RDRP_ROTSP
ID RDRP_ROTSP Reviewed; 1088 AA.
AC O37061;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 29-SEP-2021, entry version 71.
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=Protein VP1;
OS Rotavirus A (strain RVA/SA11-Patton/G3P[X]) (RV-A) (Simian Agent 11 (strain
OS Patton)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=36434;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9371626; DOI=10.1128/jvi.71.12.9618-9626.1997;
RA Patton J.T., Jones M.T., Kalbach A.N., He Y.-W., Xiaobo J.;
RT "Rotavirus RNA polymerase requires the core shell protein to synthesize the
RT double-stranded RNA genome.";
RL J. Virol. 71:9618-9626(1997).
RN [2]
RP INTERACTION WITH NSP2.
RX PubMed=8030243; DOI=10.1006/viro.1994.1402;
RA Kattoura M.D., Chen X., Patton J.T.;
RT "The rotavirus RNA-binding protein NS35 (NSP2) forms 10S multimers and
RT interacts with the viral RNA polymerase.";
RL Virology 202:803-813(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), COFACTOR, AND FUNCTION.
RX PubMed=19000820; DOI=10.1016/j.str.2008.09.006;
RA Lu X., McDonald S.M., Tortorici M.A., Tao Y.J., Vasquez-Del Carpio R.,
RA Nibert M.L., Patton J.T., Harrison S.C.;
RT "Mechanism for coordinated RNA packaging and genome replication by
RT rotavirus polymerase VP1.";
RL Structure 16:1678-1688(2008).
CC -!- FUNCTION: RNA-directed RNA polymerase that is involved in both
CC transcription and genome replication. Together with VP3 capping enzyme,
CC forms an enzyme complex positioned near the channels situated at each
CC of the five-fold vertices of the core. Following infection, the
CC outermost layer of the virus is lost, leaving a double-layered particle
CC (DLP) made up of the core and VP6 shell. VP1 then catalyzes the
CC transcription of fully conservative plus-strand genomic RNAs that are
CC extruded through the DLP's channels into the cytoplasm where they
CC function as mRNAs for translation of viral proteins. One copy of each
CC of the viral (+)RNAs is also recruited during core assembly, together
CC with newly synthesized polymerase complexes and VP2. The polymerase of
CC these novo-formed particles catalyzes the synthesis of complementary
CC minus-strands leading to dsRNA formation. To do so, the polymerase
CC specifically recognizes and binds 4 bases 5'-UGUG-3' in the conserved
CC 3'-sequence of plus-strand RNA templates. VP2 presumably activates the
CC autoinhibited VP1-RNA complex to coordinate packaging and genome
CC replication. Once dsRNA synthesis is complete, the polymerase switches
CC to the transcriptional mode, thus providing secondary transcription.
CC {ECO:0000255|PROSITE-ProRule:PRU00539, ECO:0000269|PubMed:19000820,
CC ECO:0000269|PubMed:9371626}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with VP3 (Potential). Interacts with VP2; this
CC interaction activates VP1. Interacts with NSP5; this interaction is
CC probably necessary for the formation of functional virus factories.
CC Interacts with NSP2; this interaction is weak (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Attached inside the
CC inner capsid as a minor component. Also found in spherical cytoplasmic
CC structures, called virus factories, that appear early after infection
CC and are the site of viral replication and packaging (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the reoviridae RNA-directed RNA polymerase
CC family. {ECO:0000305}.
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DR EMBL; AF015955; AAC58684.1; ALT_TERM; mRNA.
DR PDB; 2R7O; X-ray; 3.35 A; A=1-1088.
DR PDB; 2R7Q; X-ray; 2.90 A; A=1-1088.
DR PDB; 2R7R; X-ray; 2.60 A; A=1-1088.
DR PDB; 2R7S; X-ray; 3.24 A; A=1-1088.
DR PDB; 2R7T; X-ray; 3.00 A; A=1-1088.
DR PDB; 2R7U; X-ray; 3.10 A; A=1-1088.
DR PDB; 2R7V; X-ray; 2.80 A; A=1-1088.
DR PDB; 2R7W; X-ray; 2.60 A; A=1-1088.
DR PDB; 2R7X; X-ray; 2.80 A; A/B=1-1088.
DR PDB; 4F5X; X-ray; 5.00 A; W=1-1088.
DR PDBsum; 2R7O; -.
DR PDBsum; 2R7Q; -.
DR PDBsum; 2R7R; -.
DR PDBsum; 2R7S; -.
DR PDBsum; 2R7T; -.
DR PDBsum; 2R7U; -.
DR PDBsum; 2R7V; -.
DR PDBsum; 2R7W; -.
DR PDBsum; 2R7X; -.
DR PDBsum; 4F5X; -.
DR SMR; O37061; -.
DR EvolutionaryTrace; O37061; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR Gene3D; 1.10.10.1990; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042032; RNA-dir_pol_4-hel_dom.
DR InterPro; IPR001795; RNA-dir_pol_luteovirus.
DR InterPro; IPR007097; RNA-dir_pol_reovirus.
DR InterPro; IPR022071; Rotavirus_VP1_C.
