P03315
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
Autoinhibitory domains (AIDs)
Target domain |
119-267 (Peptidase S3) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
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 | Toll/interleukin-1 receptor homology (TIR) domain | 561 - 704 | IPR000157 |
domain | Sterile alpha motif domain | 410 - 477 | IPR001660-1 |
domain | Sterile alpha motif domain | 480 - 549 | IPR001660-2 |
Functions
Description | ||
---|---|---|
EC Number | 3.4.21.90 | Serine endopeptidases |
Subcellular Localization |
|
|
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 |