ID A0A0D2L2K4_9EURO Unreviewed; 1562 AA.
AC A0A0D2L2K4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Chromatin remodeling complex subunit {ECO:0008006|Google:ProtNLM};
GN ORFNames=Z520_01736 {ECO:0000313|EMBL:KIY03269.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY03269.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIY03269.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY03269.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KN848063; KIY03269.1; -; Genomic_DNA.
DR RefSeq; XP_016637391.1; XM_016772252.1.
DR STRING; 1442371.A0A0D2L2K4; -.
DR GeneID; 27707482; -.
DR VEuPathDB; FungiDB:Z520_01736; -.
DR OrthoDB; 1384108at2759; -.
DR Proteomes; UP000053411; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd17919; DEXHc_Snf; 1.
DR CDD; cd15489; PHD_SF; 1.
DR CDD; cd18793; SF2_C_SNF; 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; 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; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR040934; Znf-CCCH_6.
DR InterPro; IPR041684; Znf-PHD-like.
DR InterPro; IPR001965; Znf_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; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 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:UP000053411};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 758..944
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1078..1229
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1329..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1524..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1536..1562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1562 AA; 178694 MW; 0B0C065801810C7D CRC64;
MEDIDFTTWM GKPPEKPSRV DEPVEDASSQ QLNAQVRQTE LSLSDESSEA GDILHDDGNA
HQKDYGSHVS SEEPTSDQEV ENGGDLSVGL FQKRFYIDVP NLSEEEKETY EYLPGHFSVD
KVLSEHKKNT YVVRLGSGEQ SIVSARELRD LDNGYDALQE FEASVASSRG RRASRKDPSM
IDWTTIPLSE SEEESGPKRR RKQHDSEASE GEEGGDLSEA DDESLSGEDL VEGRRSARLS
KLRKSAYFNQ GLLELEDDSD SRTTKRHGRS RASTQRPTRS STRGIAHPQR SSRLRRDSSS
EVELLTGTRR SERTKTRPKR SMRERQEDEI SSYEGEKAGP KVVGTKEHFS RIPDNDPFRR
RHRQECDTCY VKGDDNVKGP LVFCQGCTNS YHKACLGFRG TRDHLVTKVG EDLFVLQCKR
CIGLAHEKDE MAPHQGRCSG CRELGELSKP FRGRLTTRQE QLQREENGGR DPITIVESKL
INNVGNVMFR CSQCARAWHM HHLPDRKTAH SLDDEEEEGM VDDTQLAQKR FELYHRSWIC
KDCVENQHQI TTLVAWRPID IDTYAPGTGV MEIAEDDKEY LVKWKAQSYF RTTWMPGDWI
WGIATPTMRI AFFKKPENQL PKLTTADAIP EEVYRVDIVF DVRYSSVVRN STKEIDLARV
KEVDSAFVKY KGLGYEDAIW EKPPAYADTE RWNDFKAAYE DYVMKLHMSI PPQTTLKRHL
TQIRTLDFET NLIKKKQPTI VTGGELMRYQ LEGLNWLLYQ WFTNQNAILA DEMGLGKTIQ
LVAFFATLVQ DHKCWPFLVV VPNSTCPNWR REIKKWAPSL RVVTYYGSSV ARKLTHDHEL
FPKDKEEDSH GPPKKKSHEV KDIKAHIVVA SYESIVEEKT RKSLMRVPWQ ALVVDEGQRL
KSDRTQIYDI LSKFRFPFKV LLTGTPLQNN ARELFNLLQF LDKSISAADL EAKYANLTQE
NVPELHTMLR KFFLRRTKAQ VLTFLPPMAQ IIVPVSMSTV QKKVYKSILA KNPQLMKSIF
VRDSNLPQKE RHNLNNILMQ LRKSLCHPFV YSREIEERAV DGAVSYRNLV EASSKLQLLA
IMLPKLQERG HRVLMFSQFL DNLDILEDFL DGLGMQHRRL DGSISAAEKQ KRIDEFNAPN
SPYFAFLLST RAGGVGINLA TADTVIILDP DFNPHQDIQA LSRAHRIGQK EKVLVFQLMT
RDSVEEKIMQ IGRKKMALDH VLIERMDKED DAGEDLESIL RHGAEALFQD DSGAHDIIYD
SASIDRLLDR TQIEDTKIDE EKSAESQFSF ARIWANDKSA LEDDLPDRTG QSTPNPGIWD
KILQERERQF AEEQARKAQA FGRGKRKRQN VDYGLGDGDK GEPDSSKVKR GVKAADPDYR
APEQQSEDDD DAEITETDLE SKPRPKVQAR PFQRVRVPLG PAPHFNGDGA FDFRPIHPMP
AVHHCSACNE QHPMGWCRLK LAGVEHCGLC GIAHLGHSRT CPHLNNETQV MTLLQTLKES
TESRELIDQA TKYLRMVRGD LVQRKRARER KEQETQVQQY PPAQQYPPAQ WQQPLQDAGP
RT
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