RDRP_I68A6
ID RDRP_I68A6 Reviewed; 757 AA.
AC P03432;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 98.
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/Northern Territory/60/1968 H3N2) (Influenza A
OS virus (strain NT60)) (Influenza A virus (strain A/NT/60/1968 H3N2)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=384505;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9721; Cetacea (whales).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9709; Phocidae (true seals).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7041090; DOI=10.1093/nar/10.4.1335;
RA Bishop D.H.L., Huddleston J.A., Brownlee G.G.;
RT "The complete sequence of RNA segment 2 of influenza A/NT/60/68 P1
RT protein.";
RL Nucleic Acids Res. 10:1335-1343(1982).
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 -!- SIMILARITY: Belongs to the influenza viruses polymerase PB1 family.
CC {ECO:0000255|HAMAP-Rule:MF_04065}.
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DR EMBL; J02138; AAA43579.1; -; Genomic_RNA.
DR PIR; A93415; P1IV68.
DR PDB; 6QNW; X-ray; 3.31 A; B/E/H/K=1-757.
DR PDB; 6QPG; X-ray; 3.34 A; B/E/H/K=1-757.
DR PDB; 6QX8; EM; 4.07 A; B/F=1-757.
DR PDB; 6QXE; EM; 4.15 A; B/F=1-757.
DR PDB; 6RR7; EM; 3.01 A; B=1-757.
DR PDBsum; 6QNW; -.
DR PDBsum; 6QPG; -.
DR PDBsum; 6QX8; -.
DR PDBsum; 6QXE; -.
DR PDBsum; 6RR7; -.
DR SMR; P03432; -.
DR IntAct; P03432; 2.
DR ABCD; P03432; 1 sequenced antibody.
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_0000078762"
FT DOMAIN 286..483
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT REGION 50..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 COMPBIAS 50..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 142
FT /note="A -> T (in Ref. 1; AAA43579)"
FT CONFLICT 632
FT /note="V -> I (in Ref. 1; AAA43579)"
FT HELIX 5..10
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:6QNW"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6QNW"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 249..264
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 276..292
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 295..304
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 315..325
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 339..343
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 360..363
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:6QNW"
FT HELIX 383..392
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 413..424
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 446..455
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 456..471
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:6QNW"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 495..501
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 519..535
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 541..559
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 571..574
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 575..582
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:6QNW"
FT HELIX 591..593
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 601..603
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 604..606
FT /evidence="ECO:0007829|PDB:6QNW"
FT TURN 608..612
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 618..624
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 637..639
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 640..645
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 674..676
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 681..699
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 701..704
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 711..713
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 714..731
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 737..754
FT /evidence="ECO:0007829|PDB:6RR7"
SQ SEQUENCE 757 AA; 86413 MW; 178E54ED5B3D6F94 CRC64;
MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNTE
TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEVVQQTRVD
RLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMDKEEME
ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RVNKRSYLIR ALTLNTMTKD AERGKLKRRA
IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF
TITGDNTKWN ENQNPRMFLA MITYITKNQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK
SMKLRTQIPA EMLASIDLKY FNESTRKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG
VSILNLGQKR YTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVDRFYRTC KLVGINMSKK
KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG
PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFELEKLW EQTRSKAGLL VSDGGPNLYN
IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHKEIESV NNAVVMPAHG PAKSMEYDAV
ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPVG ISSMVEAMVS
RARIDARIDF ESGRIKKEEF AEIMKICSTI EELRRQK
