Pol polyprotein - Equine infectious anemia virus (isolate 1369) (EIAV)

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P11204 (POL_EIAV9) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 108. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Pol polyprotein

Cleaved into the following 3 chains:

Protease
Alternative name(s):
Retropepsin
EC=3.4.23.-
Reverse transcriptase/ribonuclease H
Short name=RT
EC=2.7.7.49
EC=3.1.26.13
Alternative name(s):
Exoribonuclease H
EC=3.1.13.2
Integrase
Short name=IN

Gene names

Name:

pol

Organism

Equine infectious anemia virus (isolate 1369) (EIAV)

Taxonomic identifier

11670 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Lentivirus › Equine lentivirus group

Virus host

Equus asinus (Donkey) [TaxID: 9793]
Equus caballus (Horse) [TaxID: 9796]

Protein attributes

Sequence length	1146 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase.
Catalytic activity	Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus. 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Post-translational modification	Specific enzymatic cleavages in vivo yield mature proteins.
Sequence similarities	Belongs to the retroviral Pol polyprotein family. Contains 1 integrase catalytic domain. Contains 1 integrase-type DNA-binding domain. Contains 1 integrase-type zinc finger. Contains 1 peptidase A2 domain. Contains 1 reverse transcriptase domain. Contains 1 RNase H domain.
Sequence caution	The sequence AAB59862.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	DNA integration DNA recombination Initiation of viral infection Viral genome integration
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Aspartyl protease Endonuclease Hydrolase Nuclease Nucleotidyltransferase Protease RNA-directed DNA polymerase Transferase
PTM	Cleavage on pair of basic residues
Technical term	3D-structure Multifunctional enzyme
Gene Ontology (GO)
Biological process	DNA integration Inferred from electronic annotation. Source: UniProtKB-KW DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW RNA-dependent DNA replication Inferred from electronic annotation. Source: InterPro dUTP metabolic process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: InterPro RNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW exoribonuclease H activity Inferred from electronic annotation. Source: EC ribonuclease H activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 195

195

Protease

PRO_0000038838

Chain

196 – 914

719

Reverse transcriptase/ribonuclease H

PRO_0000038839

Chain

915 – 1146

232

Integrase

PRO_0000038840

Regions

Domain

100 – 174

Peptidase A2

Domain

230 – 419

190

Reverse transcriptase

Domain

617 – 740

124

RNase H

Domain

921 – 1078

158

Integrase catalytic

Zinc finger

878 – 919

Integrase-type

DNA binding

1096 – 1144

Integrase-type

Sites

Active site

105

By similarity

Secondary structure

1146

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P11204 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 2BEB2E04F93FA36F
Show »

FASTA

1,146

129,510

        10         20         30         40         50         60 
TAWTFLKAMQ KCSKKREARG SREAPETNFP DTTEESAQQI CCTRDSSDSK SVPRSERNKK 

        70         80         90        100        110        120 
GIQCQGEGSS RGSQPGQFVG VTYNLEKRPT TIVLINDTPL NVLLDTGADT SVLTTAHYNR 

       130        140        150        160        170        180 
LKYRGRKYQG TGIIGVGGNV ETFSTPVTIK KKGRHIKTRM LVADIPVTIL GRDILQDLGA 

       190        200        210        220        230        240 
KLVLAQLSKE IKFRKIELKE GTMGPKIPQW PLTKEKLEGA KEIVQRLLSE GKISEASDNN 

       250        260        270        280        290        300 
PYNSPIFVIK KRSGKWRLLQ DLRELNKTVQ VGTEISRGLP HPGGLIKCKH MTVLDIGDAY 

       310        320        330        340        350        360 
FTIPLDPEFR PYTAFTIPSI NHQEPDKRYV WNCLPQGFVL SPYIYQKTLQ EILQPFRERY 

       370        380        390        400        410        420 
PEVQLYQYMD DLFVGSNGSK KQHKELIIEL RAILLEEGFE TPDDKLQEVP PYSWLGYQLC 

