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Protein

Gag polyprotein

Gene

gag

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Gag polyprotein: Mediates, with Gag-Pol polyrotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi).1 Publication
Matrix protein p17: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity).By similarity
Capsid protein p24: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (PubMed:12660176). Host restriction factors such as monkey TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (PubMed:23785198). Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (PubMed:24554657).By similarity5 Publications
Nucleocapsid protein p7: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly.6 Publications
p6-gag: Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri390 – 407CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri411 – 428CCHC-type 2PROSITE-ProRule annotationAdd BLAST18

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Viral budding, Viral budding via the host ESCRT complexes, Virus exit from host cell

Keywords - Ligandi

Metal-binding, RNA-binding, Viral nucleoprotein, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-162585. Uncoating of the HIV Virion.
R-HSA-162588. Budding and maturation of HIV virion.
R-HSA-162592. Integration of provirus.
R-HSA-162594. Early Phase of HIV Life Cycle.
R-HSA-164516. Minus-strand DNA synthesis.
R-HSA-164525. Plus-strand DNA synthesis.
R-HSA-164843. 2-LTR circle formation.
R-HSA-173107. Binding and entry of HIV virion.
R-HSA-174490. Membrane binding and targetting of GAG proteins.
R-HSA-174495. Synthesis And Processing Of GAG, GAGPOL Polyproteins.
R-HSA-175474. Assembly Of The HIV Virion.
R-HSA-175567. Integration of viral DNA into host genomic DNA.
R-HSA-177539. Autointegration results in viral DNA circles.
R-HSA-180689. APOBEC3G mediated resistance to HIV-1 infection.
R-HSA-180910. Vpr-mediated nuclear import of PICs.

Names & Taxonomyi

Protein namesi
Recommended name:
Gag polyprotein
Alternative name(s):
Pr55Gag
Cleaved into the following 6 chains:
Matrix protein p17
Short name:
MA
Capsid protein p24
Short name:
CA
Spacer peptide 1By similarity
Short name:
SP1
Alternative name(s):
p2
Spacer peptide 2By similarity
Short name:
SP2
Alternative name(s):
p1
Gene namesi
Name:gag
OrganismiHuman immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Taxonomic identifieri11706 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000002241 Componenti: Genome

Subcellular locationi

Gag polyprotein :
  • Host cell membrane; Lipid-anchor
  • Host endosomehost multivesicular body By similarity

  • Note: These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cell membrane, Host cytoplasm, Host endosome, Host membrane, Host nucleus, Membrane, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi6S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication1
Mutagenesisi9S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication1
Mutagenesisi18K → A: Replication-defective, induces nuclear mislocalization of matrix protein; when associated with G-22. 1 Publication1
Mutagenesisi22R → G: Replication-defective, induces nuclear mislocalization of matrix protein; when associated with A-18. 1 Publication1
Mutagenesisi27K → A: No effect on subcellular localization of matrix protein; when associated with A-18 and G-22. 1 Publication1
Mutagenesisi67S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication1
Mutagenesisi72S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication1
Mutagenesisi217P → A: 3-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi218V → A: 2.7-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi219H → A or Q: 8-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi220A → G: 44-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi220A → V: 3.4-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi221G → A: 31-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi221G → V: 154-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi222P → A: 36-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi222P → V: More than 150-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi223I → A: 1.2-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi223I → V: 1.0-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi224A → G: 2.3-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi224A → V: 1.7-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi225P → A: 1.6-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi394N → F or G: Decreases infectivity and replication. 1 Publication1
Mutagenesisi400H → C: Complete loss of infectivity and in vitro chaperone activity. 1 Publication1
Mutagenesisi405C → H: Complete loss of infectivity and DNA synthesis. 1 Publication1
Mutagenesisi421H → C: Partial loss of infectivity. Complete loss of in vitro chaperone activity. 1 Publication1
Mutagenesisi426C → H: Partial loss of infectivity. 1 Publication1

