ID S3DTZ2_GLAL2 Unreviewed; 1207 AA.
AC S3DTZ2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=GLAREA_01018 {ECO:0000313|EMBL:EPE29858.1};
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:EPE29858.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE29858.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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DR EMBL; KE145367; EPE29858.1; -; Genomic_DNA.
DR RefSeq; XP_008083967.1; XM_008085776.1.
DR AlphaFoldDB; S3DTZ2; -.
DR STRING; 1116229.S3DTZ2; -.
DR GeneID; 19460076; -.
DR KEGG; glz:GLAREA_01018; -.
DR eggNOG; KOG0926; Eukaryota.
DR HOGENOM; CLU_001832_0_4_1; -.
DR OMA; FCYLDDK; -.
DR OrthoDB; 5490433at2759; -.
DR Proteomes; UP000016922; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd17982; DEXHc_DHX37; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EPE29858.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922}.
FT DOMAIN 396..573
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 595..833
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 98..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..266
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..297
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1207 AA; 134133 MW; 45FBBEA11641FA43 CRC64;
MPKFVPRQRK HKVIARAKGN GRQPEFEVVD SNVVEHIPAA KSELEEKKLR LKEELKKEGQ
KISGKKAKRL EKYIDTKLRK DENRELIAKL AHATTDTSLF QSSRKLGQGR ETKRERLGRA
LRDKQAGIDI DGDNDELLFE KRIVREVEDE PSSDENEPEQ ASAGGLFQTS LTAQLPAKQS
YAVGGGLKRP LEVGDDGRPV LKKRKRRGGV QSKVQLMPDP APEPEWEGFE SASEASSNTD
ESSQSSAEED DSSVEEEDEM LSEQDESKVD EDVSNSSESS GDEEEEDDSE DSSEESDDGE
GTPQRQERSS AFKSWANQQL NEALGYESVS NVPNATETPK IAGFEPRALE EDPLPVELQP
TTNLGRKAFS VSVERSPDIQ TVRLQLPVVA EEQKIMEAVH NSNLVVVYGA TGSGKTTQVP
QFLFEAGYGS LGSPTPGMIG VTQPRRVAAV SMAKRVGDEM GNQGKKVAYQ IRFEGTVSQD
TAIKFMTDGV LLREVAQDIA LRKYSAIIID EAHERSVNTD ILIGMLSRVV KLRQEMAQED
QSTKPLKLII MSATLRITDF TENTTLFSEP PPVLQAEGRQ YPVTTHFSRR TNHDYVEEAF
QKISKGHKKL PPGGILVFLT GQNEITQLSK KLKEAFRMGH TSTGPQVRIS GKDAPIETED
IDFGDFGDDR NDDFDEDDEA DIDVGEDEEF KLEGEEEETG PAKMHILPLY SLLPTKEQLR
VFEPPPEGSR LVVLATNVAE TSLTIPGIRY VFDCGRSKER KYDKNTGVQS FEISWISKAS
ASQRAGRAGR TGPGHCYRLY SSAVYERDFE EFAEPEILRM PIEGVVLQLK SMNLQHVINF
PFPTPPDRQS LASSEKLLTY LSAISPTGQI TSTGATMSIF PLSPRFARIL LVGHLHDCLP
YTIALVAGLS AADIFIPSNQ AIPQIAALEP DTYLTALDHA ESERAAAIRR HFNAVQKSFC
FLDSKSDAIK LLQVVGEFAH EPTETWCISH FVRFKPLTEI QKLRKQITDL LRTNIPAFST
LAYQDKLPPP TPKQVKALKQ MVAAGFIDHI AIRADLAPVP PEMRKATRAI DVPYLPLLPT
HADSPSVYIH PSSPLSHLST RECPEYIVYS YLQRSLENPL QPERTPKTRM HALTDISGAQ
IAALAKGTPL ISWGKPIKEV KVWEEGRKRE VWCVPTFRAE GMGGVGWALP ARKVVQRREG
GRGWVVE
//
