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Protein

Endogenous retrovirus group K member 9 Pol protein

Gene

ERVK-9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

The products of the Gag polyproteins of infectious retroviruses perform highly complex orchestrated tasks during the assembly, budding, maturation, and infection stages of the viral replication cycle. During viral assembly, the proteins form membrane associations and self-associations that ultimately result in budding of an immature virion from the infected cell. Gag precursors also function during viral assembly to selectively bind and package two plus strands of genomic RNA. Endogenous Gag proteins may have kept, lost or modified their original function during evolution (By similarity).By similarity
Early post-infection, the reverse transcriptase converts the viral RNA genome into double-stranded viral DNA. The RNase H domain of the reverse transcriptase performs two functions. It degrades the RNA template and specifically removes the RNA primer from the RNA/DNA hybrid. Following nuclear import, the integrase catalyzes the insertion of the linear, double-stranded viral DNA into the host cell chromosome. Endogenous Pol proteins may have kept, lost or modified their original function during evolution (By similarity).By similarity

Catalytic activityi

Processing at the authentic HIV-1 PR recognition site and release of the mature p17 matrix and the p24 capsid protein, as a result of the cleavage of the -SQNY-|-PIVQ-cleavage site.
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).PROSITE-ProRule annotation
Endonucleolytic cleavage to 5'-phosphomonoester.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei805 – 8051PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri544 – 56118CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri580 – 59718CCHC-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Protease, RNA-directed DNA polymerase, Transferase

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Endogenous retrovirus group K member 9 Pol protein
Alternative name(s):
HERV-K(C6) Gag-Pol protein
HERV-K109 Gag-Pol protein
HERV-K_6q14.1 provirus ancestral Gag-Pol polyprotein
Including the following 2 domains:
Protease (EC:3.4.23.50)
Alternative name(s):
PR
Retropepsin
Reverse transcriptase/ribonuclease H (EC:2.7.7.49, EC:2.7.7.7, EC:3.1.26.4)
Alternative name(s):
p66 RT
Gene namesi
Name:ERVK-9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:39005. ERVK-9.

Subcellular locationi

  • Cell membrane

  • Note: Cytoplasmic membrane (in a transfection system).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Polymorphism and mutation databases

DMDMi118572691.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedSequence analysis
Chaini2 – 11171116Endogenous retrovirus group K member 9 Pol proteinPRO_0000186764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineSequence analysis

Post-translational modificationi

Myristoylation is essential for retroviral assembly. Alteration of the glycine residue leads to a block in the budding of particles and an accumulation of Gag inside the cell (By similarity).By similarity
Specific enzymatic cleavages may yield mature proteins.Curated

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

PRIDEiP63128.

Structurei

3D structure databases

ProteinModelPortaliP63128.
SMRiP63128. Positions 578-606.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 195138Reverse transcriptasePROSITE-ProRule annotationAdd
BLAST
Domaini800 – 87576Peptidase A2PROSITE-ProRule annotationAdd
BLAST
Domaini890 – 93647G-patchPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi168 – 25790Pro-richAdd
BLAST
Compositional biasi611 – 66656Gln-richAdd
BLAST

Domaini

The LPQG motifs are catalytically important and conserved among many retroviruses.
HERV-K Gag polyprotein contains regions homologous to the matrix (MA), capsid (CA) and nucleocapsid (NC) proteins from infectious retroviruses. Evidence suggests that HERV-K(HML-2) Gag polyprotein can be cleaved into mature MA, CA and NC under certain circumstances. However, the exact boundaries as well as the size of processed Gag proteins have not been precisely determined yet.

Sequence similaritiesi

Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation
Contains 1 G-patch domain.PROSITE-ProRule annotation
Contains 1 peptidase A2 domain.PROSITE-ProRule annotation
Contains 1 reverse transcriptase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri544 – 56118CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri580 – 59718CCHC-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

HOVERGENiHBG082155.
PhylomeDBiP63128.

Family and domain databases

Gene3Di1.10.1200.30. 1 hit.
1.10.375.10. 1 hit.
2.40.70.10. 1 hit.
2.70.40.10. 1 hit.
4.10.60.10. 1 hit.
InterProiIPR001969. Aspartic_peptidase_AS.
IPR003322. B_retro_matrix.
IPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR000467. G_patch_dom.
IPR000721. Gag_p24.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR018061. Retropepsins.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
IPR000477. RT_dom.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00692. dUTPase. 1 hit.
PF01585. G-patch. 1 hit.
PF02337. Gag_p10. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
ProDomiPD004265. B_retro_matrix_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00443. G_patch. 1 hit.
SM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF51283. SSF51283. 1 hit.
SSF57756. SSF57756. 2 hits.
PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50174. G_PATCH. 1 hit.
PS50878. RT_POL. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[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: This protein is synthesized as Gag-Pro and Gag-Pro-Pol polyprotein precursors. These polyproteins are thought, by similarity with type-B retroviruses, to be generated by -1 frameshifts occurring at the Gag-Pro and Pro-Pol genes boundaries.

