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Database: UniProt
Entry: S3D1L2_GLAL2
LinkDB: S3D1L2_GLAL2
Original site: S3D1L2_GLAL2 
ID   S3D1L2_GLAL2            Unreviewed;       877 AA.
AC   S3D1L2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=p-loop containing nucleoside triphosphate hydrolase {ECO:0000313|EMBL:EPE31054.1};
GN   ORFNames=GLAREA_04021 {ECO:0000313|EMBL:EPE31054.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE31054.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE31054.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KE145363; EPE31054.1; -; Genomic_DNA.
DR   RefSeq; XP_008082465.1; XM_008084274.1.
DR   AlphaFoldDB; S3D1L2; -.
DR   STRING; 1116229.S3D1L2; -.
DR   GeneID; 19463076; -.
DR   KEGG; glz:GLAREA_04021; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   HOGENOM; CLU_000315_17_3_1; -.
DR   OMA; PNIFTDW; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000016922; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18793; SF2_C_SNF; 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; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF923; PASG; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EPE31054.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922}.
FT   DOMAIN          153..327
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          634..801
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..466
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..523
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   877 AA;  99048 MW;  C7FDDBA0ED8CE563 CRC64;
     MRSSEAGTRS PSPASRLPTS TPSSPPDLRD EDELEPEFLS KEDQLLYEEE RAARAANEKA
     EAKKRAAALK KKKKQEESKE EREKKSMKLE ELLKKSEAFS ARLTGKTQCL GRVGSSVDGK
     SLGEHNLTMA KQPKCMVGGT MRDYQLEGLT WMVEICSQGM SGILADEMGL GKTIQTISLI
     AHLREVEDYL GPHLIIAPLS TLSNWIEEFQ KWTPDVPVLL YHGTQAHRRE IFKSQIMKHV
     GKGGRPTKRF PVVCTSPEMV LRDFNDLTKI MWEFIIIDEG HRMKNNESKL FQVLKTFTSA
     SRLLITGTPL QNNMKELWSL LNFLLPTIFI HWEQFEEWFD FSDLQDEEGT AQFIADKQNK
     ELLRKMRVVL QPLLLRRIKA DVEHLLPKKR EYILYAPMTK DQTELYNAIT DKKTDTRKFL
     EDKILERLTA TAGASNGSSV KAEASDDDGS DDEKPLALRP RPKAETKTAP KNAFQQMMQK
     KSATSSRASS KGSLKRKSPA DVETPVPKSA KSSRHSTPAT SVRRTKTRGR KVYKEADASD
     EDELSDDEFE QKLVEEAAEL EKKNNVREVA GTKEELELAK MVELAKKEVS GKKLGNPIMQ
     LRLICNSVHN FYNPWATGLP VDESLVTSSG KMLLLDRLLK ALFERGHKVL VFSQFKVQLD
     LLEDYARDLR KWNVCRIDGS VAQDDRRLQI KEFNENPEFR LFLLSTRAGG QGINLASADT
     VILFDSDWNP QQDLQAQDRA HRIGQKNPVV IFRLATKNTV EEGLLSSAEG KRRLEKAVIK
     KTEFGKGPMT DDTKMQLELK QLLLKDGMVF TGTGKNKEEI LSDKDLDILC DRSDAAYERA
     AKGLGDTENF KVIETKYDGI ASMMGNEEAE ASLPVEA
//
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