ID A0A178AHQ7_9PLEO Unreviewed; 1118 AA.
AC A0A178AHQ7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 35.
DE RecName: Full=Chromatin remodelling complex ATPase chain ISW1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=IQ06DRAFT_380786 {ECO:0000313|EMBL:OAK96479.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK96479.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK96479.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK96479.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; KV441720; OAK96479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AHQ7; -.
DR STRING; 765868.A0A178AHQ7; -.
DR InParanoid; A0A178AHQ7; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT DOMAIN 206..371
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 502..653
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 867..919
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1081
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 127911 MW; 283344EC4CB47D31 CRC64;
MARKGNVDSD GPSTADVSAN EDVEMQDQDT KMSGFKKFGY YQDTPDYTDS DTNPNTTASS
VAGDAPVDGR KKRAETMNMR KSIYGKKHDR LGASKEDDTI RRFRYLLGLT DLFRHFIDTN
PNPRIKDILA EIDRQDAEEA KKSKASKMRK GGAGAERRRK TEQEEDAELV REEKHGGHNE
TIFRESPGYI HGLMRDYQVA GLNWLISLHE NGISGILADE MGLGKTLQTI SFIGYLRFIA
GITGPHLVVV PKSTLDNWKR EFERWIPEID VLVLQGNKDD RAELIKDRLV DEKFDVCITS
YEMILREKSH LKKFAWEYII IDEAHRIKNE ESSLAQMVRL FNSRNRLLIT GTPLQNNLHE
LWALLNFLLP DVFGDSAAFD DWFSQQNADS DAVVKQLHKV LRPFLLRRVK ADVEKSLLPK
KEINLYVGLS DMQVSWYKKI LEKDIDAVNG GSGSKESKTR LLNIVMQLRK CCNHPYLFDG
AEPGPPYTTD EHLVNNAAKM VMLDKLLKRM KAQGSRVLIF SQMSRVLDIM EDYSVMRGYQ
YCRIDGSTAH EDRIAAIDDY NKPDSEKFLF LLTTRAGGLG INLTTADIVV LFDSDWNPQA
DLQAMDRAHR IGQTKQVYVF RFVTEGAIEE KVLERAAQKL RLDQLVIQQG RAQQPAKGAA
SKDELLTMIQ HGAEKVFNSK GSIGLATGDN AADDDFEAVM KRGEEMTQEL NKKYESLGLD
DLQKFQSDST YEWNGETFEP RKKNVGLTWI NPAKRERKEQ NYGIDMYYRK TLVTGGRTEN
KQPRIPRAPK QILIHDYQFF PERLAELQDK ETAWYRKENN LKAPLPEGPD EDLEAREADQ
ELAQKEIDNA EPLTEEEKTE KEKLIAKGFP EWNKRDFQQF LNGSAKYGRA NYDGISEEVD
GKTAAEIADY AKVFWKKYKT LDNWQKHLSV IEDGELRVRQ SEQKKELLKK KIGMYRMPLQ
QMVIKYTVST TNKKVYTEEE DRFLLVMLNK YGVEGDQIYE QIRDEIRESP LFRFDWFFLS
RTPQEISRRC TTLIQTVVRE LGGDDMKNGK GGKRVYEDED TEEEVEEPVK KKAKNGVKNK
QLDQVKGKAS PASASTSRAS SVVSNGSTTK AKGKGKKK
//