ID A0A1B7NXG9_9EURO Unreviewed; 634 AA.
AC A0A1B7NXG9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=ACJ72_04203 {ECO:0000313|EMBL:OAX81453.1};
OS Emergomyces africanus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1955775 {ECO:0000313|EMBL:OAX81453.1, ECO:0000313|Proteomes:UP000091918};
RN [1] {ECO:0000313|EMBL:OAX81453.1, ECO:0000313|Proteomes:UP000091918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 136260 {ECO:0000313|EMBL:OAX81453.1,
RC ECO:0000313|Proteomes:UP000091918};
RA Cuomo C.A., Schwartz I.S., Kenyon C., de Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., de Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal subunit
CC biogenesis. Required for the processing and cleavage of 35S pre-rRNA at
CC sites A0, A1, and A2, leading to mature 18S rRNA.
CC {ECO:0000256|ARBA:ARBA00024310}.
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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 ECO:0000256|RuleBase:RU365068};
CC -!- SUBUNIT: Associates in the nucleolus with the 60S and pre-60S ribosomal
CC subunits. {ECO:0000256|ARBA:ARBA00024365}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX18/HAS1
CC subfamily. {ECO:0000256|ARBA:ARBA00024357}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAX81453.1}.
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DR EMBL; LGUA01000472; OAX81453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7NXG9; -.
DR STRING; 1658172.A0A1B7NXG9; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000091918; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd17942; DEADc_DDX18; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR044773; DDX18/Has1_DEADc.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR24031:SF301; ATP-DEPENDENT RNA HELICASE DDX18; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Reference proteome {ECO:0000313|Proteomes:UP000091918};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT DOMAIN 163..191
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 194..370
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 384..546
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 163..191
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 50..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..101
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..134
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 634 AA; 70947 MW; 71B01815FF1E7CAC CRC64;
MPMAMETAKE SSKKRKRKHG HSGESTRKRD KPATVDESAS PSAAPSVESS KSKESKKRKT
DHSAAGNGKK KRGHDEPAKV YEEESDAGVE EVDEDEGISQ GSDEEGDRCA EREKELEEEE
EAEEEEEEEE EKAEETNGQS NGGHLELPSL NAVSLPQTEA EPQKFSELNL SEKTMKAIED
MKFETMTEIQ RRGIPPLLAG RDVLGAAKTG SGKTLAFLIP AVEMLSALRF KPRNGTGVIV
VSPTRELALQ IFGVARELMA HHSQTYGIVI GGASRRAEAE KLAKGVNLLI ATPGRLLDHL
QNTQGFVFKN LKALVIDEAD RILEVGFEDE MRQIVKILPT EDRQTMLFSA TQTTKVEDLA
RISLRQGPLY INVDHRKEHS TVEGLEQGYV ICDSDKRFLL LFSFLKRNLK KKIIVFFSSC
NCVKYHAELL NYIDLPVLDL HGKQKQQKRT NTFFEFCNAT QGTLICTDVA ARGLDIPAVD
WIVQFDPPDD PRDYIHRVGR TARGANGKGR SLMFLQPSEE ARVPVVEFDF PAKKIVNVQS
QLEKLIGQNY YLNKSAKEGY KSYLQAYASH SLRSVFDVHK LDLVKVAKGF GFPTPPRVDI
TLAASMSRDK KQQGRRNYGS QPKHAPKFKR KAEY
//
