LMBD1_REOVJ
ID LMBD1_REOVJ Reviewed; 1275 AA.
AC Q9WAB1;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Inner capsid protein lambda-1;
DE Short=Lambda1;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent DNA helicase lambda-1;
DE AltName: Full=Lambda1(Hel);
OS Reovirus type 2 (strain D5/Jones) (T2J) (Mammalian orthoreovirus 2).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Spinareovirinae; Orthoreovirus.
OX NCBI_TaxID=10885;
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10329567; DOI=10.1006/viro.1999.9707;
RA Harrison S.J., Farsetta D.L., Kim J., Noble S., Broering T.J., Nibert M.L.;
RT "Mammalian reovirus L3 gene sequences and evidence for a distinct amino-
RT terminal region of the lambda1 protein.";
RL Virology 258:54-64(1999).
CC -!- FUNCTION: Inner capsid (core) component. Displays NTPase, RNA 5'-
CC triphosphatase (RTPase) and RNA helicase activities and probably
CC participates in transcription of the viral genome. Helicase activity
CC might be involved in unwinding or reannealing dsRNA during RNA
CC synthesis. RTPase enzymatic activity represents the first step in RNA
CC capping, which yields a 5'-diphosphorylated plus-strand RNA (By
CC similarity). {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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with protein mu-NS; in viral inclusions.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Found in the inner
CC capsid (120 copies). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the orthoreovirus lambda-1 protein family.
CC {ECO:0000305}.
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DR EMBL; AF129821; AAD42305.1; -; mRNA.
DR SMR; Q9WAB1; -.
DR Proteomes; UP000006370; Genome.
DR GO; GO:0039625; C:viral inner capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1830.10; -; 1.
DR InterPro; IPR044949; Lambda-1/VP3.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Capsid protein; Helicase; Hydrolase; Inner capsid protein;
KW Metal-binding; mRNA capping; mRNA processing; Nucleotide-binding; Virion;
KW Zinc; Zinc-finger.
FT CHAIN 1..1275
FT /note="Inner capsid protein lambda-1"
FT /id="PRO_0000344997"
FT ZN_FING 181..203
FT /note="C2H2-type"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1275 AA; 142031 MW; 1238F825C0A27CF2 CRC64;
MKRIPRKTRG KSSGKGNDST ERADDGSAQL RDKQSSKVTQ NVKEPGTTLK EQYKTRPSLQ
TVQKATENAE LPMQTNDEGA VDKKGNTKGD KTNEHVEAEV NAADATKRQA KDTDKQKAQV
TYNDTGINNA NELSRSGNVD NEGGDNQKPM TTRIAEATSA IISKHPARVG LPPTASSGHG
YQCHVCSAVL FSPLDLDAHV ASHGLHGNMT LTSSEIQRHI TEFISSWQNH PIVQVSADVE
NKKTAQLLHA DTPRLVTWDA GLCTSFKIVP IVPAQVPQDV LAYTFFTSSY AIQSPFPEAA
VSRIVVHTRW ASNVDFDRDS SVIMAPPTEN NIHLFKQLLN NETLSVRGAN PLMFRANVLH
MLLEFVLDNL YINKHTGFSQ DHTPFTEGAN LRSLPGPDAE KWYAIMYPTR MGTPNVSKIC
NFVASCVRNR VGRFDRAQMM NGAMSEWVDV FETSDALTVS IRGRWMARLA RMNINPTEIE
WALTECAHGY VTVTSPYAPS VNRLMPYRVS NAERQISQII RIMNIGNNAT VIQPVLQDIS
VLLQRISPLQ IDPTIISNTM STVSESTTQT LSPASSILGK LRPSNSDFSS FRVALAGWLY
NGVVTTVIDD SSYPKDGGSV TSLENLWDFF ILALALPLTT DPCAPVKAFM TLANMMVGFE
TIPMDNQIYT QSRRASAFST PHTWPRCFMN IQLISPIDAP ILRQWAEIIH RYWPNPSQIR
FGAPNVFGSA NLFTPPEVLL LPIDHQPANV TTPTLDFTNE LTNWRARVCE LMKNLVDNQR
YQPGWTQSLV SSMRGTLDKL KLIKSMTPMY LQQLAPVELA VIAPMLPFPP FQVPYVRLDR
DRVPTMVGVT RQSRDTITQP ALSLSTTNTT VGVPLALDAR AITVALLSGK YPSDLVTNVW
YADAIYPMYA DTEVFSNLQR DMITCEAVQT LITLVAQISE TQYPVDRYLD WIPSLRASAA
TAATFAEWVN TSMKTAFDLS DMLLEPLLSG DPRMSQLAIQ YQQYNGRTFN VIPEMPGSVV
TDCVQLTAEV FNHEYNLFGI ARGDIIIGRV QSTHLWSPLA PPPDLVFDRD TPGVHVFGRD
CRISFGMNGA APMIRDETGM MVPFEGNWIF PLALWQMNTR YFNQQFDAWI KTGELRIRIE
MGAYPYMLHY YDPRQYANAW NLTSAWLEEI SPTSIPSVPF MVPISSDHDI SSAPAVQYII
STEYNDRSLF CTNSSSPQTI AGPDKHIPVE RYNILTNPDA PPTQIQLPEV VDLYNVVTRY
AYETPPITAV VMGVP