ID E9EKJ2_METRA Unreviewed; 1025 AA.
AC E9EKJ2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Helicase {ECO:0000313|EMBL:EFZ03066.1};
GN ORFNames=MAA_00140 {ECO:0000313|EMBL:EFZ03066.1};
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:EFZ03066.1, ECO:0000313|Proteomes:UP000002498};
RN [1] {ECO:0000313|EMBL:EFZ03066.1, 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:EFZ03066.1, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:EFZ03066.1}.
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DR EMBL; ADNJ02000012; EFZ03066.1; -; Genomic_DNA.
DR RefSeq; XP_007816329.1; XM_007818138.1.
DR AlphaFoldDB; E9EKJ2; -.
DR GeneID; 19254426; -.
DR KEGG; maj:MAA_00140; -.
DR HOGENOM; CLU_000315_16_2_1; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000002498; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd14279; CUE; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF46934; UBA-like; 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:EFZ03066.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 486..660
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 852..1010
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1025 AA; 115414 MW; A0ADA644DB3AA7EC CRC64;
MIDSSPPPPT RHSSTAPRNP SISQVPTGLD DIDELAGDTI PCSPSAFLRN PSREREITQP
TQILSKPGLA LAMDRSSSPA SIIEVPASSP FQPKEPSKLG SRLAPAGTFF RPPPRPPPPR
SKESKRPAAE PISLISDDEG DSSPPRGDIR PTTFKAKIAE FVYNPAAEER ETKNKLRQIY
DVFGDKYPSE RVREALRACG NDLDDAIIWL ESAPKQTGKS IFPESSKPNK RRLVSKATLQ
NNARRPISLD RNTSPSLHSS PPQKKEKPQK RRLVQGLKKR NDSSPQKSFD GPTSSRKNAV
VIDLVDNDKE DAFEAEPSPA PSEENDDRVL NCLNTSTLKE LAAMTGMKED LLEPLMEKRP
FDSLSQARRV SATKKAGARK SPRVSIGESA VDAVEVFLNA VTAIDDVVAK CEMKGQAVKN
VMDSWDLDMF GHNKRSSRAS PDNDMPPTPS SMTSKYTSPL VPRQPRMMDG HCQMKPFQLF
GLNWMSLLCS YDIGCILADE MGLGKTCQVI SLMCHMVEEY EREPKANRPW PNLIVVPPST
YNNWLHEFER FAPDLSVVGY RGSKSERAEI AYEVERDPES YHVVLATYSQ INSDEDIEAM
QSFDLNAAVF DEGHKMKNPE TKIYRDLRRI TATWKMLLTG TPVQNNLLEM TALLNFINPQ
MFDGYMDDIR YIFSQKVTIK DVSNGAFLYA ERVRRARTIL EPFILQRRKD QVLSDMPPKI
CTVVHCDMTD SQKKTYAEYE ELFKLEPSLR ASKAKGRQND QNNAWIQLRK AALHPLLFRR
HFTDEMVTEM GKILMDRIPQ SELHQPDIKH LVQELKNSSD FELHLWCRDY PRLLKQFDIS
SAAELDSGKV TKLLELIRQY QENGDRVLVF SKFSRLIDLL QEVLALQGID HRVLMGSTDV
SERQVLIDEF NGNANIPVFL LTTGAGGTGI NLTAANKVII FDQSDNPQDD IQAENRAHRL
GQKRDVEVVR LIASQTIEEL VYKACQKKIE LANKVTGALE DTHGAEQNME QEVRKMMLEG
KMTPP
//
