ID A0A2G7FL45_9EURO Unreviewed; 1552 AA.
AC A0A2G7FL45;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Chromodomain helicase (Chd1) {ECO:0000313|EMBL:PIG81324.1};
DE Flags: Fragment;
GN ORFNames=AARAC_007292 {ECO:0000313|EMBL:PIG81324.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG81324.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG81324.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG81324.1,
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:PIG81324.1}.
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DR EMBL; NEXV01000567; PIG81324.1; -; Genomic_DNA.
DR STRING; 656916.A0A2G7FL45; -.
DR OrthoDB; 5482994at2759; -.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.140.1440; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
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 PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
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:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:PIG81324.1};
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:UP000231358};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1552
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013849267"
FT DOMAIN 300..372
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 400..460
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 498..669
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 800..958
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 61..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PIG81324.1"
SQ SEQUENCE 1552 AA; 176371 MW; D2C7433247453946 CRC64;
SKYRKLSRVL LFYATLYLSS LARPVLSFNA NVSSHIATSM VIPSTSEPST VMAFANGHSA
SPASDTVSFG NEPLASDGDS NMFDSVDNHV VSDSSPDPDA ADESFNADSP DAEGYEDDSA
MEDNAKDSSQ SSSENSSSSE SGRGTKRKSS SVNESDYIRQ NPDLYGLRRS GRARTTRQVA
QSLSDSDSDA VAPRSKRRRP VASQQTSKRP SRSATQSSFS EDSETSESEY GGSRARTSKA
KRRRQQASAS APSHAEVRFS TRNAARVSTY NEDDDDSMFE DDPDEVMQNY WVNAVEDDRP
AVDIVLNHRL KAGVDSSNTD LDRHDFEFYI KWQGKSHYHA TWETAESLAN CRSTRRLDNY
IRKVLYEDIR LRQDEDVAPE DREKWNLDRE RDVDAIEDYK QVERVIATRE GDEGTEYLVK
WKRLFYDSCT WENEELVSEI AQCEIDRFLN RSSRPPVSDK SESNPASRKS FEAIKGTPSF
LRNGELKEFQ VKGVNFMAFN WVKNRNVVLA DEMGLGKTVQ TVSFINWLRH VRRQQGPFVV
VVPLSTMPSW AETFDNWTPD LNYVVYNGNE AARTVLREHE LMIDGNPRRP KFNVLLTTYE
YVLLDSSFLS QFKWQFMAID EAHRLKNRES QLYAKLLEFR SPARLLITGT PIQNNLAELS
ALLDFLNPGM VDIDADMDLN AEAASHKLAE LTKAIQPFML RRTKSKVESD LPPKVEKIIR
VELSDVQLEY YKNILTKNYA ALNDGAKGQK QSLLNIMMEL KKASNHPFMF PNAEAKILDG
STRREDVLRA MITSSGKMML LDQLLAKLKR DGHRVLIFSQ MVKMLDLLGE YMEFRGYTYQ
RLDGTIPAAS RRLAIEHYNA PGSSDFAFIL STRAGGLGIN LMTADTVVLF DSDWNPQADL
QAMARAHRIG QTRPVSVYRL VSKDTVEEEV IERARNKLLL EFITIQRGVT DKEASEIQNK
MARNGISITE PNSTEDISRI LKRRGQRMFE QTGNQEKLEQ LDIDSVLANA ELHQTEQAED
IQADGGEEFL KAFDYVDIKV DDLTWDDIIP KEQLEEIKAE EKKKADERYL AEVIEQNRPR
KRNVPGDERD SREERKAKRQ ARAQVSLDDG DESDSNTQLD PKRPLIEKEY RHLLRAFLRY
GDIDDREEDV IREARLLDRD RETVKGALRE ITEKASSLVR EDIEKMEALE HAGKMPTKKE
KKAVLFDLHG VKRLNAYTIV ERPAEMRILK EATNAVSDFK NFRVPEATKA ADYSCPWGAR
EDGMLCIGII RHGYGAWAQI RDDPDLALGD KFFLEEHRVE RKNERLNAED KSTKSPGAVH
LVRRADYLLS VLKDKVTNGS SVNAKRAVEN HHRNNRKGSR PHASASVSAS PAPSISRKGH
REMDRSRHRS HTHGARDSVE RHHTPNYDSR PRSFHESERA RHRTSDASSE DVRRRKNSEN
GYSAGKEDVA RLFFKPIRED LRKVSAVTKE NYPNKAERAS ELRNLLRKIG EFIDGTLKGQ
NSVHSLETRL WHFVADNHWP NKEAGGAKLQ EMYRKLMAAQ KVAAAAPASN GS
//
