NDTFAPIRGL
     LGQGRTAHKS KSRSPRARPA RPGRGARLSR WKRLQEASGS LGADGGRTDS LARPAGGLPA
     DLGPMDVPRA AGRWSLLPEP SADPTLLAHA TAEYLLDRYG VITRGSVVAE EVPGGFATQY
     RLLTRMEEAG QVRRGYYVEH LGAAQFSTGA TVDRLRGFAQ QDVPGPRPQH AGAPSPWQDA
     RAAPAPQAVA LAATDPANPY GAALPWPELP AGPDGVRPTG QRPGRKAGAV VVLVAGELAL
     YVERGGRTLL LFSDEPSALA PMATALAWAL RTARVEKMSL EKVNGLPLTG TPLATALAEA
     GFYSSPSGLR FRS
//
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