P03315

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
Semliki forest virus (SFV)
KEGG Pathway
vg:922351
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)

266-267 (C-terminal residues of capsid protease) SS

Target domain

119-267 (Peptidase S3)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

9 structures for P03315

Entry ID Method Resolution Chain Position Source
1DYL EM 900 A A/B/C/D 119-267 PDB
1I9W X-ray 300 A A 816-1205 PDB
1RER X-ray 320 A A/B/C 816-1206 PDB
1VCP X-ray 300 A A/B/C 119-267 PDB
1VCQ X-ray 310 A A/B 119-267 PDB
2ALA X-ray 300 A A 816-1206 PDB
2V33 X-ray 155 A A/B 1107-1197 PDB
8D87 EM 320 A A/B/C 816-1206 PDB
8IHP EM 300 A PDB

21 variants for P03315

Variant ID(s) Position Change Description Diseaes Association Provenance
62 A>T strain: A7 [UniProt] No
63 R>G strain: L10 [UniProt] No
85 N>K strain: A7, L10 and MTV [UniProt] No
279 A>T strain: A7 [UniProt] No
291 V>A strain: A7 [UniProt] No
370 V>I strain: A7, L10 and MTV [UniProt] No
437 K>T strain: A7, L10 and MTV [UniProt] No
545 N>S strain: A7 [UniProt] No
548 M>K strain: A7 and MTV [UniProt] No
614 E>K strain: MTV [UniProt] No
700 V>A strain: A7 [UniProt] No
704 V>A strain: A7 [UniProt] No
722 V>A strain: A7 and MTV [UniProt] No
880 A>S strain: A7 [UniProt] No
930 R>K strain: A7 [UniProt] No
1043 M>T strain: A7 and MTV [UniProt] No
1112 I>T strain: A7 and MTV [UniProt] No
1134 T>K strain: A7 [UniProt] No
1138 N>D strain: A7, L10 and MTV [UniProt] No
1165 G>R strain: MTV [UniProt] No
1188 R>K strain: A7 and MTV [UniProt] No

No associated diseases with P03315

3 regional properties for P03315

Type Name Position InterPro Accession
domain Peptidase S3, togavirin 110 - 268 IPR000930
domain Alphavirus E3 spike glycoprotein 275 - 333 IPR002533
domain Alphavirus E1 glycoprotein 751 - 1253 IPR002548

Functions

Description
EC Number 3.4.21.90 Serine endopeptidases
Subcellular Localization
  • [Capsid protein]: Virion
  • Host cytoplasm
  • Host cell membrane
  • Host nucleus
  • Shuttles between the cytoplasm and the 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 endosome A membrane-bounded organelle that carries materials newly ingested by endocytosis. It passes many of the materials to host cell lysosomes for degradation.
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.

4 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).
small molecule binding Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.
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 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 assembly A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed.
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
MNYIPTQTFY GRRWRPRPAA RPWPLQATPV APVVPDFQAQ QMQQLISAVN ALTMRQNAIA
70 80 90 100 110 120
PARPPKPKKK KTTKPKPKTQ PKKINGKTQQ QKKKDKQADK KKKKPGKRER MCMKIENDCI
130 140 150 160 170 180
FEVKHEGKVT GYACLVGDKV MKPAHVKGVI DNADLAKLAF KKSSKYDLEC AQIPVHMRSD
190 200 210 220 230 240
ASKYTHEKPE GHYNWHHGAV QYSGGRFTIP TGAGKPGDSG RPIFDNKGRV VAIVLGGANE
250 260 270 280 290 300
GSRTALSVVT WNKDMVTRVT PEGSEEWSAP LITAMCVLAN ATFPCFQPPC VPCCYENNAE
310 320 330 340 350 360
ATLRMLEDNV DRPGYYDLLQ AALTCRNGTR HRRSVSQHFN VYKATRPYIA YCADCGAGHS
370 380 390 400 410 420
CHSPVAIEAV RSEATDGMLK IQFSAQIGID KSDNHDYTKI RYADGHAIEN AVRSSLKVAT
430 440 450 460 470 480
SGDCFVHGTM GHFILAKCPP GEFLQVSIQD TRNAVRACRI QYHHDPQPVG REKFTIRPHY
490 500 510 520 530 540
GKEIPCTTYQ QTTAETVEEI DMHMPPDTPD RTLLSQQSGN VKITVGGKKV KYNCTCGTGN
550 560 570 580 590 600
VGTTNSDMTI NTCLIEQCHV SVTDHKKWQF NSPFVPRADE PARKGKVHIP FPLDNITCRV
610 620 630 640 650 660
PMAREPTVIH GKREVTLHLH PDHPTLFSYR TLGEDPQYHE EWVTAAVERT IPVPVDGMEY
670 680 690 700 710 720
HWGNNDPVRL WSQLTTEGKP HGWPHQIVQY YYGLYPAATV SAVVGMSLLA LISIFASCYM
730 740 750 760 770 780
LVAARSKCLT PYALTPGAAV PWTLGILCCA PRAHAASVAE TMAYLWDQNQ ALFWLEFAAP
790 800 810 820 830 840
VACILIITYC LRNVLCCCKS LSFLVLLSLG ATARAYEHST VMPNVVGFPY KAHIERPGYS
850 860 870 880 890 900
PLTLQMQVVE TSLEPTLNLE YITCEYKTVV PSPYVKCCGA SECSTKEKPD YQCKVYTGVY
910 920 930 940 950 960
PFMWGGAYCF CDSENTQLSE AYVDRSDVCR HDHASAYKAH TASLKAKVRV MYGNVNQTVD
970 980 990 1000 1010 1020
VYVNGDHAVT IGGTQFIFGP LSSAWTPFDN KIVVYKDEVF NQDFPPYGSG QPGRFGDIQS
1030 1040 1050 1060 1070 1080
RTVESNDLYA NTALKLARPS PGMVHVPYTQ TPSGFKYWLK EKGTALNTKA PFGCQIKTNP
1090 1100 1110 1120 1130 1140
VRAMNCAVGN IPVSMNLPDS AFTRIVEAPT IIDLTCTVAT CTHSSDFGGV LTLTYKTNKN
1150 1160 1170 1180 1190 1200
GDCSVHSHSN VATLQEATAK VKTAGKVTLH FSTASASPSF VVSLCSARAT CSASCEPPKD
1210 1220 1230 1240 1250
HIVPYAASHS NVVFPDMSGT ALSWVQKISG GLGAFAIGAI LVLVVVTCIG LRR