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Database: UniProt
Entry: A0A0N1P1Y1_9EURO
LinkDB: A0A0N1P1Y1_9EURO
Original site: A0A0N1P1Y1_9EURO 
ID   A0A0N1P1Y1_9EURO        Unreviewed;      1573 AA.
AC   A0A0N1P1Y1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Chromatin remodeling factor mit1 {ECO:0000313|EMBL:KPI44544.1};
GN   ORFNames=AB675_8332 {ECO:0000313|EMBL:KPI44544.1};
OS   Phialophora attinorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI44544.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI44544.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI44544.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-2015) 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:KPI44544.1}.
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DR   EMBL; LFJN01000003; KPI44544.1; -; Genomic_DNA.
DR   RefSeq; XP_018004507.1; XM_018148770.1.
DR   STRING; 1664694.A0A0N1P1Y1; -.
DR   GeneID; 28740650; -.
DR   OrthoDB; 1384108at2759; -.
DR   Proteomes; UP000038010; 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; cd15489; PHD_SF; 1.
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; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
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:SF17; 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; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          753..935
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1069..1218
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1333..1396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..231
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..286
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1333..1372
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1573 AA;  178640 MW;  52480912BBB22A77 CRC64;
     MDGEDTPDLS LWTAKPPPKP ATAPVEGDSS PQAGSVVARS KRGSSAATSE ASSNAGDVNY
     DAQRPPFTED QVPEMQREST ARKMMLSRSM TEEEKAGYSF APGHMRVREV LAETNRGIFR
     TRLGSGDIEE LTLKQLNQRN HAQSALRFFR LKSLRMEGRG RRSAGAQKPT ASGFVNWDDV
     AKGSDDESDG AVVGFRKRKQ QLAEDSDVEM NGNTDQDSDN EDDGDSESDS DQDEGPAGRR
     SSRLKGNRKS YTLETDLDLI TRSPPRLRGR TSTRPTRGRG GRRTNSRRAR SLSSSPEPAQ
     GTRRSGRTRT KPVGSMRERQ EDEISEHSGN DAGMKVVGTK EVFRRVDEHD DFRKRHREEC
     DTCDRRGDDP TKGPLVFCQG CTTAYHKTCL GYRGTREHMV TKIGEENFVL QCRRCIGIAR
     DKDPLAPHLG QCETCNEMGV NSTPFRIRLT VKQEQAQREE NGGKDPITIV EDHHINKPEN
     VLFRCFSCQR GWHVHHLPNR QTVTSTAEDD EEDKELSDEE RAEKRWQLYH RGWRCKDCIE
     NKYAIDALVA WRPVNIDTYI PGYHADMVQD SQKEYLVKWK NKSYLRCNWM PGSWVWGTAA
     GNMRMSFMKK PENYIPRMTT KDAIPEEFFR IDIVFAVRYT SVVRNTSKEV DFARVREVES
     AFVKYKGLGY EDAIWESPPS FRDTERWNDF NSAYNDYVLK LHTSIPIRTT LNRTLTALRQ
     LDFEKSLMRK EQPSSITGGS MMQYQLEGLN WLYFQWFQNQ NAILADEMGL GKTIQLVAFF
     ALLVQEHKCW PFLVVVPNST VPNWRREIKT WVPSLRVVTY YGSAQARKIT HDYELFPEEF
     TKKKSRSGDP QDIKAHVVIA SYESIIEDKT RNSLKNVPWQ GLVVDEGQRL KNDKNQVYDI
     LTKTFRFPFK VLLTGTPLQN NVRELFNLLQ FLDRTINAAE MEARYATLTQ DNVPELHEKL
     RKFFLRRTKA QVLTFLPPMA QIIIPVSMSG LQKKLYKSIL AKNPQLMKSI FTRDPTAATK
     ERVSLNNILM QLRKTLCHPF VYSREIEERN VDSGEAQVRL IDASPKLQLL SLMLPKLKDR
     GHRVLIFSQF LDNLDIIEDF LDGLGLMHRR LDGNTASLEK QKRIDEYNAP DSPYFAFLLS
     TRAGGVGINL ATADTVIILD PDFNPHQDIQ ALSRAHRIGQ KNKVLVFQLM TKDSAEEKIM
     QIGKKKMALD HVLIENMNQD DEAGMDLESI LRHGAEALFD EDSKADDIVY DAPSIDKLLD
     RSQVEDTKIN DEQSAESQFS FARVWANKTG AFEEAPLSED TNGTNTPNPG IWDKILKERE
     RAYEEEMALK AQTFGRGKRR RQIVDYGQDG VDGGSPDKRK KGDVASDGDF TGKDTEQDED
     DATEDDSEVD FKRPTVKARP FKRVKVPTGQ PPYNLDGTTD YMPRDGIMPP SHHCTACDER
     HPMGWCRLKV AGVEHCGLCG IAHLGHSRTC PHLTDEKQLV RLLETLKESP ESREDVEAAT
     KYLRMIRGDL VSRARRKREE EQVARSLATV STNLGTISTG LAGGHQQGVA ANGYQHGGTP
     EGRWGARFVE GGR
//
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