ID E9EXQ0_METRA Unreviewed; 897 AA.
AC E9EXQ0;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=SNF2 family protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MAA_04799 {ECO:0000313|EMBL:EFY99870.1};
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:EFY99870.1, ECO:0000313|Proteomes:UP000002498};
RN [1] {ECO:0000313|EMBL:EFY99870.1, 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:EFY99870.1, 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:EFY99870.1}.
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DR EMBL; ADNJ02000001; EFY99870.1; -; Genomic_DNA.
DR RefSeq; XP_007821086.1; XM_007822895.1.
DR AlphaFoldDB; E9EXQ0; -.
DR GeneID; 19259085; -.
DR KEGG; maj:MAA_04799; -.
DR HOGENOM; CLU_007345_1_0_1; -.
DR OrthoDB; 200191at2759; -.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF17; HELICASE-LIKE TRANSCRIPTION FACTOR; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 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; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 242..419
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 732..886
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 100895 MW; CCD15F4F584C4CEB CRC64;
MAKADKTIET PISKHDLHDA QTLNEATTRS AKNNSQYRNK ARDMNKVQVK TEPGTEPGTA
GTGNKEDNSL NSEESSDSGT EGEHDSDFKC SEDESEIKPR VAKTPAKKPS RNRAAPAKTA
QAINKEASKR PKTINASSGS DLFASLTHLM FGGFSDGGPP APAMPEINAH THQKQFVLLR
DSIPKGADTR RTKTQHRDLR EAAKLFGYKK VKATSGNWLL QGMETPLYGY QLTAAAWMLK
RVCDRAQPFG GMIADEMGIG KTITSLACVV GNPPEAEDLK TYTKGTLVIV PNVSIANQWR
EEVKKHCSDD FGKTVMIHQS KNQAPAVSYQ NLMIVITTTN EVLAYYRRLQ SGKKHEDEVL
GFNWYRIILD EAHSIKNLKS LTKQSMCTLK AKHRWALTGT PLSNSATGFE VEERKKCFAK
EYMDKNKANK KLEALISSFM YRRTQRDTFL GHQIVPIPRS ETHDIWVPLT VEEEAIYIFM
KKLSSSDMTE SDDEQDKIES EKEVVQQQQR KRHMSLRRLI SHPYNIERLL RNFEEAAQIQ
ELRDSIRQVT GTQTVLQQIL SQNEAKSSLE RYKSGLTQMR TYTNTAFGGI FKFDEHLAAV
QDELKLKDME CIKCQSSDLE MPMIIPKCDH IYCGHCYDQI IQSTRLCKTP NEVPLTCVAD
GCNMPFESAK KLKTMSAEVD EALKLGNYPD TDDNKVTLAR KKDQIGFFIS SYTTPGLSMV
PNSRLTTAMT VLLSWRADYP DDKIIVFTLN VTTAKVLGSM LKHARIGFVY YFGSMGDKKK
KKALEMFKKS PTTNVFLSGL MAGGQSLNIT CANRIIIIDP WWNVTSELQA AGRTSRIGQT
KKCYVVRIFT SAATDARVAE LQKSKSEEVD HALQDDGHVP QELDYQERLE LFERTRG
//