DR Pfam; PF02123; RdRP_4; 1.
DR Pfam; PF12289; Rotavirus_VP1; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50523; RDRP_DSRNA_REO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Nucleotide-binding; Nucleotidyltransferase;
KW RNA-binding; RNA-directed RNA polymerase; Transferase;
KW Viral RNA replication; Virion.
FT CHAIN 1..1088
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000367812"
FT DOMAIN 501..687
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 32..49
FT /evidence="ECO:0007829|PDB:2R7R"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:2R7R"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:2R7R"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 138..151
FT /evidence="ECO:0007829|PDB:2R7R"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 157..178
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:2R7R"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:2R7X"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:2R7R"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 282..297
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 302..310
FT /evidence="ECO:0007829|PDB:2R7R"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:2R7R"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 320..328
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 339..344
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 361..373
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 376..380
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 389..396
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 399..410
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 413..419
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 420..428
FT /evidence="ECO:0007829|PDB:2R7R"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 442..445
FT /evidence="ECO:0007829|PDB:2R7V"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 468..485
FT /evidence="ECO:0007829|PDB:2R7R"
FT TURN 491..493
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 499..508
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 514..520
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 522..525
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 528..546
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 552..569
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 571..576
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 578..586
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 596..616
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 622..629
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 632..638
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 645..660
FT /evidence="ECO:0007829|PDB:2R7R"
FT TURN 661..663
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 667..673
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 675..677
FT /evidence="ECO:0007829|PDB:2R7Q"
FT STRAND 681..683
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 686..688
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:2R7V"
FT HELIX 706..723
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 729..740
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 742..752
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 754..758
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 759..761
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 779..790
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 797..804
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 806..819
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 826..837
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 838..841
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 843..860
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 874..881
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 882..884
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 885..890
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 905..914
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 929..937
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 944..951
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 955..964
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 969..975
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 979..996
FT /evidence="ECO:0007829|PDB:2R7R"
FT TURN 997..1000
FT /evidence="ECO:0007829|PDB:2R7R"
FT TURN 1002..1006
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 1012..1016
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 1027..1048
FT /evidence="ECO:0007829|PDB:2R7R"
FT STRAND 1049..1056
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 1060..1070
FT /evidence="ECO:0007829|PDB:2R7R"
FT HELIX 1079..1087
FT /evidence="ECO:0007829|PDB:2R7R"
SQ SEQUENCE 1088 AA; 125252 MW; 7A5AD04A37BA0E8C CRC64;
MGKYNLILSE YLSFIYNSQS AVQIPIYYSS NSELENRCIE FHSKCLENSK NGLSLRKLFV
EYNDVIENAT LLSILSYSYD KYNAVERKLV KYAKGKPLEA DLTVNELDYE NNKMTSELFP
TAEEYTDSLM DPAILTSLSS NLNAVMFWLE KHENDVAEKL KVYKRRLDLF TIVASTINKY
GVPRHNAKYR YEYDVMKDKP YYLVTWANSS IEMLMSVFSH DDYLIAKELI VLSYSNRSTL
AKLVSSPMSI LVALVDINGT FITNEELELE FSNKYVRAIV PDQTFDELNQ MLDNMRKAGL
VDIPKMIQDW LVDRSIEKFP LMAKIYSWSF HVGFRKQKML DAALDQLKTE YTENVDDEMY
REYTMLIRDE VVKMLEEPVK HDDHLLRDSE LAGLLSMSSA SNGESRQLKF GRKTIFSTKK
NMHVMDDMAN ERYTPGIIPP VNVDKPIPLG RRDVPGRRTR IIFILPYEYF IAQHAVVEKM
LIYAKHTREY AEFYSQSNQL LSYGDVTRFL SNNTMVLYTD VSQWDSSQHN TQPFRKGIIM
GLDILANMTN DAKVLQTLNL YKQTQINLMD SYVQIPDGNV IKKIQYGAVA SGEKQTKAAN
SIANLALIKT VLSRISNKHS FATKIIRVDG DDNYAVLQFN TEVTKQMIQD VSNDVRETYA
RMNAKVKALV STVGIEIAKR YIAGGKIFFR AGINLLNNEK RGQSTQWDQA AILYSNYIVN
RLRGFETDRE FILTKIMQMT SVAITGSLRL FPSERVLTTN STFKVFDSED FIIEYGTTVD
EVYIQRAFMS LSSQKSGIAD EIAASSTFKN YVTRLSEQLL FSKNNIVSRG IALTEKAKLN
SYAPISLEKR RAQISALLTM LQKPVTFKSS KITINDILRD IKPFFTVSDA HLPIQYQKFM
PTLPDNVQYI IQCIGSRTYQ IEDDGSKSAI SRLISKYSVY KPSIEELYKV ISLHENEIQL
YLISLGIPKI DADTYVGSKI YSRDKYRILE SYVYNLLSIN YGCYQLFDFN SPDLEKLIRI
PFKGKIPAVT FILHLYAKLE VINYAIKNGS WISLFCNYPK SEMIKLWKKM WNITSLRSPY
TNANFFQE
