ID HAS1_ASPFU Reviewed; 622 AA. AC Q4WQM4; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 2. DT 08-FEB-2011, entry version 47. DE RecName: Full=ATP-dependent RNA helicase has1; DE EC=3.6.4.13; GN Name=has1; ORFNames=AFUA_4G13330; OS Aspergillus fumigatus (Sartorya fumigata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Neosartorya. OX NCBI_TaxID=5085; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Af293 / CBS 101355 / FGSC A1100; RX PubMed=16372009; DOI=10.1038/nature04332; RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., RA Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., RA Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., RA Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., RA Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., RA Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., RA Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., RA Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., RA Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., RA Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., RA Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., RA Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., RA Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., RA Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., RA White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., RA Machida M., Hall N., Barrell B.G., Denning D.W.; RT "Genomic sequence of the pathogenic and allergenic filamentous fungus RT Aspergillus fumigatus."; RL Nature 438:1151-1156(2005). CC -!- FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal CC subunit biogenesis. Required for the processing and cleavage of CC 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SUBUNIT: Associates in the nucleolus with the 60S and pre-60S CC ribosomal subunits (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity). CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD CC box family of RNA helicases and controls ATP binding and CC hydrolysis. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX18/HAS1 CC subfamily. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAHF01000005; EAL89460.2; -; Genomic_DNA. DR RefSeq; XP_751498.2; XM_746405.2. DR ProteinModelPortal; Q4WQM4; -. DR SMR; Q4WQM4; 140-536. DR STRING; Q4WQM4; -. DR EnsemblFungi; CADAFUAT00008178; CADAFUAP00008178; CADAFUAG00008178. DR GeneID; 3509518; -. DR GenomeReviews; CM000172_GR; has1. DR KEGG; afm:AFUA_4G13330; -. DR eggNOG; fuNOG05799; -. DR GeneTree; EFGT00050000000529; -. DR HOGENOM; HBG737336; -. DR OrthoDB; EOG9QC2NM; -. DR PhylomeDB; Q4WQM4; -. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR InterPro; IPR014001; DEAD-like_N. DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. 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; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Nucleus; Ribosome biogenesis; RNA-binding; KW rRNA processing. FT CHAIN 1 622 ATP-dependent RNA helicase has1. FT /FTId=PRO_0000232205. FT DOMAIN 171 347 Helicase ATP-binding. FT DOMAIN 361 531 Helicase C-terminal. FT NP_BIND 184 191 ATP (By similarity). FT MOTIF 140 168 Q motif. FT MOTIF 294 297 DEAD box. FT MOTIF 373 389 Bipartite nuclear localization signal (By FT similarity). SQ SEQUENCE 622 AA; 69202 MW; 4C2226E7F937CE74 CRC64; MSGPVDTAKS ITKKRKRKHG GGARAATETD DAITRPAIEN GAVNDSPEKE EDTKKSEKNG KDKSAKKRKV SHASSDEGDE SQEEQGAPAQ ADGDSDDNKD DGNDQSEAEN GDNGDKKDTE STDLPSAGTL SLPTVEGEPQ KFTELGLSEK TLKAINDMGF ETMTEIQRRT IPPLLAGRDV LGAAKTGSGK TLSFLIPAVE MLSALRFKPR NGTGVIVVSP TRELALQIFG VARELCQYHS QTYGIVIGGA NRRAEAEKLM KGVNLLIATP GRLLDHLQNT QGFVFKNLKT LVIDEADRIL EVGFEDEMRQ IVKILPSEER QTMLFSATQT TKVEDLARIS LRPGPLYINV DHRKEHSTVE GLEQGYVICE ADKRFLLLFS FLKRNLKKKI IVFFSSCNCV KYHAELLNYI DLPVLELHGK QKQQKRTNTF FEFCNAKQGT LICTDVAARG LDIPAVDWII QFDPPDDPRD YIHRVGRTAR GTNAKGRSLM FLQPSEVGFL KHLKEARVPV VEFEFPANKI VNVQSQLEKL IGQNYYLNKS AKEGYRSYLQ AYASHSLRSV FDVHKLDLVK VAKGFGFSTP PRIDIQLGAS LSRDKKQQQQ GRRSYGSQPH SKGLKFKRKH DD //