RDRP_HPBVH
ID RDRP_HPBVH Reviewed; 534 AA.
AC Q50LE4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 29-SEP-2021, entry version 47.
DE RecName: Full=Potential RNA-dependent RNA polymerase;
DE EC=2.7.7.48;
GN Name=Segment-2; ORFNames=ORF3;
OS Human picobirnavirus (strain Human/Thailand/Hy005102/-) (PBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Duplopiviricetes;
OC Durnavirales; Picobirnaviridae; Picobirnavirus.
OX NCBI_TaxID=647332;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15847933; DOI=10.1016/j.jviromet.2005.02.010;
RA Wakuda M., Pongsuwanna Y., Taniguchi K.;
RT "Complete nucleotide sequences of two RNA segments of human
RT picobirnavirus.";
RL J. Virol. Methods 126:165-169(2005).
CC -!- FUNCTION: RNA-directed RNA polymerase that is involved in both
CC transcription and genome replication. {ECO:0000305}.
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;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
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DR EMBL; AB186898; BAD98236.1; -; Genomic_RNA.
DR RefSeq; YP_239361.1; NC_007027.1.
DR PDB; 5I61; X-ray; 2.40 A; A/B=2-534.
DR PDB; 5I62; X-ray; 2.00 A; A=2-534.
DR PDBsum; 5I61; -.
DR PDBsum; 5I62; -.
DR SMR; Q50LE4; -.
DR PRIDE; Q50LE4; -.
DR GeneID; 5075908; -.
DR KEGG; vg:5075908; -.
DR Proteomes; UP000007252; Genome.
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 InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR Pfam; PF00680; RdRP_1; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; RNA-directed RNA polymerase; Transferase;
KW Viral RNA replication; Virion.
FT CHAIN 1..534
FT /note="Potential RNA-dependent RNA polymerase"
FT /id="PRO_0000379525"
FT DOMAIN 255..373
FT /note="RdRp catalytic"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:5I62"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:5I62"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:5I62"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:5I62"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 208..228
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 288..296
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:5I61"
FT HELIX 327..345
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 370..378
FT /evidence="ECO:0007829|PDB:5I62"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 390..398
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 419..427
FT /evidence="ECO:0007829|PDB:5I62"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 435..438
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 441..451
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 452..454
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 460..469
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:5I62"
FT TURN 480..482
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 486..491
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 501..505
FT /evidence="ECO:0007829|PDB:5I61"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:5I62"
FT HELIX 525..532
FT /evidence="ECO:0007829|PDB:5I62"
SQ SEQUENCE 534 AA; 60975 MW; 291A6AC71B028C4F CRC64;
MQVAPNVWSK YFNIPNPGLR AYFSNVVSGQ PEVYRTPFYK GMSLESICDE WYKKLVSIDT
QWPTLMEFED DLRKKVGPMS VMLPLKERMS DIDSYYDSIS KDQVPFDTKA ISAAKSEWKG
VSRLRLRSEV NTVAVMKKST NSGSPYFSKR KAVVSKTIPC DVYMDGRYCV MRQNGREWSG
AAVLGWRGQE GGPKPTDVKQ RVVWMFPFAV NIRELQVYQP LILTFQRLGL VPAWVSMEAV
DRRITKMFDT KGPRDVVVCT DFSKFDQHFN PTCQSVAKEL LADLLTGQEA VDWLERVFPI
KYAIPLAYNW GEIRYGIHGM GSGSGGTNAD ETLVHRVLQH EAAISHHTTL NPNSQCLGDD
GVLTYPGISA EDVMQSYSRH GLDMNLEKQY VSKQDCTYLR RWHHTDYRVD GMCVGVYSTM
RALGRLAMQE RYYDPDVWGE KMVTLRYLSI IENVKYHPLK EEFLDFCIKG DKTRLGLGIP
GFLDNIAGEA QKAIDMMPDF LGYTKSLQYD GDLRRNAAAG IENWWVVQAL KSRR