Keywords - Diseasei

AIDS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00002612162 – 500Gag polyproteinAdd BLAST499
ChainiPRO_00000385932 – 132Matrix protein p17By similarityAdd BLAST131
ChainiPRO_0000038594133 – 363Capsid protein p24By similarityAdd BLAST231
PeptideiPRO_0000038595364 – 377Spacer peptide 1By similarityAdd BLAST14
ChainiPRO_0000038596378 – 432Nucleocapsid protein p7By similarityAdd BLAST55
PeptideiPRO_0000038597433 – 448Spacer peptide 2By similarityAdd BLAST16
ChainiPRO_0000038598449 – 500p6-gagBy similarityAdd BLAST52

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Modified residuei148Phosphoserine; by host MAPK1By similarity1
Modified residuei387Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6By similarity1
Modified residuei409Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6By similarity1

Post-translational modificationi

Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins.By similarity
Matrix protein p17: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association (PubMed:17656588).1 Publication
Capsid protein p24: Phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating.By similarity
Nucleocapsid protein p7: Methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei132 – 133Cleavage; by viral proteaseBy similarity2
Sitei363 – 364Cleavage; by viral proteaseBy similarity2
Sitei377 – 378Cleavage; by viral proteaseBy similarity2
Sitei432 – 433Cleavage; by viral proteaseBy similarity2
Sitei448 – 449Cleavage; by viral proteaseBy similarity2

Keywords - PTMi

Lipoprotein, Methylation, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Gag polyprotein: Homotrimer; further assembles as hexamers of trimers (By similarity). Oligomerization possibly creates a central hole into which the cytoplasmic tail of the gp41 envelope protein may be inserted.Gag polyprotein: Interacts with host TRIM22; this interaction seems to disrupt proper trafficking of Gag polyprotein and may interfere with budding (PubMed:18389079). Gag polyprotein: Interacts with host PDZD8 (By similarity). Matrix protein p17: Homotrimer; further assembles as hexamers of trimers (PubMed:19327811). Matrix protein p17: Interacts with gp41 (via C-terminus) (By similarity). Matrix protein p17: Interacts with host CALM1; this interaction induces a conformational change in the Matrix protein, triggering exposure of the myristate group (PubMed:24500712). Matrix protein p17: Interacts with host AP3D1; this interaction allows the polyprotein trafficking to multivesicular bodies during virus assembly (By similarity). Matrix protein p17: Part of the pre-integration complex (PIC) which is composed of viral genome, matrix protein, Vpr and integrase (By similarity). Capsid protein p24: Homodimer; the homodimer further multimerizes as homohexamers or homopentamers (PubMed:19914170). Capsid protein p24: Interacts with human PPIA/CYPA;this interaction stabilizes the capsid (PubMed:9223641). Capsid protein p24: Interacts with human NUP153 (By similarity). Capsid protein p24: Interacts with host PDZD8; this interaction stabilizes the capsid (PubMed:20573829). Capsid protein p24: Interacts with monkey TRIM5; this interaction destabilizes the capsid (PubMed:23785198). p6-gag interacts with Vpr; this interaction allows Vpr incorporation into the virion (By similarity). p6-gag interacts with host TSG101 (By similarity). p6-gag interacts with host PDCD6IP/AIP1 (By similarity).By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AIMP1Q129043EBI-6179719,EBI-1045802From a different organism.
AIMP2Q131553EBI-6179719,EBI-745226From a different organism.
Cct3P803183EBI-10634977,EBI-772361From a different organism.
CTNNA3Q9UI472EBI-6179727,EBI-3937546From a different organism.
EEF1E1O433244EBI-6179719,EBI-1048486From a different organism.
LRRC47Q8N1G42EBI-6179727,EBI-2509921From a different organism.
MRPL11Q9Y3B73EBI-6179727,EBI-5453723From a different organism.
NOLC1Q149782EBI-6179719,EBI-396155From a different organism.
OLA1Q9NTK54EBI-6179719,EBI-766468From a different organism.
PRMT1Q998732EBI-6179727,EBI-78738From a different organism.
SDCCAG8Q86SQ72EBI-6179719,EBI-1047850From a different organism.
SEPSECSQ9HD403EBI-6163428,EBI-6163446From a different organism.
SNU13P557692EBI-6179727,EBI-712228From a different organism.
STAU1O95793-24EBI-6163428,EBI-358189From a different organism.
YTHDF3Q7Z7392EBI-6179727,EBI-2849837From a different organism.

