GenomeNet

Database: UniProt
Entry: Q5UQ98
LinkDB: Q5UQ98
Original site: Q5UQ98 
ID   YL538_MIMIV             Reviewed;         445 AA.
AC   Q5UQ98;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   18-SEP-2019, entry version 54.
DE   RecName: Full=Putative ATP-dependent RNA helicase L538;
DE            EC=3.6.4.13;
GN   OrderedLocusNames=MIMI_L538;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=16971431; DOI=10.1128/jvi.00940-06;
RA   Renesto P., Abergel C., Decloquement P., Moinier D., Azza S.,
RA   Ogata H., Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D.;
RT   "Mimivirus giant particles incorporate a large fraction of anonymous
RT   and unique gene products.";
RL   J. Virol. 80:11678-11685(2006).
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: Virion {ECO:0000269|PubMed:16971431}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. {ECO:0000305}.
DR   EMBL; AY653733; AAV50802.1; -; Genomic_DNA.
DR   PRIDE; Q5UQ98; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Reference proteome; Virion.
FT   CHAIN         1    445       Putative ATP-dependent RNA helicase L538.
FT                                /FTId=PRO_0000253413.
FT   DOMAIN       14    151       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      273    442       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      27     34       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       101    104       DEAH box.
SQ   SEQUENCE   445 AA;  51580 MW;  CBDA9ECDC5FF95CF CRC64;
     MDSIILKNHQ KKPIEFMKNN RGVILYHSTG AGKTLTAIYS VYQFDYPIII IGPKSSKKAF
     TDNIEKAGMD ISRFTFYTYT KIKMILESDI TIFKNMSVIV DEAHSLRNEN MYNLYISSAL
     MLASKIILLT ATPVVNYFND LAVLVNIVRG EDSLPTERAL FDQMFYDEET MTLINAPILF
     NKLLNTISYY KIIDTINYPT SESHIKQVEM DHLQIDEYKY YIKQILYSNE NVPDNVDIFN
     INYGLLPSKK RNFFLNVTRQ LSNVAKIADT SPKIEDIMKY IISGPYPIVI YSNFLKSGIY
     TLAVRLEKEN ISYKIISGFV SQDKLNMIVN NYNNGLFKVL LISSAGSESL DLKNTHQVHI
     MEPHWNESKI IQVIGRSIRY GSHISLPQNE RKVDIYRWIS IFPNQYRNIS ADEYLTTLSQ
     RKMELWNKYN QIVIDASIEN NYFAK
//
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