GenomeNet

Database: UniProt
Entry: C1H8G9_PARBA
LinkDB: C1H8G9_PARBA
Original site: C1H8G9_PARBA 
ID   C1H8G9_PARBA            Unreviewed;      1130 AA.
AC   C1H8G9;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 2.
DT   03-MAY-2023, entry version 83.
DE   SubName: Full=ISWI chromatin-remodeling complex ATPase ISW1 {ECO:0000313|EMBL:EEH36547.2};
GN   ORFNames=PAAG_06965 {ECO:0000313|EMBL:EEH36547.2};
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH36547.2, ECO:0000313|Proteomes:UP000002059};
RN   [1] {ECO:0000313|EMBL:EEH36547.2, ECO:0000313|Proteomes:UP000002059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC       {ECO:0000256|ARBA:ARBA00009687}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KN294012; EEH36547.2; -; Genomic_DNA.
DR   RefSeq; XP_015700512.1; XM_015846077.1.
DR   AlphaFoldDB; C1H8G9; -.
DR   STRING; 502779.C1H8G9; -.
DR   GeneID; 9094241; -.
DR   KEGG; pbl:PAAG_06965; -.
DR   VEuPathDB; FungiDB:PAAG_06965; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   HOGENOM; CLU_000315_0_2_1; -.
DR   OMA; VHDYQFF; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000002059; Partially assembled 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; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; ISW-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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002059}.
FT   DOMAIN          211..376
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          507..658
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          873..925
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          141..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1050..1130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1059..1084
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1090..1123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1130 AA;  129330 MW;  F4795659DB8B3134 CRC64;
     MAPSVSHLSG SESPPQADTP MEDANGYPSK TSIGNQNEDH SMTDYQDTPD YTDSDTNPNT
     TASSIAGDLA QQDGRKRRSE AFQLRKSVLG RKHGRLDESK EDDSIRRFRY LLGLTDLFRH
     FIETNPNPRI KEIMAEIDRQ NEAEASARKG STRKGGASGE RRRRTEQEED AELLKDEKRG
     GKSETVFRES PTFIKGGEMR DYQVAGLNWL VSLHENGISG ILADEMGLGK TLQTIAFLGY
     LRHICGITGP HLITVPKSTL DNWNREFAKW TPDVNVLVLQ GAKDDRHKLI NERLVDEKFD
     VCITSYEMVL REKSHLKKFA WEYIIIDEAH RIKNEESSLA QIIRVFHSRN RLLITGTPLQ
     NNLLELWALL NFLLPDVFGD SEAFNQWFSN QEADQDTVVQ QLHRVLRPFL LRRVKSDVEK
     SLLPKKEMNL YVGMSDMQVK WYQKILEKDI DAVNGAQGKR ESKTRLLNIV MQLRKCCNHP
     YLFEGAEPGP PYTTDEHLID NAGKMVILDK ILKRMKNQGS RVLIFSQMSR VLDILEDYCV
     FREHQYCRID GSTAHEDRIA AIDEYNRPGS EKFIFLLTTR AGGLGINLTS ADIVILYDSD
     WNPQADLQAM DRAHRIGQTK QVVVFRFVTE NAIEEKVLKR AAQKLRLDQL VIQQGRAQQQ
     AKSAASKDEL LSMIQHGAAS VFNTKGATGV LAKGNDISED DIDEILKKGE ERTAELNKKY
     EKLGIDDLQK FTSDNAYEWN GEDFTNRKKD IGINWINPAK RERKEQSYSM DQYYRQALAT
     GGRTADPKPK VPRAPKQIAI HDWQFFPPKL QELQEKETAY FHKEIGYKAI LPDGPEEELS
     DREAERELEQ QEIDNAVPLT EEEQDEKAAL SEEGFGHWNR RDFQQFINGS AKFGRTNYTE
     IATEVDSKDP DEIKEYAKVF WKRYTEIQDY PKHIRVIEQG EEKMRKMNHQ RKMLRKKMEM
     YRVPLQQLKV NYTVSTTNKK VYTEEEDRFL LVMLDRHGVD GEGLYEKIRE EIRESPLFRF
     DWFFLSRTPV EIGRRCTTLL NTVAKEFEVD GKAPNGDSGG KGRVRDREDD VENEDMEAPA
     KKKTKNGVVN KQLKAVQSAS GSRATSTATS RAASVSSSTP ATSKSKGKKK
//
DBGET integrated database retrieval system