ID A0A075AWZ8_ROZAC Unreviewed; 1055 AA.
AC A0A075AWZ8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Helicase, superfamily 1/2, ATP-binding domain-containing protein {ECO:0000313|EMBL:EPZ34649.1};
GN ORFNames=O9G_002967 {ECO:0000313|EMBL:EPZ34649.1}, ROZALSC1DRAFT_27044
GN {ECO:0000313|EMBL:RKP21558.1};
OS Rozella allomycis (strain CSF55).
OC Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC Cryptomycota incertae sedis; Rozella.
OX NCBI_TaxID=988480 {ECO:0000313|EMBL:EPZ34649.1, ECO:0000313|Proteomes:UP000030755};
RN [1] {ECO:0000313|EMBL:EPZ34649.1, ECO:0000313|Proteomes:UP000030755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSF55 {ECO:0000313|EMBL:EPZ34649.1,
RC ECO:0000313|Proteomes:UP000030755}, and CSF55
RC {ECO:0000313|EMBL:EPZ34649.1};
RX PubMed=23932404; DOI=10.1016/j.cub.2013.06.057;
RA James T.Y., Pelin A., Bonen L., Ahrendt S., Sain D., Corradi N.,
RA Stajich J.E.;
RT "Shared signatures of parasitism and phylogenomics unite Cryptomycota and
RT microsporidia.";
RL Curr. Biol. 23:1548-1553(2013).
RN [2] {ECO:0000313|Proteomes:UP000281549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSF55 {ECO:0000313|Proteomes:UP000281549};
RX PubMed=30297742; DOI=10.1038/s41564-018-0261-0;
RA Ahrendt S.R., Quandt C.A., Ciobanu D., Clum A., Salamov A.,
RA Andreopoulos B., Cheng J.F., Woyke T., Pelin A., Henrissat B.,
RA Reynolds N.K., Benny G.L., Smith M.E., James T.Y., Grigoriev I.V.;
RT "Leveraging single-cell genomics to expand the fungal tree of life.";
RL Nat. Microbiol. 3:1417-1428(2018).
RN [3] {ECO:0000313|EMBL:RKP21558.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CSF55 {ECO:0000313|EMBL:RKP21558.1};
RG DOE Joint Genome Institute;
RA Ahrendt S.R., Quandt C.A., Ciobanu D., Clum A., Salamov A.,
RA Andreopoulos B., Cheng J.-F., Woyke T., Pelin A., Henrissat B.,
RA Reynolds N., Benny G.L., Smith M.E., James T.Y., Grigoriev I.V.;
RT "Leveraging single-cell genomics to expand the Fungal Tree of Life.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; KE560931; EPZ34649.1; -; Genomic_DNA.
DR EMBL; ML004945; RKP21558.1; -; Genomic_DNA.
DR STRING; 988480.A0A075AWZ8; -.
DR EnsemblFungi; EPZ34649; EPZ34649; O9G_002967.
DR HOGENOM; CLU_000315_0_2_1; -.
DR OMA; TAFYRKE; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000030755; Unassembled WGS sequence.
DR Proteomes; UP000281549; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; 1.10.1040.30; 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, ECO:0000313|EMBL:EPZ34649.1};
KW Helicase {ECO:0000313|EMBL:EPZ34649.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030755}.
FT DOMAIN 208..373
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 505..656
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 862..914
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1055 AA; 123188 MW; 33EDBF77CD3AA98E CRC64;
METSEPRPNI DSNSAEAISK VEIKREEDVP NAVEKIAQGG ETDAFAEVKE EPVDVKIKME
ENAEDGMQVE SEERGEMSVD TEMASNEEER GSELDRDVKS ENMEVEEVEE KKVGKKKTHA
QNKAEDAMKR YRFLLGQTDI FKHFIDPEKL GIDMNELNVN KKRKTEKEED KELMDQDEDG
VITNLRESPR YVKGTMRDYQ LQGLNWMISL YENGINGILA DEMGLGKTLQ SISMLGYLKH
MRGIRGSHLV IVPKSTLQNW KNEFNKWVPD FDAFIFHGNQ QERAELIGER IKTMDFEICI
TSFEICILEK SALKKITWEY IVIDEAHRIK NENSLLSQIV RLFECRNRLL LTGTPLQNNL
HELWALLNFL LPDVFKSAED FDLWFEKHGN DQEKMVIQLR KILEPFLMRR LKADVEHSLL
PKKEVNLYVG MTEMQKKYYQ KCLEKDIDAV NGGITGKRQN KNRLLNIVMQ LRKCCNHPYL
FDGAEPGPPY STGEHLVYNS GKMIVLDKLL KKMRDNGSRV LIFSQMSRVL DILEDYCNYR
GYECCRIDGQ TPHEERIEAI EEYNKPNSSK FVFLLTTRAG GLGINLATAD VVVLYDSDWN
PQADLQAQDR AHRIGQTKQV YVFRFITENS IEEKIIERAI QKLRLDQLVI QNGKRDNLNQ
KLGQEDLLTM IRHGAQDAFI EGSTVIDEDI EIVLNKGEEK TRELMKKYET AGLEDLQKFN
VDNSFNTYEW DGKDFSKKKN KSLFILETSK RERKSNYAID SYYRDTLGIQ ITRGPSSKAP
RAPKQPAIYD YQFYPLRLIE LFTKENLYYR KSVDYKVVQR KPEKNETLEQ VELQAIQEQE
KIDNAEPLNE EEEIEKDKLI HLGYGNWTRK DFQQFIKGCE KFGRNNFVEI EKEVETKSLD
EIKDYSKVFW SRITELSDHE KIVSSIEKGE LKLKKIQEIQ SLIDNKITSV KKPLQDLSLS
NCKSKSFSEI EDRFLLLKIH QIGYSTDDLY EKIRFEIKNS HLFKFNWFFR SRNANELMKR
CQTLIASLQK ESEIEERKKR KSIQQSTKPK KSKNE
//
