P05674

SS
Gene name
Protein name
Structural polyprotein
Names
p130 [Cleaved into: Capsid protein , EC 3.4.21.90 , Coat protein , C; Precursor of protein E3/E2 , p62 , pE2; Assembly protein E3; Spike glycoprotein E2 , E2 envelope glycoprotein; 6K protein; Spike glycoprotein E1 , E1 envelope glycoprotein]
Species
Venezuelan equine encephalitis virus (strain TC-83) (VEEV)
KEGG Pathway
EC number
3.4.21.90: Serine endopeptidases
Protein Class

Descriptions

This structural polyprotein forms an icosahedral capsid that binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release. Autoinhibition of the suicidal capsid protease (CP) involves the C-terminal tryptophan localizing to the active pocket, effectively deactivating the enzyme. This results in the lack of enzymatic activity, crucial for halting the viral replication cycle as the virus cannot produce infectious progeny.

Autoinhibitory domains (AIDs)

274-275 (C-terminal residues of capsid protease) SS

Target domain

126-275 (Peptidase S3)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

11 structures for P05674

Entry ID Method Resolution Chain Position Source
1EP5 X-ray 230 A A/B/C 119-275 PDB
1EP6 X-ray 245 A A/B/C 119-275 PDB
3J0C EM - PDB
3J0G EM - M/N/O/P 276-334 PDB
7SFU EM 420 A PDB
7SFV EM 400 A PDB
7SFW EM 320 A PDB
8DEQ EM 600 A A/B/C/D/E/F 813-1214 PDB
8DER EM 330 A PDB
8EEU EM 350 A A/B/C/D/E/F 1-1254 PDB
8EEV EM 360 A A/B/F/G/J/K 1-1254 PDB

No variants for P05674

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P05674

2 associated diseases with P05674

[MIM: 303600]: Coffin-Lowry syndrome (CLS)

An X-linked disorder characterized by intellectual disability associated with facial and digital dysmorphisms, progressive skeletal malformations, growth retardation, hearing deficit and paroxysmal movement disorders. {ECO:0000269|PubMed:10094187, ECO:0000269|PubMed:10528858, ECO:0000269|PubMed:14986828, ECO:0000269|PubMed:15214012, ECO:0000269|PubMed:8955270, ECO:0000269|PubMed:9837815}. Note=The disease is caused by variants affecting the gene represented in this entry.

[MIM: 300844]: Intellectual developmental disorder, X-linked 19 (XLID19)

A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:10319851, ECO:0000269|PubMed:17100996}. Note=The disease is caused by variants affecting the gene represented in this entry.

Without disease ID
  • An X-linked disorder characterized by intellectual disability associated with facial and digital dysmorphisms, progressive skeletal malformations, growth retardation, hearing deficit and paroxysmal movement disorders. {ECO:0000269|PubMed:10094187, ECO:0000269|PubMed:10528858, ECO:0000269|PubMed:14986828, ECO:0000269|PubMed:15214012, ECO:0000269|PubMed:8955270, ECO:0000269|PubMed:9837815}. Note=The disease is caused by variants affecting the gene represented in this entry.
  • A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:10319851, ECO:0000269|PubMed:17100996}. Note=The disease is caused by variants affecting the gene represented in this entry.

10 regional properties for P05674

Type Name Position InterPro Accession
domain Protein kinase domain 68 - 327 IPR000719-1
domain Protein kinase domain 422 - 679 IPR000719-2
domain AGC-kinase, C-terminal 328 - 397 IPR000961
active_site Serine/threonine-protein kinase, active site 189 - 201 IPR008271-1
active_site Serine/threonine-protein kinase, active site 535 - 547 IPR008271-2
binding_site Protein kinase, ATP binding site 74 - 100 IPR017441-1
binding_site Protein kinase, ATP binding site 428 - 451 IPR017441-2
domain Protein kinase, C-terminal 351 - 387 IPR017892
domain Ribosomal protein S6 kinase alpha-3, C-terminal catalytic domain 402 - 740 IPR041905
domain Ribosomal S6 kinase, N-terminal catalytic domain 72 - 388 IPR041906

Functions

Description
EC Number 3.4.21.90 Serine endopeptidases
Subcellular Localization
  • [Capsid protein]: Virion
  • Host cytoplasm
  • Host cell membrane
  • Host nucleus
  • ;
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
host cell cytoplasm The cytoplasm of a host cell.
host cell nucleus A membrane-bounded organelle as it is found in the host cell in which chromosomes are housed and replicated. The host is defined as the larger of the organisms involved in a symbiotic interaction.
host cell plasma membrane The plasma membrane surrounding a host cell.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
T=4 icosahedral viral capsid The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with T=4 symmetry. The T=4 capsid is composed of 12 pentameric and 30 hexameric capsomeres.
viral envelope The lipid bilayer of a virion that surrounds the protein capsid. May also contain glycoproteins.
virion membrane The lipid bilayer surrounding a virion.

