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
//