ID Q0CR55_ASPTN Unreviewed; 911 AA.
AC Q0CR55;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=ATEG_03829 {ECO:0000313|EMBL:EAU35631.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU35631.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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DR EMBL; CH476598; EAU35631.1; -; Genomic_DNA.
DR RefSeq; XP_001213007.1; XM_001213007.1.
DR AlphaFoldDB; Q0CR55; -.
DR STRING; 341663.Q0CR55; -.
DR EnsemblFungi; EAU35631; EAU35631; ATEG_03829.
DR GeneID; 4318643; -.
DR VEuPathDB; FungiDB:ATEG_03829; -.
DR eggNOG; KOG0924; Eukaryota.
DR HOGENOM; CLU_001832_6_1_1; -.
DR OMA; VDVMFHR; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000007963; 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:0004386; F:helicase activity; 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; 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:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 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 Helicase {ECO:0000313|EMBL:EAU35631.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963}.
FT DOMAIN 197..360
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 382..557
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 102293 MW; BC58AE7575ADAC50 CRC64;
MASNEMPPAK RLKSNLPAPL RDAKRKDIDN WETNRMLTSG VAQRRDFDGD FMPEDEEATR
VHLLVHDLRP PFLDGRTIFT KQLEPISAVR DPQSDMAVFS RKGSKVVRER RQQRERQKQA
QEATTMAGTA LGNLMGVKED EGDSAVALPV EDTYKSGNKF AQHMKKSEGG QSSFSKSKTL
REQREFLPAF AVREDLLRVI RDNQVVVVVG ETGSGKTTQL TQFLHEDGYS KFGMIGCTQP
RRVAAMSVAK RVSEEMEVDL GDLVGYAIRF EDCTSDKTTI KYMTDGVLLR ESLVQPDLDK
YSCIIMDEAH ERALNTDVLM GLLKKVLARR RDLKLIVTSA TMNAERFSRF FGGAPEFIIP
GRTFPVDVHF SRTPCEDYVD SAVKQVLAIH VSQGPGDILV FMTGQEDIEA TCELVDERLK
LLNDPPKLSI LPIYSQMPAE QQAKIFERAA PGVRKVIVAT NIAETSLTVD GIMYVVDAGY
SKLKVYNPRM GMDTLQITPI SQANANQRSG RAGRTGPGKA YRLYTEMAYK NELYLQTIPE
IQRTSLSNTV LLLKSLGVKD LLDFDFMDPP PQETITTSLF ELWSLGALDN LGDLTSLGRR
MTPFPMDPPL AKLIITASEE YGCSEEMLTI VSMLSVPSVF YRPKERQEES DAAREKFFVP
ESDHLTLLHV YTQWKSNGYS DGWCTKHFLH AKALRRAREV RDQLHDIMVA QKMPLVSCGT
DWDVIRKCIC SGFYHQAARV KGIGEFINLR TSVTMQLHPT SALYGLGYVP EYVVYHELIL
TSKEYMSTVT AVDPHWLAEL GGVFYSVKEK GYSQRERRVT EHEFNRRMEI ESQIAADRER
AAAEKQREQE RNDPTRRRRE VEVGSVVRRP AAPGKRVGGV TASSTGGRNG TGGGGSVVKK
PPIKRKPGRA F
//
