P1_BPPH6
ID P1_BPPH6 Reviewed; 769 AA.
AC P11126;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 29-SEP-2021, entry version 80.
DE RecName: Full=Major inner protein P1;
GN Name=P1;
OS Pseudomonas phage phi6 (Bacteriophage phi-6).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Vidaverviricetes;
OC Mindivirales; Cystoviridae; Cystovirus.
OX NCBI_TaxID=10879;
OH NCBI_TaxID=319; Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv. phaseolicola).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3346944; DOI=10.1128/jvi.62.4.1180-1185.1988;
RA Mindich L., Nemhauser I., Gottlieb P., Romantschuk M., Carton J.,
RA Frucht S., Strassman J., Bamford D.H., Kalkkinen N.;
RT "Nucleotide sequence of the large double-stranded RNA segment of
RT bacteriophage phi 6: genes specifying the viral replicase and
RT transcriptase.";
RL J. Virol. 62:1180-1185(1988).
RN [2]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=14563876; DOI=10.1128/jb.185.21.6409-6414.2003;
RA Qiao X., Qiao J., Mindich L.;
RT "Analysis of specific binding involved in genomic packaging of the double-
RT stranded-RNA bacteriophage phi6.";
RL J. Bacteriol. 185:6409-6414(2003).
RN [3]
RP STRUCTURE BY ELECTRON MICROSCOPY (14.0 ANGSTROMS).
RX PubMed=17292834; DOI=10.1016/j.str.2006.12.004;
RA Jaalinoja H.T., Huiskonen J.T., Butcher S.J.;
RT "Electron cryomicroscopy comparison of the architectures of the enveloped
RT bacteriophages phi6 and phi8.";
RL Structure 15:157-167(2007).
CC -!- FUNCTION: P1 is the major inner capsid (core) protein of the polyhedral
CC procapsid, which is responsible for genomic replication and
CC transcription. Forms a dodecahedral shell from 60 asymmetric dimers.
CC Binds to RNA and may be involved in genomic packaging.
CC {ECO:0000269|PubMed:14563876}.
CC -!- SUBUNIT: Homodimer. Associates with the polymerase complex.
CC -!- INTERACTION:
CC P11126; P11126: P1; NbExp=4; IntAct=EBI-15586148, EBI-15586148;
CC -!- SUBCELLULAR LOCATION: Virion. Note=Inner capsid protein (120 copies).
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DR EMBL; M17461; AAA32357.1; -; Genomic_RNA.
DR PIR; D29885; P1BPF6.
DR RefSeq; NP_620348.1; NC_003715.1.
DR PDB; 4BTG; EM; 4.40 A; A/B=2-761.
DR PDB; 4BTQ; EM; 7.50 A; A/B=2-761.
DR PDB; 4K7H; X-ray; 3.60 A; A/B/C/D/E=2-769.
DR PDB; 5FJ5; EM; 4.80 A; A/B=2-761.
DR PDB; 5FJ7; EM; 7.90 A; A/B=2-761.
DR PDB; 5MUU; EM; 4.00 A; A/B=1-769.
DR PDB; 6HY0; EM; 3.50 A; A/B=1-769.
DR PDBsum; 4BTG; -.
DR PDBsum; 4BTQ; -.
DR PDBsum; 4K7H; -.
DR PDBsum; 5FJ5; -.
DR PDBsum; 5FJ7; -.
DR PDBsum; 5MUU; -.
DR PDBsum; 6HY0; -.
DR SMR; P11126; -.
DR DIP; DIP-29115N; -.
DR IntAct; P11126; 2.
DR GeneID; 956438; -.
DR KEGG; vg:956438; -.
DR Proteomes; UP000002610; Genome.
DR GO; GO:0039616; C:T=2 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0039625; C:viral inner capsid; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Direct protein sequencing;
KW Inner capsid protein; Reference proteome; RNA-binding;
KW T=2 icosahedral capsid protein; Transcription; Viral nucleoprotein; Virion.
FT CHAIN 1..769
FT /note="Major inner protein P1"
FT /id="PRO_0000164637"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 63..76
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:6HY0"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:6HY0"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:6HY0"
FT TURN 158..162
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 183..201
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 222..239
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 246..261
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 279..284
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 314..326
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 339..349
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 393..407
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 414..423
FT /evidence="ECO:0007829|PDB:6HY0"
FT TURN 429..433
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 442..450
FT /evidence="ECO:0007829|PDB:6HY0"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 458..464
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 473..497
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 515..523
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 530..533
FT /evidence="ECO:0007829|PDB:6HY0"
FT TURN 536..538
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 539..544
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 547..550
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 568..571
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 591..597
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 600..606
FT /evidence="ECO:0007829|PDB:6HY0"
FT TURN 610..613
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 627..651
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 657..682
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 685..705
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 710..713
FT /evidence="ECO:0007829|PDB:6HY0"
FT TURN 717..720
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 721..734
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:6HY0"
FT HELIX 740..753
FT /evidence="ECO:0007829|PDB:6HY0"
FT STRAND 756..758
FT /evidence="ECO:0007829|PDB:6HY0"
SQ SEQUENCE 769 AA; 84987 MW; 30B7C56BB6BEE326 CRC64;
MFNLKVKDLN GSARGLTQAF AIGELKNQLS VGALQLPLQF TRTFSASMTS ELLWEVGKGN
IDPVMYARLF FQYAQAGGAL SVDELVNQFT EYHQSTACNP EIWRKLTAYI TGSSNRAIKA
DAVGKVPPTA ILEQLRTLAP SEHELFHHIT TDFVCHVLSP LGFILPDAAY VYRVGRTATY
PNFYALVDCV RASDLRRMLT ALSSVDSKML QATFKAKGAL APALISQHLA NAATTAFERS
RGNFDANAVV SSVLTILGRL WSPSTPKELD PSARLRNTNG IDQLRSNLAL FIAYQDMVKQ
RGRAEVIFSD EELSSTIIPW FIEAMSEVSP FKLRPINETT SYIGQTSAID HMGQPSHVVV
YEDWQFAKEI TAFTPVKLAN NSNQRFLDVE PGISDRMSAT LAPIGNTFAV SAFVKNRTAV
YEAVSQRGTV NSNGAEMTLG FPSVVERDYA LDRDPMVAIA ALRTGIVDES LEARASNDLK
RSMFNYYAAV MHYAVAHNPE VVVSEHQGVA AEQGSLYLVW NVRTELRIPV GYNAIEGGSI
RTPEPLEAIA YNKPIQPSEV LQAKVLDLAN HTTSIHIWPW HEASTEFAYE DAYSVTIRNK
RYTAEVKEFE LLGLGQRRER VRILKPTVAH AIIQMWYSWF VEDDRTLAAA RRTSRDDAEK
LAIDGRRMQN AVTLLRKIEM IGTTGIGASA VHLAQSRIVD QMAGRGLIDD SSDLHVGINR
HRIRIWAGLA VLQMMGLLSR SEAEALTKVL GDSNALGMVV ATTDIDPSL
