ID A0A1P6C051_BRUMA Unreviewed; 1038 AA.
AC A0A1P6C051;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=BMA-ISW-1, isoform e {ECO:0000313|EMBL:CDP93715.1};
DE SubName: Full=Potential global transcription activator SNF2L, putative {ECO:0000313|WBParaSite:Bm3885b.1};
GN Name=Bma-isw-1 {ECO:0000313|EMBL:CDP93715.1,
GN ECO:0000313|WBParaSite:Bm3885b.1};
GN ORFNames=BM_Bm3885 {ECO:0000313|EMBL:CDP93715.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|EMBL:CDP93715.1};
RN [1] {ECO:0000313|EMBL:CDP93715.1, ECO:0000313|Proteomes:UP000006672}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDP93715.1,
RC ECO:0000313|Proteomes:UP000006672};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CDP93715.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDP93715.1};
RG WormBase Consortium;
RA Ghedin E., Paulini M.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:Bm3885b.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2019) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; LN856894; CDP93715.1; -; Genomic_DNA.
DR EnsemblMetazoa; Bm3885b.1; Bm3885b.1; WBGene00224146.
DR WBParaSite; Bm3885b.1; Bm3885b.1; WBGene00224146.
DR Proteomes; UP000006672; 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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.20.5.1190; iswi atpase; 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; 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; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006672}.
FT DOMAIN 154..319
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 448..599
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 813..865
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 81..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 120138 MW; D764295A2E90B390 CRC64;
MIAVKIEPET VEKETVEMKA NLDIDPMDTV ENKGDIIETS TSSNSYNVGT QFEKDSFKRF
EMLLKKTENF SHCLSAGDVE TVDVSSPNSM GAKGRPRNQS EGDHRHRKTE KEEDEELINQ
VKKSETLIRF EKTPFYIENG EMRDYQIRGL NWLISLQHNG INGILADEMG LGKTLQTVAV
IGFMKHYKNA SGPHLVIAPK STLQNWINEF GKWCPSLKAI ALIGIAEARA DLIRNEILPG
KWDVLVTSYE MVLKEKSLLR KYVWQYLVID EAHRIKNEHS KLSEIVREFK SKHRLLITGT
PLQNNLHELW ALLNFLLPDM FALASDFDSW FTNDMMGNQD LVARLHKVLK PFLLRRLKSD
VEKTLLPKKE VKIYVGLSKM QREWYTRILM KDIDVVNGAG KLEKARIMNI LMHLRKCCNH
PYLFDGAEPG PPYTTDQHLV DNSGKMVLLD KLLVKLKAQG SRVLIFSSMS RMLDLLEDYC
WWRGYRYCRL DGQTVHDERQ KSIDEFNKPD SDKFIFMLTT RAGGLGINLT AADVVIIYDS
DWNPQVDLQA MDRAHRIGQK KQVRVFRFIT DNTVDERIIE RAEMKLHLDS IVIQQGRLTD
SQKALGKEDM LDMIRHGADQ VFASKDSTIT DENIDTILEK AEQKTEALNK KIASMGETSL
RNFALDAPTF DADSNYTVYK FEGEDYREKQ KNVGGIGYWI EPPKRERKAN YQVDAYFREA
MRGGHAEPKA PKAPRPPKQP NVQDFQFYPK RLFELLEKEV YLHRKTIGYR AQRPPDLATK
EAERKQKEEQ KKIDSAVPLT EEEQNEKIQL LTQGQSNWSR REFQQFIKAN EKYGRHDLEN
IAKEIDTKSA TEVEEYAKLF WERLDELSDH ERILATIEKG EARIQRRQSI KKALDEKIAK
YKAPFHQLRI QYGTNKGKNY TEEEDRFMVC QLHKLGFDKD NVYEELRQAV RSAPQFRFDW
FIKSRTSTEL QRRCNTLISL IEKEMGEVEV KRKHGQKSSA NTPTTNTSEP KVTPAAKSGQ
KRKNEQSTSK GSSSKRQK
//
