ID A0A2V5J801_9EURO Unreviewed; 1486 AA.
AC A0A2V5J801;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Chromatin remodeling complex subunit {ECO:0000313|EMBL:PYI30716.1};
GN ORFNames=BP00DRAFT_426277 {ECO:0000313|EMBL:PYI30716.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI30716.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI30716.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI30716.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KZ825512; PYI30716.1; -; Genomic_DNA.
DR Proteomes; UP000248817; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
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; IPR040934; Znf-CCCH_6.
DR InterPro; IPR041684; Znf-PHD-like.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623:SF13; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF18585; zf-CCCH_6; 1.
DR Pfam; PF15446; zf-PHD-like; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 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:0000256|ARBA:ARBA00022806};
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 479..543
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 680..851
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 987..1143
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 22..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1486 AA; 168674 MW; 13D5322F1A9C8E1A CRC64;
MSDNSDSEGG LVGELLARFK SGPAVRTSEA PQDGSALKES GVPEIEASED DFPPQQDSPE
RNLIQESPLE PQLPRPVVEV PLAPSSVIED CEYLPGHFEA LYIISEEVSE TEGGLLYRIR
LKSGEILKAS SEQLETLNNG RQALTNFFQY GPNESAASQS PDTSEEDSDL SDARKRTRRS
TQRSTRAKNT GFTAFFGNLS SDDEIGHPRR GGYSSSEDII ASSGTTTRRR RILRARKSKS
RSEILLSDEE DSRRSTPAGT RQSTRTRKVL RKNLRERNED EISENEGTPK HHEKYFGAKE
RFQKMPENDP FRERHRGACK SCHLIGDDHA KGPLVFCQGC TSSFHHSCLG PRAARDHLVT
KVTEDLFVLQ CRNCLGVTHS KDPIVPHQGH CAICNREGNM SRPLRDRLTP KQEQQSRQQN
GGKDPITFID MSRVNNVANL LFRCTTCHRA FHFEHLSDVA HLTWHCQDCA SVPGEVGAIV
AWRPVDPKAK TAKEAEREYL IKWKNQSYGH ATWMPGSWVW GFVNHIMRRA FLKKNLAPQR
TIEEAVPDDY LRIDIIFDVR YSSSSPPGES KQRSYEADLE RIDNVSQVYV KFKGLPYEEV
VWDTPPDRND VERWEDFKAA FADWVKREYV RQPNQETLRR HLAKKRKKNF QTDLVKDHQP
TIMTGGEMMD YQHDGVNWLY YMWFKQQNAI LADEMGLGKT IQVIGFMATL IQYHRCWPFL
VVVPNSTCPN WRKEIKSWVP SMRVVTYYGS AFSRNLAKEY EMYADDDPTL RCHVVVTSYE
TMVDDASRRS LAKIPWAGLI VDEGQRLKND KSQLYEALSR IRFPFKLLLT GTPLQNNIRE
LFNLLQFCDP SKKAFDLEQE YGTLSQENIT KLHEMLRPFF LRRTKAQVLT FLPPVAQIIV
PVSMSVVQKK LYKSILAKNP QLIKSIFQRN GAKALKQAER HNLNNILMQL RKCLCHPFVY
SRAIEERTAD RMKSHRHLVD AAGKLQLLEL MLPKLKDRGH RVLIFSQFLE NLDIIEDFLD
GMGLPHLRLD GRMNSLEKQK TIDDYNAQDS PYFAFLLSTR SGGVGINLAT ADTVIIMDPD
FNPHQDMQAL SRAHRIGQTN KVLVFQLMTR SSAEEKIMQI GKKKMVLDHV LIDRMVAEED
DGQDLESVLR HGAQALFDDD DSGDVRYDSE SVDKLLDRSQ AEQAKAPVEG DPESQFSFAR
VWANDNQNLE DRLQEMTEQT EQAVPNADIW DNILREREQA AAEEARRKAE TFGRGKRKRT
NVDYGKTIRE SSPVDDHIMR LADSDGEYQA EDAVDSDSDL APELDREELA IVPKRTKVRE
FERIAPINLP LAMDGSAEPD QTQQPTCIAC KQAHPVGSCR LRLAGVEHCP LCGLAHYGYS
RTCPHLKSDA QVARMLDAIK HSTEDKELVL LAKKYLTGIR GNLALRKRKE ASKAAAGAST
SIATSSPVTD LTTEHRMQPA GPALMNPVQS FPSSTQIPQH HPTNGV
//
