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Database: UniProt
Entry: Q9H6R0
LinkDB: Q9H6R0
Original site: Q9H6R0 
ID   DHX33_HUMAN             Reviewed;         707 AA.
AC   Q9H6R0; B4DHF9; Q4G149; Q5CZ73; Q9H5M9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   16-OCT-2019, entry version 155.
DE   RecName: Full=ATP-dependent RNA helicase DHX33 {ECO:0000305};
DE            EC=3.6.4.13;
DE   AltName: Full=DEAH box protein 33;
GN   Name=DHX33 {ECO:0000312|HGNC:HGNC:16718}; Synonyms=DDX33;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Hepatoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 119-128; 130-138 AND 200-211, SUBCELLULAR
RP   LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RA   Bienvenut W.V.;
RL   Submitted (AUG-2005) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 293-707.
RC   TISSUE=Melanoma;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   FUNCTION, ASSOCIATION WITH RIBOSOMAL DNA LOCI, INTERACTION WITH UBTF,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=21930779; DOI=10.1128/mcb.05832-11;
RA   Zhang Y., Forys J.T., Miceli A.P., Gwinn A.S., Weber J.D.;
RT   "Identification of DHX33 as a mediator of rRNA synthesis and cell
RT   growth.";
RL   Mol. Cell. Biol. 31:4676-4691(2011).
RN   [8]
RP   FUNCTION, DOUBLE-STRANDED RNA-BINDING, MUTAGENESIS OF LYS-103,
RP   INTERACTION WITH NLRP3, AND SUBCELLULAR LOCATION.
RX   PubMed=23871209; DOI=10.1016/j.immuni.2013.07.001;
RA   Mitoma H., Hanabuchi S., Kim T., Bao M., Zhang Z., Sugimoto N.,
RA   Liu Y.J.;
RT   "The DHX33 RNA helicase senses cytosolic RNA and activates the NLRP3
RT   inflammasome.";
RL   Immunity 39:123-135(2013).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DDX3X; EIF3G; EIF3H;
RP   RPL3; RPL7; RPL26 AND RPL27, AND RNA-BINDING.
RX   PubMed=26100019; DOI=10.1128/mcb.00315-15;
RA   Zhang Y., You J., Wang X., Weber J.;
RT   "The DHX33 RNA Helicase Promotes mRNA Translation Initiation.";
RL   Mol. Cell. Biol. 35:2918-2931(2015).
CC   -!- FUNCTION: Implicated in nucleolar organization, ribosome
CC       biogenesis, protein synthesis and cytoplasmic dsRNA sensing (By
CC       similarity) (PubMed:21930779, PubMed:23871209, PubMed:26100019).
CC       Stimulates RNA polymerase I transcription of the 47S precursor
CC       rRNA. Associates with ribosomal DNA (rDNA) loci where it is
CC       involved in POLR1A recruitment (PubMed:21930779). In the
CC       cytoplasm, promotes elongation-competent 80S ribosome assembly at
CC       the late stage of mRNA translation initiation (PubMed:26100019).
CC       Senses cytosolic dsRNA mediating NLRP3 inflammasome formation in
CC       macrophages and type I interferon production in myeloid dendritic
CC       cells (PubMed:23871209). Required for NLRP3 activation induced by
CC       viral dsRNA and bacterial RNA (PubMed:23871209). In dendritic
CC       cells, required for induction of type I interferon production
CC       induced by cytoplasmic dsRNA via the activation of MAPK and NF-
CC       kappa-B signaling pathways (By similarity).
CC       {ECO:0000250|UniProtKB:Q80VY9, ECO:0000269|PubMed:21930779,
CC       ECO:0000269|PubMed:23871209, ECO:0000269|PubMed:26100019}.
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   -!- SUBUNIT: Interacts with UBTF (PubMed:21930779). Interacts with
CC       DDX3X, EIF3G and EIF3H; the interaction is independent of RNA
CC       (PubMed:26100019). Interacts (via HA2 region and Helicase C-
CC       terminal domain) with the components of the large ribosomal
CC       subunit RPL3, RPL7, RPL26 and RPL27 (PubMed:26100019). Interacts
CC       (via DEAH box) with NLRP3 (via NACHT domain) (PubMed:23871209).