3 GO annotations of molecular function

Name Definition
RNA binding Binding to an RNA molecule or a portion thereof.
serine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
structural molecule activity The action of a molecule that contributes to the structural integrity of a complex.

6 GO annotations of biological process

Name Definition
clathrin-dependent endocytosis of virus by host cell Any clathrin-mediated endocytosis that is involved in the uptake of a virus into a host cell. Begins by invagination of a specific region of the host cell plasma membrane around the bound virus to form a clathrin-coated pit, which then pinches off to form a clathrin-coated endocytic vesicle containing the virus.
fusion of virus membrane with host endosome membrane Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
suppression by virus of host gene expression Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of gene expression in the host organism. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein. Some protein processing events may be included when they are required to form an active form of a product from an inactive precursor form.
suppression by virus of host toll-like receptor signaling pathway Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of toll-like receptor (TLR) signaling in the host organism.
virion attachment to host cell The process by which a virion protein binds to molecules on the host cellular surface or host cell surface projection.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MFPFQPMYPM QPMPYRNPFA APRRPWFPRT DPFLAMQVQE LTRSMANLTF KQRRDAPPEG
70 80 90 100 110 120
PSAKKPKKEA SQKQKGGGQG KKKKNQGKKK AKTGPPNPKA QNGNKKKTNK KPGKRQRMVM
130 140 150 160 170 180
KLESDKTFPI MLEGKINGYA CVVGGKLFRP MHVEGKIDND VLAALKTKKA SKYDLEYADV
190 200 210 220 230 240
PQNMRADTFK YTHEKPQGYY SWHHGAVQYE NGRFTVPKGV GAKGDSGRPI LDNQGRVVAI
250 260 270 280 290 300
VLGGVNEGSR TALSVVMWNE KGVTVKYTPE NCEQWSLVTT MCLLANVTFP CAQPPICYDR
310 320 330 340 350 360
KPAETLAMLS VNVDNPGYDE LLEAAVKCPG RKRRSTEELF NEYKLTRPYM ARCIRCAVGS
370 380 390 400 410 420
CHSPIAIEAV KSDGHDGYVR LQTSSQYGLD SSGNLKGRTM RYDMHGTIKE IPLHQVSLYT
430 440 450 460 470 480
SRPCHIVDGH GYFLLARCPA GDSITMEFKK DSVRHSCSVP YEVKFNPVGR ELYTHPPEHG
490 500 510 520 530 540
VEQACQVYAH DAQNRGAYVE MHLPGSEVDS SLVSLSGSSV TVTPPDGTSA LVECECGGTK
550 560 570 580 590 600
ISETINKTKQ FSQCTKKEQC RAYRLQNDKW VYNSDKLPKA AGATLKGKLH VPFLLADGKC
610 620 630 640 650 660
TVPLAPEPMI TFGFRSVSLK LHPKNPTYLI TRQLADEPHY THELISEPAV RNFTVTEKGW
670 680 690 700 710 720
EFVWGNHPPK RFWAQETAPG NPHGLPHEVI THYYHRYPMS TILGLSICAA IATVSVAAST
730 740 750 760 770 780
WLFCRSRVAC LTPYRLTPNA RIPFCLAVLC CARTARAETT WESLDHLWNN NQQMFWIQLL
790 800 810 820 830 840
IPLAALIVVT RLLRCVCCVV PFLVMAGAAA PAYEHATTMP SQAGISYNTI VNRAGYAPLP
850 860 870 880 890 900
ISITPTKIKL IPTVNLEYVT CHYKTGMDSP AIKCCGSQEC TPTYRPDEQC KVFTGVYPFM
910 920 930 940 950 960
WGGAYCFCDT ENTQVSKAYV MKSDDCLADH AEAYKAHTAS VQAFLNITVG EHSIVTTVYV
970 980 990 1000 1010 1020
NGETPVNFNG VKITAGPLST AWTPFDRKIV QYAGEIYNYD FPEYGAGQPG AFGDIQSRTV
1030 1040 1050 1060 1070 1080
SSSDLYANTN LVLQRPKAGA IHVPYTQAPS GFEQWKKDKA PSLKFTAPFG CEIYTNPIRA
1090 1100 1110 1120 1130 1140
ENCAVGSIPL AFDIPDALFT RVSETPTLSA AECTLNECVY SSDFGGIATV KYSASKSGKC
1150 1160 1170 1180 1190 1200
AVHVPSGTAT LKEAAVELTE QGSATIHFST ANIHPEFRLQ ICTSYVTCKG DCHPPKDHIV
1210 1220 1230 1240 1250
THPQYHAQTF TAAVSKTAWT WLTSLLGGSA VIIIIGLVLA TIVAMYVLTN QKHN