RDRP_I18A0
ID RDRP_I18A0 Reviewed; 757 AA.
AC Q3HM40;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=RNA-directed RNA polymerase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_04065};
DE EC=2.7.7.48 {ECO:0000255|HAMAP-Rule:MF_04065};
DE AltName: Full=Polymerase basic protein 1 {ECO:0000255|HAMAP-Rule:MF_04065};
DE Short=PB1 {ECO:0000255|HAMAP-Rule:MF_04065};
DE AltName: Full=RNA-directed RNA polymerase subunit P1 {ECO:0000255|HAMAP-Rule:MF_04065};
GN Name=PB1 {ECO:0000255|HAMAP-Rule:MF_04065};
OS Influenza A virus (strain A/Brevig Mission/1/1918 H1N1) (Influenza A virus
OS (strain A/South Carolina/1/1918 H1N1)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=88776;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16208372; DOI=10.1038/nature04230;
RA Taubenberger J.K., Reid A.H., Lourens R.M., Wang R., Jin G., Fanning T.G.;
RT "Characterization of the 1918 influenza virus polymerase genes.";
RL Nature 437:889-893(2005).
CC -!- FUNCTION: RNA-dependent RNA polymerase which is responsible for
CC replication and transcription of virus RNA segments. The transcription
CC of viral mRNAs occurs by a unique mechanism called cap-snatching. 5'
CC methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides
CC by PA. In turn, these short capped RNAs are used as primers by PB1 for
CC transcription of viral mRNAs. During virus replication, PB1 initiates
CC RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn
CC serves as a template for the production of more vRNAs.
CC {ECO:0000255|HAMAP-Rule:MF_04065}.
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|HAMAP-Rule:MF_04065};
CC -!- SUBUNIT: Influenza RNA polymerase is composed of three subunits: PB1,
CC PB2 and PA. Interacts (via N-terminus) with PA (via C-terminus).
CC Interacts (via C-terminus) with PB2 (via N-terminus); this interaction
CC is essential for transcription initiation. {ECO:0000255|HAMAP-
CC Rule:MF_04065}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04065}.
CC Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04065}.
CC -!- PTM: Phosphorylated by host PRKCA. {ECO:0000255|HAMAP-Rule:MF_04065}.
CC -!- MISCELLANEOUS: South Carolina isolate has been sequenced from formalid
CC fixed-lung tissues of a 21-year-old male which died in 1918 at Ft.
CC Jackson, SC. Brevig Mission isolate has been sequenced from lung
CC tissues of an Inuit woman buried in the permafrost in a gravesite near
CC Brevig Mission, Alaska. This sample was recovered by John Hultin,
CC retired pathologist.
CC -!- SIMILARITY: Belongs to the influenza viruses polymerase PB1 family.
CC {ECO:0000255|HAMAP-Rule:MF_04065}.
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DR EMBL; DQ208310; ABA55039.1; -; mRNA.
DR PDB; 7NHA; EM; 2.91 A; B=1-757.
DR PDB; 7NHC; EM; 2.87 A; B=1-757.
DR PDB; 7NHX; EM; 3.23 A; B=1-757.
DR PDB; 7NI0; EM; 3.32 A; B=1-757.
DR PDB; 7NIK; EM; 6.20 A; B=1-757.
DR PDB; 7NIL; EM; 5.01 A; B=1-757.
DR PDB; 7NIR; EM; 6.70 A; B=1-757.
DR PDB; 7NIS; EM; 5.96 A; B=1-757.
DR PDB; 7NJ3; EM; 4.48 A; B=1-757.
DR PDB; 7NJ4; EM; 5.84 A; B=1-757.
DR PDB; 7NJ5; EM; 4.63 A; B=1-757.
DR PDB; 7NJ7; EM; 4.82 A; B=1-757.
DR PDB; 7NK1; EM; 4.22 A; B=1-757.
DR PDB; 7NK2; EM; 4.84 A; B=1-757.
DR PDB; 7NK4; EM; 5.32 A; B=1-757.
DR PDB; 7NK6; EM; 6.72 A; B=1-757.
DR PDB; 7NK8; EM; 5.34 A; B=1-757.
DR PDB; 7NKA; EM; 4.07 A; B=1-757.
DR PDB; 7NKC; EM; 4.46 A; B=1-757.
DR PDB; 7NKI; EM; 4.67 A; B=1-757.