CC       Binds to mRNA (PubMed:26100019). Binds to double-stranded RNA (via
CC       the helicase C-terminal domain) (PubMed:23871209). Interacts (via
CC       the helicase C-terminal domain) with MAVS (By similarity).
CC       {ECO:0000250|UniProtKB:Q80VY9, ECO:0000269|PubMed:21930779,
CC       ECO:0000269|PubMed:23871209, ECO:0000269|PubMed:26100019}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000269|PubMed:21930779, ECO:0000269|PubMed:26100019}.
CC       Nucleus, nucleoplasm {ECO:0000269|PubMed:21930779}. Cytoplasm
CC       {ECO:0000269|PubMed:23871209, ECO:0000269|PubMed:26100019}.
CC       Nucleus {ECO:0000269|PubMed:23871209}. Inflammasome
CC       {ECO:0000269|PubMed:23871209}. Note=Predominantly in the
CC       nucleolus. During mitosis, localizes with the nucleolar organizing
CC       regions (PubMed:21930779). Upon dsRNA-binding, localizes in the
CC       inflammasome (PubMed:23871209). {ECO:0000269|PubMed:21930779,
CC       ECO:0000269|PubMed:23871209}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H6R0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H6R0-2; Sequence=VSP_016256;
CC   -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC       Deubiquitinated by USP36. {ECO:0000250|UniProtKB:Q80VY9}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH30017.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
DR   EMBL; AK025625; BAB15193.1; -; mRNA.
DR   EMBL; AK026944; BAB15596.1; -; mRNA.
DR   EMBL; AK295074; BAG58120.1; -; mRNA.
DR   EMBL; AC004148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471108; EAW90332.1; -; Genomic_DNA.
DR   EMBL; BC030017; AAH30017.1; ALT_INIT; mRNA.
DR   EMBL; CR936655; CAI56793.1; -; mRNA.
DR   CCDS; CCDS11072.1; -. [Q9H6R0-1]
DR   RefSeq; NP_001186628.1; NM_001199699.1. [Q9H6R0-2]
DR   RefSeq; NP_064547.2; NM_020162.3. [Q9H6R0-1]
DR   RefSeq; XP_016880366.1; XM_017024877.1.
DR   SMR; Q9H6R0; -.
DR   BioGrid; 121247; 26.
DR   IntAct; Q9H6R0; 13.
DR   MINT; Q9H6R0; -.
DR   STRING; 9606.ENSP00000225296; -.
DR   iPTMnet; Q9H6R0; -.
DR   PhosphoSitePlus; Q9H6R0; -.
DR   BioMuta; DHX33; -.
DR   DMDM; 296434478; -.
DR   EPD; Q9H6R0; -.
DR   jPOST; Q9H6R0; -.
DR   MassIVE; Q9H6R0; -.
DR   MaxQB; Q9H6R0; -.
DR   PaxDb; Q9H6R0; -.
DR   PeptideAtlas; Q9H6R0; -.
DR   PRIDE; Q9H6R0; -.
DR   ProteomicsDB; 81012; -. [Q9H6R0-1]
DR   ProteomicsDB; 81013; -. [Q9H6R0-2]
DR   Ensembl; ENST00000225296; ENSP00000225296; ENSG00000005100. [Q9H6R0-1]
DR   GeneID; 56919; -.
DR   KEGG; hsa:56919; -.
DR   UCSC; uc002gca.3; human. [Q9H6R0-1]
DR   CTD; 56919; -.
DR   DisGeNET; 56919; -.
DR   GeneCards; DHX33; -.
DR   HGNC; HGNC:16718; DHX33.
DR   HPA; HPA073875; -.
DR   MIM; 614405; gene.
DR   neXtProt; NX_Q9H6R0; -.
DR   OpenTargets; ENSG00000005100; -.
DR   PharmGKB; PA27220; -.
DR   eggNOG; KOG0922; Eukaryota.
DR   eggNOG; COG1643; LUCA.
DR   GeneTree; ENSGT00940000156747; -.
DR   HOGENOM; HOG000175261; -.
DR   InParanoid; Q9H6R0; -.
DR   KO; K17820; -.
DR   OMA; RCYMRDL; -.
DR   OrthoDB; 354219at2759; -.
DR   PhylomeDB; Q9H6R0; -.
DR   TreeFam; TF354245; -.
DR   ChiTaRS; DHX33; human.
DR   GenomeRNAi; 56919; -.