Isoform 1 (identifier: P63128-1) [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
MGQTKSKIKS KYASYLSFIK ILLKRGGVKV STKNLIKLFQ IIEQFCPWFP
60 70 80 90 100
EQGTLDLKDW KRIGKELKQA GRKGNIIPLT VWNDWAIIKA ALEPFQTEED
110 120 130 140 150
SISVSDAPGS GIIDCNEKTR KKSQKETESL HCEYVAEPVM AQSTQNVDYN
160 170 180 190 200
QLQEVIYPET LKLEGKGPEL VGPSESKPRG TSPLPAGQVP VTLQPQKQVK
210 220 230 240 250
ENKTQPPVAY QYWPPAELQY RPPPESQYGY PGMPPAPQGR APYPQPPTRR
260 270 280 290 300
LNPTAPPSRQ GSELHEIIDK SRKEGDTEAW QFPVTLEPMP PGEGAQEGEP
310 320 330 340 350
PTVEARYKSF SIKILKDMKE GVKQYGPNSP YMRTLLDSIA HGHRLIPYDW
360 370 380 390 400
EILAKSSLSP SQFLQFKTWW IDGVQEQVRR NRAANPPVNI DADQLLGIGQ
410 420 430 440 450
NWSTISQQAL MQNEAIEQVR AICLRAWEKI QDPGSTCPSF NTVRQGSKEP
460 470 480 490 500
YPDFVARLQD VAQKSIADEK ARKVIVELMA YENANPECQS AIKPLKGKVP
510 520 530 540 550
AGSDVISEYV KACDGIGGAM HKAMLMAQAI TGVVLGGQVR TFGGKCYNCG
560 570 580 590 600
QIGHLKKNCP VLNKQNITIQ ATTTGREPPD LCPRCKKGKH WASQCRSKFD
610 620 630 640 650
KNGQPLSGNE QRGQPQAPQQ TGAFPIQPFV PQGFQGQQPP LSQVFQGISQ
660 670 680 690 700
LPQYNNCPPP QVAVQQVDLC TIQAVSLLPG EPPQKIPTGV YGPLPEGTVG
710 720 730 740 750
LILGRSSLNL KGVQIHTSVV DSDYKGEIQL VISSSVPWSA SPGDRIAQLL
760 770 780 790 800
LLPYIKGGNS EIKRIGGLGS TDPTGKAAYW ASQVSENRPV CKAIIQGKQF
810 820 830 840 850
EGLVDTGADV SIIALNQWPK NWPKQKAVTG LVGIGTASEV YQSMEILHCL
860 870 880 890 900
GPDNQESTVQ PMITSIPLNL WGRDLLQQWG AEITMPAPLY SPTSQKIMTK
910 920 930 940 950
RGYIPGKGLG KNEDGIKIPF EAKINQKREG IGYPFLGAAT IEPPKPIPLT
960 970 980 990 1000
WKTEKPVWVN QWPLPKQKLE ALHLLANEQL EKGHIEPSFS PWNSPVFVIQ
1010 1020 1030 1040 1050
KKSGKWRMLT DLRAVNAVIQ PMGPLQPGLP SPAMIPKDWP LIIIDLKDCF
1060 1070 1080 1090 1100
FTIPLAEQDC EKFAFTIPAI NNKEPATRFQ WKVLPQGMLN SPTICQTFVG
1110
RALQPVKVFR LLYYSLY
Length:1,117
Mass (Da):123,620
Last modified:January 23, 2007 - v3
Checksum:iF7614F482B4117DD
GO
Isoform 2 (identifier: P63126-1) [UniParc]FASTAAdd to basket

The sequence of this isoform can be found in the external entry P63126.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Gag-Pro polyprotein is produced from conventional translation of the gag ORF.
Length:666
Mass (Da):74,005
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF164615 Genomic DNA. Translation: AAD51799.1. Sequence problems.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF164615 Genomic DNA. Translation: AAD51799.1. Sequence problems.

3D structure databases

ProteinModelPortaliP63128.
SMRiP63128. Positions 578-606.
ModBaseiSearch...
MobiDBiSearch...

Polymorphism and mutation databases

DMDMi118572691.

Proteomic databases

PRIDEiP63128.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GeneCardsiERVK-9.
HGNCiHGNC:39005. ERVK-9.
neXtProtiNX_P63128.
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG082155.
PhylomeDBiP63128.

Family and domain databases

Gene3Di1.10.1200.30. 1 hit.
1.10.375.10. 1 hit.
2.40.70.10. 1 hit.
2.70.40.10. 1 hit.
4.10.60.10. 1 hit.
InterProiIPR001969. Aspartic_peptidase_AS.
IPR003322. B_retro_matrix.
IPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR000467. G_patch_dom.
IPR000721. Gag_p24.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR018061. Retropepsins.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
IPR000477. RT_dom.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00692. dUTPase. 1 hit.
PF01585. G-patch. 1 hit.
PF02337. Gag_p10. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
ProDomiPD004265. B_retro_matrix_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00443. G_patch. 1 hit.
SM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF51283. SSF51283. 1 hit.
SSF57756. SSF57756. 2 hits.
PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50174. G_PATCH. 1 hit.
PS50878. RT_POL. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Many human endogenous retrovirus K (HERV-K) proviruses are unique to humans."
    Barbulescu M., Turner G., Seaman M.I., Deinard A.S., Kidd K.K., Lenz J.
    Curr. Biol. 9:861-868(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiPOK9_HUMAN
AccessioniPrimary (citable) accession number: P63128
Secondary accession number(s): Q9UKH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Truncated; frameshift leads to premature stop codon.Curated

Keywords - Technical termi

Complete proteome, ERV, Multifunctional enzyme, Reference proteome, Transposable element

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.