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
//