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Database: UniProt
Entry: E9EQX9_METRA
LinkDB: E9EQX9_METRA
Original site: E9EQX9_METRA 
ID   E9EQX9_METRA            Unreviewed;       992 AA.
AC   E9EQX9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=MAA_02217 {ECO:0000313|EMBL:EFZ02635.1};
OS   Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS   anisopliae (strain ARSEF 23)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655844 {ECO:0000313|EMBL:EFZ02635.1, ECO:0000313|Proteomes:UP000002498};
RN   [1] {ECO:0000313|EMBL:EFZ02635.1, ECO:0000313|Proteomes:UP000002498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
RN   [2] {ECO:0000313|EMBL:EFZ02635.1, ECO:0000313|Proteomes:UP000002498}
RP   GENOME REANNOTATION.
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034617};
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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:EFZ02635.1}.
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DR   EMBL; ADNJ02000001; EFZ02635.1; -; Genomic_DNA.
DR   RefSeq; XP_007818406.1; XM_007820215.1.
DR   AlphaFoldDB; E9EQX9; -.
DR   GeneID; 19256503; -.
DR   KEGG; maj:MAA_02217; -.
DR   HOGENOM; CLU_004585_4_2_1; -.
DR   OrthoDB; 208346at2759; -.
DR   Proteomes; UP000002498; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd18807; SF1_C_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50132; RGS; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
FT   DOMAIN          11..284
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          285..596
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   DOMAIN          489..565
FT                   /note="RGS"
FT                   /evidence="ECO:0000259|PROSITE:PS50132"
FT   REGION          147..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..769
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          799..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          893..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          950..992
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        710..736
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        803..822
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..922
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   992 AA;  110508 MW;  9097136283C82E45 CRC64;
     MESPHPETIL NSLNEAQRRA VTSNSPTVAI LAGPGSGKTH TLTSRVVWLV QHVGYQPADV
     IVATFTVKAA REMKGRIGKR LGEECEKKIV LGTFHSIARR YLAVYGKRIG LDPKFGIADD
     GDSRAIIQRI IKRLDLQIEP AHAKSWISKK KSKGTTPVPK QSGRRPNETP SLNECYTAYQ
     DHLARSNLLD YDDLLVRCVE LLQEHPSCVS NVQAVLIDEY QDTNGIQYDL MKLFAQARQR
     ITIVGDPDQS IYGWRSAEIK NLYRLLRDYP ETDEISLEEN YRSSQLILDM SLQVIQQDSK
     RYQKVLLPVH TKGTKPVLRR LKSSSREGEW IVSELRRAIT MFGGAIKNED VAILLRSAYL
     SRHIESALGK AGISYRMIGG HKFYERKEIK ILLDYLRVVY QPNMNDALAR IINVPRRGIG
     ETTIKSLLEE AEMSKLSLWA LLWRHCRGGR RATTKLRPNM EQKLNTELLR IVSSLRQSME
     DIIAGGSMSL VDLIEQLISQ LSFKKYLEAE YQEDHEQRWA NVQELLSLAN DFVRDYDNEG
     EEEALPEIEN LDQVKDNDIL GKFLANVALA SDAQSGDKEQ DKASQVTIST IHASKGLEWP
     VVFIPSVYGG SIPHSRAEDM DEERRLLYVA MTRAKALLYL SCPLYGSQGL GNKVELSPFV
     SAFAESFAQK GPSFDRPVVE GVGKILGRVI PSEKSIFDKI PIMFCPEDDQ HPIDPFDHEN
     PDYLDPHDDN SYGRPPKKQK TQHYVNNGGT AQEKPWKPDY STTMEQSSGF TMSSLPGFAS
     ASTHRTALAA SGAEAEMSRN AAGKAYSNRS VKGTTNRRPD QRSLLGFVTT ESRQLATAAG
     MKPAPRDFSL ARYQAAASRA AHRTSQPAVN INAEATIDPT FAKHKVTGAK PISRPNVAQS
     TTKEPSAKHY ACFSSSPTRP LSPEPQHDEG KAAATVSQRP ATVFHSTTFT SMKPAGGIRR
     PVGLGPPPSM DRLRKPFKPL TINRPRGPPG NS
//
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