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Database: UniProt
Entry: S3DCI0_GLAL2
LinkDB: S3DCI0_GLAL2
Original site: S3DCI0_GLAL2 
ID   S3DCI0_GLAL2            Unreviewed;       951 AA.
AC   S3DCI0;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=p-loop containing nucleoside triphosphate hydrolase {ECO:0000313|EMBL:EPE36127.1};
GN   ORFNames=GLAREA_05465 {ECO:0000313|EMBL:EPE36127.1};
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:EPE36127.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE36127.1, 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; KE145353; EPE36127.1; -; Genomic_DNA.
DR   RefSeq; XP_008076945.1; XM_008078754.1.
DR   AlphaFoldDB; S3DCI0; -.
DR   STRING; 1116229.S3DCI0; -.
DR   GeneID; 19464519; -.
DR   KEGG; glz:GLAREA_05465; -.
DR   eggNOG; KOG0390; Eukaryota.
DR   HOGENOM; CLU_000315_10_1_1; -.
DR   OMA; KCQTHEL; -.
DR   OrthoDB; 5480555at2759; -.
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; cd18004; DEXHc_RAD54; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR   PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 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; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EPE36127.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922}.
FT   DOMAIN          315..485
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          638..792
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          828..853
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..853
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   951 AA;  105299 MW;  60195C42D2C3C010 CRC64;
     MNKPFRPPLL KSKQKAEEID LTRIPDSDDE VEINPRPYKK RKLLVHVIES SSPPAKTLSS
     PAVHAPRKPL LVVSNPREPN STAKATSEGL EGYYMVLWRK FTTKKNKTWD GDGVLSVYGG
     YARLQDISGR DMGRSMYNEP LLPGSTLSVG GKDVEVDSAI SKADFLARKP FLKTSTKRSS
     SGESQASPMI QGKPTTPAST YKPVVSPKMP TEKIEKKPVV LKKEIPAKSF YASASKIGTT
     FKTPLLKSSV LQPKAGGGPQ PRHAPDAPGA LVMKRPKYFP KGKDIVDVVV DPFLSQHLRD
     HQREGVKFLY ECVMGMRDFN GQGALLADEM GLGKTLQTIA LIWTLLKQNP IYGPEGVIKK
     ALIVCPVTLI TNWKKEFQKW LGNERIGVLV ADDKKVRLTD FTHGKSYSVM IIGYEKLRSV
     QDELKRGAGI DLVVADEGHR LKTAQNKSAQ AIKALNTDRR IILSGTPMQN DLSEFFEMVD
     FCNPGLLGKY NTFKKEFETP ITKSRQPGAS DRDIEKGTAR GEELSALTRT FILRRTAEVL
     SKYLPPKTEY VLFCNPTRAQ IQVYQHVLES SVFGSMIGNT ECKLQLITML KKICNAPSLL
     VKADEEASGN AKMAQLLDVI PSELLRKSPV VASSKFRVLD QLIKYLSKET SEKIVLVSNY
     TATLDILGQH LASLSLPFLR LDGSTPANRR QELVDTFNKT SASKNFAFLL SAKSGGTGLN
     LIGASRLVLF DVDWNPAVDL QAMARIHRDG QKRPVKIYRM LMAGGMDEKI YQRQVSKTGL
     ADSVVDGKKN EGSFSPEELR DLFRLATNPG CQTHDLLGCD CKGLGSEQIT APGSDEEDDQ
     DKEEWSDDAE DSDDEMLFPA VVPATKANVE AIQKIDDNKG KSKKRKGKEG MQALMHYKHI
     DASVFKGETE DVFGYELEDF EKIKGILGDD ALTTILKEDT CKVNFVFAKH G
//
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