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Database: UniProt
Entry: A0A1Y2G7Z2_9FUNG
LinkDB: A0A1Y2G7Z2_9FUNG
Original site: A0A1Y2G7Z2_9FUNG 
ID   A0A1Y2G7Z2_9FUNG        Unreviewed;      1099 AA.
AC   A0A1Y2G7Z2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=SNF2 family N-terminal domain-domain-containing protein {ECO:0000313|EMBL:ORZ01965.1};
GN   ORFNames=BCR41DRAFT_426201 {ECO:0000313|EMBL:ORZ01965.1};
OS   Lobosporangium transversale.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX   NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ01965.1, ECO:0000313|Proteomes:UP000193648};
RN   [1] {ECO:0000313|EMBL:ORZ01965.1, ECO:0000313|Proteomes:UP000193648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ01965.1,
RC   ECO:0000313|Proteomes:UP000193648};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007025}.
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:ORZ01965.1}.
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DR   EMBL; MCFF01000062; ORZ01965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2G7Z2; -.
DR   STRING; 64571.A0A1Y2G7Z2; -.
DR   InParanoid; A0A1Y2G7Z2; -.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000193648; Unassembled WGS sequence.
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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014905; HIRAN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45626:SF22; HELICASE-LIKE TRANSCRIPTION FACTOR; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08797; HIRAN; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00910; HIRAN; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193648};
KW   Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          418..639
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          821..865
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          930..1085
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          285..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1099 AA;  122722 MW;  33968D015E55632B CRC64;
     MADVPQHLSA LSDILGPDVD LATLEKLHVI SNGDLNRAIN HFYEGSYHTV TNPGVPAISS
     TISTSKAPKI VSANGGLGSI YRDDQPRISI VGAKRKAQDS FFPKYFGELT VIAYALGGMV
     KIEAGEEVLF DRKRPNSQVQ HGRKKKGLGS VSIGWGRTAK ENHVVRFTKQ NGFEIGRLQV
     DTSRWVSKLM DYKLAEFRGT IILAPPQLRT GAEIVLTMRC YLTAEAFSSL GSNQKLTLKS
     KSGQPVFVNE AQETEDEVDL KQKKYAVNAL FRELALTPVA TNTSVGPRDR GIDIHDGSTT
     EGSLAASNGE DNENEQEPEV SDKELDVLYE KAQQHGRAFE PMDPPKTMTY TLKPYQRVAL
     AWMYNKEVLE TASDNHKALH PLWEEYEFKK EDGYEPKLDE PKKYYFNPYS GEMSLEFPTS
     DKLCRGGILA DEMGLGKTIE ILSLVHSNPM NKSSIDTPEE AFSRLSTSTS ASNSTSTDKQ
     SSPTTLVVCP MSLLSQWRDE AINSSDGSLS VEVYYGAARG WTDSSLQQKG APDILITSYG
     TVLSEFSSLL NNSGADTSKS LTNMLDIKAQ NNWKKGSALF NVEFHRVVLD EAHHIKSRMT
     QTAKACYALN SPRRWVVTGT PIQNKLEDLF SLVHFLRAEP WSNFSFWRTF ITIPFESKDK
     DKALKVVTSV LEPLVLRRTK MTKDENGNPI ITLPERIVEI EYLKFSEQEN DIYQALFKDG
     KTKFNHYCRA GTVLKHYASI FQLLMRMRQV CDHPMLVLNN RTKQTEGKDS SELALDMKDG
     PIQLEELMKK FSSGEGDNSE QTFGASVLQN LVSSTGEVTE CPICYEELAD GVLMPCMHSA
     CRSCILDYLQ RLDNKGEMGE CPICRKGPIT EDSLIEYTTL SVSDSIPSDA KEEEEKRSGF
     VAGNVLDAGA ETNGGRVVQI RRNNFKSSAK LEALMKHLNE LRKTEPKTKS VVFSQFTGML
     DLVEKILERD GFQFLRLDGS HSHVAREQTL QAFRTVDHPA RVMLISLRAG GVGLNLTTAS
     RVFMLDPWWN YAIEAQAIDR VHRIGQLKPV IVKRFIIENS VEEKILSIQN RKNALASGLG
     MTKLEAQGAR MEDLQEIFS
//
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