LMBD1_REOVL
ID LMBD1_REOVL Reviewed; 1275 AA.
AC Q9WAB2;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 23-FEB-2022, entry version 90.
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);
GN Name=L3;
OS Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Spinareovirinae; Orthoreovirus.
OX NCBI_TaxID=10884;
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).
RN [2]
RP INTERACTION WITH PROTEIN MU-NS.
RX PubMed=14747553; DOI=10.1128/jvi.78.4.1882-1892.2004;
RA Broering T.J., Kim J., Miller C.L., Piggott C.D., Dinoso J.B., Nibert M.L.,
RA Parker J.S.L.;
RT "Reovirus nonstructural protein mu NS recruits viral core surface proteins
RT and entering core particles to factory-like inclusions.";
RL J. Virol. 78:1882-1892(2004).
RN [3]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.0 ANGSTROMS).
RX PubMed=16216585; DOI=10.1016/j.str.2005.07.012;
RA Zhang X., Ji Y., Zhang L., Harrison S.C., Marinescu D.C., Nibert M.L.,
RA Baker T.S.;
RT "Features of reovirus outer capsid protein mu1 revealed by electron
RT cryomicroscopy and image reconstruction of the virion at 7.0 Angstrom
RT resolution.";
RL Structure 13:1545-1557(2005).
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:0000269|PubMed:14747553}.
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; AF129820; AAD42304.1; -; mRNA.
DR PDB; 2CSE; EM; 7.00 A; V/W=1-1275.
DR PDB; 6XF7; EM; 6.60 A; B/C=217-1275.
DR PDB; 6XF8; EM; 6.50 A; B/C=217-1275.
DR PDB; 6ZTS; EM; -; A/B=301-1275.
DR PDBsum; 2CSE; -.
DR PDBsum; 6XF7; -.
DR PDBsum; 6XF8; -.
DR PDBsum; 6ZTS; -.
DR SMR; Q9WAB2; -.
DR EvolutionaryTrace; Q9WAB2; -.
DR Proteomes; UP000007253; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Capsid protein; Helicase; Hydrolase;
KW Inner capsid protein; Metal-binding; mRNA capping; mRNA processing;
KW Nucleotide-binding; Reference proteome; Virion; Zinc; Zinc-finger.
FT CHAIN 1..1275
FT /note="Inner capsid protein lambda-1"
FT /id="PRO_0000344998"
FT ZN_FING 181..203
FT /note="C2H2-type"
FT REGION 1..149
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..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:6ZTS"
FT TURN 333..336
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 356..367
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 399..406
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 418..425
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 428..436
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 446..454
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 456..470
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 478..486
FT /evidence="ECO:0007829|PDB:6ZTS"
FT TURN 487..490
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 511..524
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 532..544
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 552..562
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 573..580
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 592..597
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 605..608
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 624..635
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 636..638
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 644..655
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 657..660
FT /evidence="ECO:0007829|PDB:6ZTS"
FT TURN 667..669
FT /evidence="ECO:0007829|PDB:6ZTS"
FT TURN 675..677
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 681..683
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 686..689
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 691..693
FT /evidence="ECO:0007829|PDB:6ZTS"
FT TURN 696..698
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 700..711
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 717..719
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 724..727
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 732..735
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 739..743
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 760..776
FT /evidence="ECO:0007829|PDB:6ZTS"
FT TURN 779..781
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 782..784
