ID A0A2G7FSQ2_9EURO Unreviewed; 1983 AA.
AC A0A2G7FSQ2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=SNF2 family helicase {ECO:0000313|EMBL:PIG83583.1};
GN ORFNames=AARAC_009084 {ECO:0000313|EMBL:PIG83583.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG83583.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG83583.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG83583.1,
RC ECO:0000313|Proteomes:UP000231358};
RA Moore G., Beltz S.B., Mack B.M.;
RT "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT Aspergillus arachidicola.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:PIG83583.1}.
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DR EMBL; NEXV01000444; PIG83583.1; -; Genomic_DNA.
DR STRING; 656916.A0A2G7FSQ2; -.
DR OrthoDB; 101644at2759; -.
DR Proteomes; UP000231358; 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:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd01846; fatty_acyltransferase_like; 1.
DR CDD; cd01389; HMG-box_ROX1-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 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; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45626:SF52; SNF2-RELATED DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Helicase {ECO:0000313|EMBL:PIG83583.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00267}; Reference proteome {ECO:0000313|Proteomes:UP000231358}.
FT DOMAIN 446..514
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 1709..1868
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DNA_BIND 446..514
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 409..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1666..1690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1885..1976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1668..1690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1938..1952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1953..1976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1983 AA; 221575 MW; A2F18758D9F13AB6 CRC64;
MRLFNKFHTV CALAVASILL SAWFLASQNY YRRVVPTNGE DSSFNVATSF DRRLVVFGDS
WSDNNAGELQ GSVWTEWLCS KFQCHHENMA QTAKSLRGKY IGSVVDNDEL PDSLLTLHKS
PLADFKAQVS QWTAAEARAV QEDLAGNKEA ISHRQNRTII VVSFGVWDVW NMLDKDYDTA
TQSVDRSIGV IIDQLNVLSQ SLGTNELKVI LTLTPDVTFL PAFRPTRSHI GRHKEAVQIT
EYWNRQLREA AEKWDLGTIY LFDTNAFLAD LIRDWQLYAA GIEEPNGLGK NQEPGWENVD
DACVENEQQL VMTSEVKKCD NPEKFLFWPT SNLLEHKIMN DNVSKVSMLD RHMDGVPVGS
SCRYAADGLP QVHLSSLNRA KIALNKIASN APIEPPKPAA PLPAKSIPFR ERSSVSERSS
SSSPVKSAAS RESVTQFCLC QPDPKIPRPR NAFILYRQHY QAAVVAQNPG LANPDISKII
GEQWRRLPQK TKDEWKALAE EEKARHQQQY PEYRYQPRRY GRDGNPRGSS SGISHNPPGS
TVCSRCGGRV MNPPVSPETP FNPNGSSNGN GASLQHEAIT GRSYPCRSKD SDRPSNPIKI
GSNGESLPPR QRQWEETVNG SPDSKRRRIS TQLPSKANIH RDRSPDGSYP ISPYTARPEA
PSSRGSFHML QPPRPYRSIQ EYPQPDPSLK LPPLQTTAPV SSSATPVTQY AQESSSLEAT
VMTIPFLNKI KVLAKISPPL LPFFRDGASR RRGAVVSVDG QDPVAVKSVV DFLNNTLEKE
GKYHTHIFEG PDIRLREGYS ESGQMGDATV DYLNTISAWH RISDDIVSFV KPLYGSLEPK
SVDEDKSTPG ASPKGSIPKG ADIHISSPAQ SSENGSVSYS SSSGSAPCPV PVALVPRYQL
TTADAFACSV PIGDSYAPLD HWQWMASLWR ACVGPDITVY VRECRKIIPR SSTTLRRALK
VIMAKIDRSP AAWSGCSSLD NMTNNNPQNS NEDESLWYIF NTLQNPVPNP DLMRDQYTKK
AMQQLLSVSP RKGDHGLDGF DDGAKLPRAY SHVPYLRTAL YPYQRRSAAV MIQREAQPTP
MLDPRLKPYA TPIGQEYYYD KEEGNIIREK RMYSGPRGGI LAETMGCGKT LICIAVILAT
QGHFPQVPLE YQDMELPIRP QTGSLLDMAA ATAGRLSLPW KSHFDLMRRT GTFFGRCIEA
CKEHRGAYTI PPPPTRYGSR TGVAYPRSPP RLIRLCSATL IVVPPNLVNH WKDEIAKHAE
GVHVLVIQDS SALVPPPDQL LEYDIVLFSK VRFEKEAGAA SNNRRSSTAP DPSPLTKLHW
LRIIVDEGHN VAGHGHRTNM VHILDQLHVE RRWIVSGTPS SGLYGVEVSL ASHETNDTSD
SDLTEATTAV LHGKEKTTII DSELKDLDEI RRIVVGFLDL KPWSNSQAND PANWTKYMKP
VGEDGKRRKA QSLRATLQSL VVRHRMEVIY SEVPLPRLYN RVVRLKPTFY DKLNLNLFIF
ILAVNAITSE RKDQDYMFHP RNRKHLSLVI NNLRQAGFWW AGSDGDIQGT IDVASNYMEA
NRERMARDEI DILTEGIQIA QKAIACQSWN AFKQFHELGV FIQDFPSHAR SMWALSPSRP
DVEPLLLGIS QAHKAQSFVT AHLNEMYPEE GLAGAGIKAR LALSGRQGHP DSVTTKKTTP
DKLSSCTVKT LPPSSPLAQT KLVATTSAKL TYLLDRVLEL HTEEKIIIFY DNNNSAFWIA
EGLELLGVDF RIYASTLKPK VRAAYLELFR EQEDVRVLLM DLHQASHGLH IANASRVFIV
NPIWQPNVES QAIKRAHRIG QTRPVFVETL VLKDTLEDKM LERRKAMSEK EMQQAERDLL
DDSTMSSIIQ NEHFLHMADD EDLTGPAYLK QPPGFFDRHG LPIPEVNESP SSAKRTPRSR
KRRPVPVDMN MDATGDSDVG TPKRRRSDGT ELRSGGFSET LPSLMDSSDG TDERTNNYVS
IFN
//
