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   27-MAR-2024, entry version 92.
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; Spinareoviridae; Orthoreovirus; Mammalian 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; Inner capsid protein lambda-1; 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
//