Protein-protein interaction databases

BioGridi1205537. 185 interactors.
IntActiP04591. 46 interactors.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TSQX-ray2.00P429-438[»]
1TSUX-ray2.10P429-436[»]
5FJBelectron microscopy9.00A/B133-350[»]
5I1ROther-A378-432[»]
ProteinModelPortaliP04591.
SMRiP04591.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04591.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni7 – 31Interaction with Gp41By similarityAdd BLAST25
Regioni8 – 43Interaction with host CALM11 PublicationAdd BLAST36
Regioni12 – 19Interaction with host AP3D1By similarity8
Regioni14 – 33Interaction with membrane phosphatidylinositol 4,5-bisphosphate and RNABy similarityAdd BLAST20
Regioni73 – 77Interaction with membrane phosphatidylinositol 4,5-bisphosphateBy similarity5
Regioni189 – 227Interaction with host PPIA/CYPA and NUP153By similarityAdd BLAST39
Regioni217 – 225PPIA/CYPA-binding loop9
Regioni277 – 363Dimerization/Multimerization of capsid protein p24Add BLAST87

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi16 – 22Nuclear export signal7
Motifi26 – 32Nuclear localization signal7
Motifi455 – 458PTAP/PSAP motif4
Motifi483 – 492LYPX(n)L motif10

Domaini

Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. p6-gag contains two L domains: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101 and a LYPX(n)L motif which interacts with PDCD6IP/AIP1.By similarity

Sequence similaritiesi

Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri390 – 407CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri411 – 428CCHC-type 2PROSITE-ProRule annotationAdd BLAST18

Keywords - Domaini

Repeat, Zinc-finger

Family and domain databases

Gene3Di1.10.1200.30. 1 hit.
1.10.150.90. 1 hit.
1.10.375.10. 1 hit.
4.10.60.10. 1 hit.
InterProiIPR000721. Gag_p24.
IPR014817. Gag_p6.
IPR000071. Lentvrl_matrix_N.
IPR012344. Matrix_HIV/RSV.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00540. Gag_p17. 1 hit.
PF00607. Gag_p24. 1 hit.
PF08705. Gag_p6. 1 hit.
PF00098. zf-CCHC. 2 hits.
[Graphical view]
PRINTSiPR00234. HIV1MATRIX.
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50158. ZF_CCHC. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by ribosomal frameshifting. AlignAdd to basket

Note: Translation results in the formation of the Gag polyprotein most of the time. Ribosomal frameshifting at the gag-pol genes boundary occurs at low frequency and produces the Gag-Pol polyprotein. This strategy of translation probably allows the virus to modulate the quantity of each viral protein. Maintenance of a correct Gag to Gag-Pol ratio is essential for RNA dimerization and viral infectivity.
Isoform Gag polyprotein (identifier: P04591-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGARASVLSG GELDRWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPGL
60 70 80 90 100
LETSEGCRQI LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIEIKDTKEA
110 120 130 140 150
LDKIEEEQNK SKKKAQQAAA DTGHSNQVSQ NYPIVQNIQG QMVHQAISPR
160 170 180 190 200
TLNAWVKVVE EKAFSPEVIP MFSALSEGAT PQDLNTMLNT VGGHQAAMQM
210 220 230 240 250
LKETINEEAA EWDRVHPVHA GPIAPGQMRE PRGSDIAGTT STLQEQIGWM
260 270 280 290 300
TNNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF
310 320 330 340 350
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPA ATLEEMMTAC
360 370 380 390 400
QGVGGPGHKA RVLAEAMSQV TNSATIMMQR GNFRNQRKIV KCFNCGKEGH
410 420 430 440 450
TARNCRAPRK KGCWKCGKEG HQMKDCTERQ ANFLGKIWPS YKGRPGNFLQ
460 470 480 490 500
SRPEPTAPPE ESFRSGVETT TPPQKQEPID KELYPLTSLR SLFGNDPSSQ
Note: Produced by conventional translation.
Length:500
Mass (Da):55,930
Last modified:January 23, 2007 - v3
Checksum:iB74C3858C20EF82C
GO
Isoform Gag-Pol polyprotein (identifier: P04585-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P04585.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by -1 ribosomal frameshifting.
Length:1,435
Mass (Da):162,042
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03455 Genomic RNA. Translation: AAB50258.1.
RefSeqiNP_057850.1. NC_001802.1.