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 787..801
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 807..812
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 814..820
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 840..842
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 844..852
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 860..863
FT /evidence="ECO:0007829|PDB:6ZTS"
FT TURN 864..866
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 874..877
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 880..886
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 897..905
FT /evidence="ECO:0007829|PDB:6ZTS"
FT TURN 906..908
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 913..934
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 936..939
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 959..976
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 985..988
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 997..1003
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1008..1011
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 1019..1031
FT /evidence="ECO:0007829|PDB:6ZTS"
FT TURN 1032..1034
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 1035..1038
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1040..1052
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 1063..1065
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1069..1071
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1074..1076
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1082..1084
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1088..1090
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1093..1095
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1097..1099
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1106..1111
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 1112..1131
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1135..1146
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1149..1151
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1157..1159
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 1163..1168
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1181..1183
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1195..1203
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1220..1222
FT /evidence="ECO:0007829|PDB:6ZTS"
FT HELIX 1233..1236
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1242..1244
FT /evidence="ECO:0007829|PDB:6ZTS"
FT TURN 1247..1249
FT /evidence="ECO:0007829|PDB:6ZTS"
FT STRAND 1253..1260
FT /evidence="ECO:0007829|PDB:6ZTS"
FT TURN 1267..1270
FT /evidence="ECO:0007829|PDB:6ZTS"
SQ SEQUENCE 1275 AA; 141880 MW; D53864D04E374BF1 CRC64;
MKRIPRKTKG KSSGKGNDST ERSDDGSSQL RDKQNNKAGP ATTEPGTSNR EQYRARPGIA
SVQRATESAE LPMKNNDEGT PDKKGNTRGD LVNEHSEAKD EADEATQKQA KDTDKSKAQV
TYSDTGINNA NELSRSGNVD NEGGSNQKPM STRIAEATSA IVSKHPARVG LPPTASSGHG
YQCHVCSAVL FSPLDLDAHV ASHGLHGNMT LTSSEIQRHI TEFISSWQNH PIVQVSADVE
NKKTAQLLHA DTPRLVTWDA GLCTSFKIVP IVPAQVPQDV LAYTFFTSSY AIQSPFPEAA
VSRIVVHTRW ASNVDFDRDS SVIMAPPTEN NIHLFKQLLN TETLSVRGAN PLMFRANVLH
MLLEFVLDNL YLNRHTGFSQ DHTPFTEGAN LRSLPGPDAE KWYSIMYPTR MGTPNVSKIC
NFVASCVRNR VGRFDRAQMM NGAMSEWVDV FETSDALTVS IRGRWMARLA RMNINPTEIE
WALTECAQGY VTVTSPYAPS VNRLMPYRIS NAERQISQII RIMNIGNNAT VIQPVLQDIS
VLLQRISPLQ IDPTIISNTM STVSESTTQT LSPASSILGK LRPSNSDFSS FRVALAGWLY
NGVVTTVIDD SSYPKDGGSV TSLENLWDFF ILALALPLTT DPCAPVKAFM TLANMMVGFE
TIPMDNQIYT QSRRASAFST PHTWPRCFMN IQLISPIDAP ILRQWAEIIH RYWPNPSQIR
YGAPNVFGSA NLFTPPEVLL LPIDHQPANV TTPTLDFTNE LTNWRARVCE LMKNLVDNQR
YQPGWTQSLV SSMRGTLDKL KLIKSMTPMY LQQLAPVELA VIAPMLPFPP FQVPYVRLDR
DRVPTMVGVT RQSRDTITQP ALSLSTTNTT VGVPLALDAR AITVALLSGK YPPDLVTNVW
YADAIYPMYA DTEVFSNLQR DMITCEAVQT LVTLVAQISE TQYPVDRYLD WIPSLRASAA
TAATFAEWVN TSMKTAFDLS DMLLEPLLSG DPRMTQLAIQ YQQYNGRTFN VIPEMPGSVI
ADCVQLTAEV FNHEYNLFGI ARGDIIIGRV QSTHLWSPLA PPPDLVFDRD TPGVHIFGRD
CRISFGMNGA APMIRDETGM MVPFEGNWIF PLALWQMNTR YFNQQFDAWI KTGELRIRIE
MGAYPYMLHY YDPRQYANAW NLTSAWLEEI TPTSIPSVPF MVPISSDHDI SSAPAVQYII
STEYNDRSLF CTNSSSPQTI AGPDKHIPVE RYNILTNPDA PPTQIQLPEV VDLYNVVTRY
AYETPPITAV VMGVP