DR   Pharos; Q9H6R0; -.
DR   PRO; PR:Q9H6R0; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000005100; Expressed in 202 organ(s), highest expression level in secondary oocyte.
DR   ExpressionAtlas; Q9H6R0; baseline and differential.
DR   Genevisible; Q9H6R0; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0072559; C:NLRP3 inflammasome complex; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0033613; F:activating transcription factor binding; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR   GO; GO:0000182; F:rDNA binding; IDA:UniProtKB.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IDA:UniProtKB.
DR   GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IDA:UniProtKB.
DR   GO; GO:0032481; P:positive regulation of type I interferon production; ISS:UniProtKB.
DR   GO; GO:0006413; P:translational initiation; IEA:Ensembl.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR011709; DUF1605.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 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; SSF52540; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Helicase; Hydrolase; Inflammasome;
KW   Nucleotide-binding; Nucleus; Polymorphism; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN         1    707       ATP-dependent RNA helicase DHX33.
FT                                /FTId=PRO_0000055164.
FT   DOMAIN       84    252       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      277    450       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      97    104       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION        1     80       Required for nucleolar location.
FT                                {ECO:0000269|PubMed:26100019}.
FT   REGION      471    562       HA2; required for interaction with EIF3G
FT                                and RPL26. {ECO:0000269|PubMed:26100019}.
FT   MOTIF       194    197       DEAH box.
FT   MOTIF       547    558       Critical for rDNA-binding. {ECO:0000250}.
FT   VAR_SEQ       1    173       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_016256.
FT   VARIANT     118    118       R -> C (in dbSNP:rs8069315).
FT                                /FTId=VAR_057239.
FT   VARIANT     483    483       H -> D (in dbSNP:rs11653658).
FT                                /FTId=VAR_057240.
FT   MUTAGEN     103    103       K->N: No effect on inflammasome
FT                                activation upon dsRNA-binding.
FT                                {ECO:0000269|PubMed:23871209}.
FT   CONFLICT     77     77       F -> L (in Ref. 1; BAB15193).
FT                                {ECO:0000305}.
FT   CONFLICT    166    166       R -> G (in Ref. 1; BAB15193).
FT                                {ECO:0000305}.
FT   CONFLICT    377    377       A -> V (in Ref. 4; AAH30017).
FT                                {ECO:0000305}.
FT   CONFLICT    539    539       P -> S (in Ref. 6; CAI56793).
FT                                {ECO:0000305}.
SQ   SEQUENCE   707 AA;  78874 MW;  E3515B12BD972431 CRC64;
     MPEEAGFPPA KRFRPGSGPP SRAGSFPPGR QVVMLLTAGS GGRGGGGGRR QQPPLAQPSA
     SPYPEAVELQ RRSLPIFQAR GQLLAQLRNL DNAVLIGETG SGKTTQIPQY LYEGGISRQG
     IIAVTQPRRV AAISLATRVS DEKRTELGKL VGYTVRFDDV TSEDTRIKFL TDGMLLREAI
     SDSLLRKYSC VILDEAHERT IHTDVLFGVV KAAQKRRKEL GKLPLKVIVM SATMDVDLFS
     QYFNGAPVLY LEGRQHPIQV FYTKQPQNDY LHAALVSVFQ IHQEAPSSQD ILVFLTGQEE
     IEAMSKTCRD IAKHLPDGCP AMLVLPLYAS LPYAQQLRVF QGAPKGYRKV IISTNIAETS
     ITITGIKYVV DTGMVKAKKY NPDSGLEVLA VQRVSKTQAW QRTGRAGRED SGICYRLYTE
     DEFEKFDKMT VPEIQRCNLA SVMLQLLAMK VPNVLTFDFM SKPSPDHIQA AIAQLDLLGA
     LEHKDDQLTL TPMGRKMAAF PLEPKFAKTI LMSPKFHCTE EILTIVSLLS VDSVLHNPPS
     RREEVQGVRK KFISSEGDHM TLLNIYRTFK NLGGNKDWCK ENFVNSKNMT LVAEVRAQLR
     DICLKMSMPI ASSRGDVESV RRCLAHSLFM STAELQPDGT YATTDTHQPV AIHPSSVLFH
     CKPACVVYTE LLYTNKCYMR DLCVIDAQWL YEAAPEYFRR KLRTARN
//
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