ID A0A4T0IT36_WALIC Unreviewed; 1368 AA.
AC A0A4T0IT36;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ISWI chromatin-remodeling complex ATPase ISW2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=E3P86_03514 {ECO:0000313|EMBL:TIB30411.1};
OS Wallemia ichthyophaga.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=245174 {ECO:0000313|EMBL:TIB30411.1, ECO:0000313|Proteomes:UP000310689};
RN [1] {ECO:0000313|EMBL:TIB30411.1, ECO:0000313|Proteomes:UP000310689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-6200 {ECO:0000313|EMBL:TIB30411.1,
RC ECO:0000313|Proteomes:UP000310689};
RA Gostincar C.;
RT "Sequencing 23 genomes of Wallemia ichthyophaga.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NAD(+) = a uridine in mRNA +
CC H(+) + NADH; Xref=Rhea:RHEA:69851, Rhea:RHEA-COMP:14658, Rhea:RHEA-
CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00033653};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853;
CC Evidence={ECO:0000256|ARBA:ARBA00033653};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NADP(+) = a uridine in mRNA +
CC H(+) + NADPH; Xref=Rhea:RHEA:69855, Rhea:RHEA-COMP:14658, Rhea:RHEA-
CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00033638};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857;
CC Evidence={ECO:0000256|ARBA:ARBA00033638};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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:TIB30411.1}.
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DR EMBL; SPOI01000263; TIB30411.1; -; Genomic_DNA.
DR Proteomes; UP000310689; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd02801; DUS_like_FMN; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR PANTHER; PTHR10799:SF879; CHROMATIN-REMODELING COMPLEX ATPASE CHAIN ISWI; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF01207; Dus; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-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.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS01136; UPF0034; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000310689};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 602..767
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 901..1058
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1255..1308
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..461
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1368 AA; 155173 MW; 3066CDFE3D452B1A CRC64;
MTQALPHSRS PSPKTAKLQE PPAKKTKVEG IPFEEVDYAN GLHLAPMVRS GALPTRLISL
EYGAKLVWTP EVIDRAIIDS QRVYNTSTGV IDYIKPTENK PIWSTHPLER PHVIYQIGSS
SPQLAVQAAQ TVAGDVAGID LNCGCPKHFS VHAGMGAALL TNTDNLVAIL NALCEALPHK
SISCKIRLLG TQQDTIELVK RICSTPIKAI TIHCRTKSMR PSEPAQHDRL AEVREAIEKM
RPDVAVVCNG DGNTHKDAQQ IMSRTGVNAV MIARGAEGNP SCFNRGGPVK LGAYWLQLAH
ALDHLFPASK FCTGQLTPFA KYGDIKKKDR SNLNQALSQA KTHEQMAEAY KITLTQDKGL
DQPMFDNYKK GFMVSPCKRH HETLLLGLIY SQDKANSREE SMLSDTIPPS AAISNINSKV
PSPKGGSANS ADSAQISADE DKDELEDQDD DDEEELDEEY DSDGQVIKSI APAPAHAPAK
DNKRPARKSK HKVKKDEIEK SKNIDSVKRF SYLIGQTDLF KHFIDRRKER DPAFRAMIEQ
SEVQTGKKKA KKNQSRRKTE KEEDEELLQD EEDEPFAFTE TPAFIQNCTM RDYQVQGLNW
MIGLHHNGIN GILADEMGLG KTLQTISFLA FLKHFKDISG YHLVCVPKST LDNWAREFSK
WCPDFKVVVL QGTKEEREKL VKEHILPGDF DVLISSYEIC LREKSAIKRL SWEYIIIDEA
HRIKNANSLL SQIVRIFNSR NRLLITGTPL QNNLMELWAL LNFLLPDVFS SSEDFDAWFT
NNQEGGNSDE VVKQLHKVLR PFLLRRVKAD VEKSLLPKKE INLYVGLTDM QRKWYKGIIE
KDIDLVNGMG SSKKEGKTRL LNIVMQLRKC CNHPYLFDGA EPGPPYTTDE HLVFNSGKML
ILDKLLKSMK AKGSRVLIFS QMSRVLDILE DYCMFRDYQY CRIDGQTSHD DRISAIDEYN
KEGSEKYIFL LTTRAGGLGI TLNTADIVVL YDSDWNPQAD LQAMDRAHRI GQKKQVFVFR
FVTEDAVEER ILERAAQKLR LDQLVIQQGR QTQQKNAGKD ELTDMIQHGA EKIINNQKRE
IVDNDIDEII KTGESKTANM ASKYEDLNLE DLNNFKSEIN FTGVNPKAKQ PLWIEPGKRE
RKQNYSIDDY YKGAMKPNPQ GRTRSNKPPP ATHKFQDYHF FPTRLLELAR RDDNYKKKED
GWEAIPRHVD PKKAEENPEL VEQAKVDAKK EQDDIDSATP LSEEEIKDME AMSHQGFTTW
TRREFQAVVR GMEQHGRNDL KGIKGVVGDG KTEEEVKEYL DVWWKRYPEL QDHQRMIQRI
EEGEKTLESV ATKTRAIKAK VNGCRYPLQM LNIPYGPQQR VSGGCSGD
//
