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Database: UniProt
Entry: FAL1_USTMA
LinkDB: FAL1_USTMA
Original site: FAL1_USTMA 
ID   FAL1_USTMA              Reviewed;         397 AA.
AC   Q4P184; A0A0D1DNP7;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=ATP-dependent RNA helicase FAL1;
DE            EC=3.6.4.13;
GN   Name=FAL1; ORFNames=UMAG_06129;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) 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 (By similarity).
CC       {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX48/FAL1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CM003160; KIS66039.1; -; Genomic_DNA.
DR   RefSeq; XP_011392473.1; XM_011394171.1.
DR   AlphaFoldDB; Q4P184; -.
DR   SMR; Q4P184; -.
DR   STRING; 237631.Q4P184; -.
DR   EnsemblFungi; KIS66039; KIS66039; UMAG_06129.
DR   GeneID; 23565823; -.
DR   KEGG; uma:UMAG_06129; -.
DR   VEuPathDB; FungiDB:UMAG_06129; -.
DR   eggNOG; KOG0328; Eukaryota.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; Q4P184; -.
DR   OMA; KHGANRV; -.
DR   OrthoDB; 1087080at2759; -.
DR   Proteomes; UP000000561; Chromosome 21.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd18045; DEADc_EIF4AIII_DDX48; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF26; EUKARYOTIC INITIATION FACTOR 4A-III; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..397
FT                   /note="ATP-dependent RNA helicase FAL1"
FT                   /id="PRO_0000232151"
FT   DOMAIN          55..225
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          236..397
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           24..52
FT                   /note="Q motif"
FT   MOTIF           173..176
FT                   /note="DEAD box"
FT   BINDING         68..75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   397 AA;  45056 MW;  B8D0927A565C2762 CRC64;
     MSGGINAGDS KLAFESSEHV KVATTFDAMG LKEDLLRGIY AYNFEKPSAI QQRAILPIIR
     GRDVIAQAQS GTGKTATFSI SMLQSIDTTL RETQALVLSP TRELAIQIQS VVLALGDYLN
     VQCHACIGGT SVGEDIRKLD YGQHIVSGTP GRVYDMIRRR HLRTKNIKML ILDESDELLN
     MGFKDQIYDV YRYLPPSTQV VLLSATLPQD VLEMTSKFMT DPVRILVKRD ELTLEGIKQF
     FVAVEKEEWK FDTLCDLYDT LTITQAVIFC NTRRKVDWLS AKMKENNFQV SSMHGEMQQK
     ERDEVMAEFR QGSSRVLITT DVWARGIDIA NISLVINYDL PTNRENYIHR IGRSGRFGRK
     GVAINFVTVD DVRTLRDIEQ FYSTQIDEMP VKLEDML
//
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