DR PDB; 7NKR; EM; 5.60 A; B=1-757.
DR PDBsum; 7NHA; -.
DR PDBsum; 7NHC; -.
DR PDBsum; 7NHX; -.
DR PDBsum; 7NI0; -.
DR PDBsum; 7NIK; -.
DR PDBsum; 7NIL; -.
DR PDBsum; 7NIR; -.
DR PDBsum; 7NIS; -.
DR PDBsum; 7NJ3; -.
DR PDBsum; 7NJ4; -.
DR PDBsum; 7NJ5; -.
DR PDBsum; 7NJ7; -.
DR PDBsum; 7NK1; -.
DR PDBsum; 7NK2; -.
DR PDBsum; 7NK4; -.
DR PDBsum; 7NK6; -.
DR PDBsum; 7NK8; -.
DR PDBsum; 7NKA; -.
DR PDBsum; 7NKC; -.
DR PDBsum; 7NKI; -.
DR PDBsum; 7NKR; -.
DR SMR; Q3HM40; -.
DR Proteomes; UP000008430; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0039523; P:suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:UniProtKB-UniRule.
DR GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
DR HAMAP; MF_04065; INFV_RDRP; 1.
DR InterPro; IPR007099; RNA-dir_pol_NSvirus.
DR InterPro; IPR001407; RNA_pol_PB1_influenza.
DR Pfam; PF00602; Flu_PB1; 1.
DR PIRSF; PIRSF000827; RdRPol_OMV; 1.
DR PROSITE; PS50525; RDRP_SSRNA_NEG_SEG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host transcription shutoff by virus; Host cytoplasm;
KW Host gene expression shutoff by virus; Host nucleus;
KW Host-virus interaction; Inhibition of host RNA polymerase II by virus;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW RNA-directed RNA polymerase; Transferase; Viral RNA replication;
KW Viral transcription.
FT CHAIN 1..757
FT /note="RNA-directed RNA polymerase catalytic subunit"
FT /id="PRO_0000310574"
FT DOMAIN 286..483
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT REGION 53..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..256
FT /note="Promoter-binding site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT MOTIF 187..195
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT MOTIF 203..216
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT HELIX 5..10
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:7NHC"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:7NHC"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:7NHA"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:7NHC"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 249..264
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:7NHA"
FT HELIX 275..289
FT /evidence="ECO:0007829|PDB:7NHC"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:7NHC"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 315..325
FT /evidence="ECO:0007829|PDB:7NHC"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 331..345
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:7NHC"
FT TURN 360..363
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:7NHC"
FT TURN 373..375
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 383..392
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:7NHA"
FT HELIX 413..425
FT /evidence="ECO:0007829|PDB:7NHC"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 446..455
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 456..471
FT /evidence="ECO:0007829|PDB:7NHC"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 495..501
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 505..511
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 519..535
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 541..559
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 573..582
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 591..593
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 601..603
FT /evidence="ECO:0007829|PDB:7NHA"
FT HELIX 608..611
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 613..615
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 618..624
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:7NHX"
FT HELIX 637..639
FT /evidence="ECO:0007829|PDB:7NHX"
FT STRAND 640..645
FT /evidence="ECO:0007829|PDB:7NHA"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:7NHA"
FT HELIX 673..676
FT /evidence="ECO:0007829|PDB:7NHC"
FT TURN 679..681
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 682..699
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 701..703
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 711..713
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 714..731
FT /evidence="ECO:0007829|PDB:7NHC"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:7NHC"
FT HELIX 737..755
FT /evidence="ECO:0007829|PDB:7NHC"
SQ SEQUENCE 757 AA; 86513 MW; DB60EB2DD7D7C4ED CRC64;
MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGRWTTNTE
TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEVVQQTRVD
KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMDKEEME
ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RLNKRSYLIR ALTLNTMTKD AERGKLKRRA
IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF
TITGDNTKWN ENQNPRMFLA MITYITRNQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK
SMKLRTQIPA EMLASIDLKY FNDSTRKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG
VSILNLGQKR YTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVDRFYRTC KLLGINMSKK
KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG
PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFEIKKLW EQTRSKAGLL VSDGGPNLYN
IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHKEIESV NNAVMMPAHG PAKNMEYDAV
ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPVG ISSMVEAMVS
RARIDARIDF ESGRIKKEEF AEIMKICSTI EELRRQK