Genome annotation databases

GeneIDi155030.
KEGGivg:155030.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Web resourcesi

BioAfrica HIV proteomics resource

Gag entry

BioAfrica HIV proteomics resource

MA (p17) entry

BioAfrica HIV proteomics resource

CA (p24) entry

BioAfrica HIV proteomics resource

p2 entry

BioAfrica HIV proteomics resource

NC (p7) entry

BioAfrica HIV proteomics resource

p1 entry

BioAfrica HIV proteomics resource

p6 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03455 Genomic RNA. Translation: AAB50258.1.
RefSeqiNP_057850.1. NC_001802.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TSQX-ray2.00P429-438[»]
1TSUX-ray2.10P429-436[»]
5FJBelectron microscopy9.00A/B133-350[»]
5I1ROther-A378-432[»]
ProteinModelPortaliP04591.
SMRiP04591.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1205537. 185 interactors.
IntActiP04591. 46 interactors.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi155030.
KEGGivg:155030.

Enzyme and pathway databases

ReactomeiR-HSA-162585. Uncoating of the HIV Virion.
R-HSA-162588. Budding and maturation of HIV virion.
R-HSA-162592. Integration of provirus.
R-HSA-162594. Early Phase of HIV Life Cycle.
R-HSA-164516. Minus-strand DNA synthesis.
R-HSA-164525. Plus-strand DNA synthesis.
R-HSA-164843. 2-LTR circle formation.
R-HSA-173107. Binding and entry of HIV virion.
R-HSA-174490. Membrane binding and targetting of GAG proteins.
R-HSA-174495. Synthesis And Processing Of GAG, GAGPOL Polyproteins.
R-HSA-175474. Assembly Of The HIV Virion.
R-HSA-175567. Integration of viral DNA into host genomic DNA.
R-HSA-177539. Autointegration results in viral DNA circles.
R-HSA-180689. APOBEC3G mediated resistance to HIV-1 infection.
R-HSA-180910. Vpr-mediated nuclear import of PICs.

Miscellaneous databases

EvolutionaryTraceiP04591.

Family and domain databases

Gene3Di1.10.1200.30. 1 hit.
1.10.150.90. 1 hit.
1.10.375.10. 1 hit.
4.10.60.10. 1 hit.
InterProiIPR000721. Gag_p24.
IPR014817. Gag_p6.
IPR000071. Lentvrl_matrix_N.
IPR012344. Matrix_HIV/RSV.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00540. Gag_p17. 1 hit.
PF00607. Gag_p24. 1 hit.
PF08705. Gag_p6. 1 hit.
PF00098. zf-CCHC. 2 hits.
[Graphical view]
PRINTSiPR00234. HIV1MATRIX.
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50158. ZF_CCHC. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGAG_HV1H2
AccessioniPrimary (citable) accession number: P04591
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

HIV-1 lineages are divided in three main groups, M (for Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast majority of strains found worldwide belong to the group M. Group O seems to be endemic to and largely confined to Cameroon and neighboring countries in West Central Africa, where these viruses represent a small minority of HIV-1 strains. The group N is represented by a limited number of isolates from Cameroonian persons. The group M is further subdivided in 9 clades or subtypes (A to D, F to H, J and K).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.