       430        440        450        460        470        480 
PENWKVQKMQ LDMVKNPTLN DVQKLMGNIT WMSSGVPGLT VKHIAATTKG CLELNQKVIW 

       490        500        510        520        530        540 
TEEAQKELEE NNEKIKNAQG LQYYNPEEEM LCEVEITKNY EATYVIKQSQ GILWAGKKIM 

       550        560        570        580        590        600 
KANKGWSTVK NLMLLLQHVA TESITRVGKC PTFKVPFTKE QVMWEMQKGW YYSWLPEIVY 

       610        620        630        640        650        660 
THQVVHDDWR MKLVEEPTSG ITIYTDGGKQ NGEGIAAYVT SNGRTKQKRL GPVTHQVAER 

       670        680        690        700        710        720 
MAIQMALEDT RDKQVNIVTD SYYCWKNITE GLGLEGPQSP WWPIIQNIRE KEIVYFAWVP 

       730        740        750        760        770        780 
GHKGICGNQL ADEAAKIKEE IMLAYQGTQI KEKRDEDAGF DLCVPYDIMI PVSDTKIIPT 

       790        800        810        820        830        840 
DVKIQVPPNS FGWVTGKSSM AKQGLLINGG IIDEGYTGEI QVICTNIGKS NIKLIEGQKF 

       850        860        870        880        890        900 
AQLIILQHHS NSRQPWDENK ISQRGDKGFG STGVFWVENI QEAQDEHENW HTSPKILARN 

       910        920        930        940        950        960 
YKIPLTVAKQ ITQECPHCTK QGSGPAGCVM RSPNHWQADC THLDNKIILT FVESNSGYIH 

       970        980        990       1000       1010       1020 
ATLLSKENAL CTSLAILEWA RLFSPKSLHT DNGTNFVAEP VVNLLKFLKI AHTTGIPYHP 

      1030       1040       1050       1060       1070       1080 
ESQGIVERAN RTLKEKIQSH RDNTQTLEAA LQLALITCNK GRESMGGQTP WEVFITNQAQ 

      1090       1100       1110       1120       1130       1140 
VIHEKLLLQQ AQSSKKFCFY KIPGEHDWKG PTRVLWKGDG AVVVNDEGKG IIAVPLTRTK 


LLIKPN

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References

[1]	"Nucleotide sequence analysis of equine infectious anemia virus proviral DNA." Kawakami T., Sherman L., Dahlberg J., Gazit A., Yaniv A., Tronick S.R., Aaronson S.A. Virology 158:300-312(1987) [PubMed: 3035786] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M16575 Genomic RNA. Translation: AAB59862.1. Different initiation.

PIR

GNLJEW. B27842.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DUC	X-ray	2.05	A	742-875	[»]
1DUN	X-ray	1.90	A	742-875	[»]

ProteinModelPortal

P11204.

SMR

P11204. Positions 81-184, 742-861.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR008180. dUTP_pyroPase.
IPR001037. Integrase_C_retrovir.
IPR001584. Integrase_cat-core.
IPR017856. Integrase_Zn-bd_dom-like_N.
IPR003308. Integrase_Zn-bd_dom_N.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RVT.
IPR010659. RVT_connect.
IPR010661. RVT_thumb.
[Graphical view]

Gene3D

G3DSA:2.30.30.10. Integrase_C. 1 hit.
G3DSA:1.10.10.200. Intgrase_N_Zn_bd. 1 hit.
G3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.

Pfam

PF00692. dUTPase. 1 hit.
PF00552. IN_DBD_C. 1 hit.
PF02022. Integrase_Zn. 1 hit.
PF00075. RNase_H. 1 hit.
PF00665. rve. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
PF06815. RVT_connect. 1 hit.
PF06817. RVT_thumb. 1 hit.
[Graphical view]

SUPFAM

SSF50122. Integrase_C. 1 hit.
SSF46919. Integrase_Zn_N. 1 hit.
SSF50630. Pept_Aspartic. 1 hit.
SSF53098. RNaseH_fold. 2 hits.

PROSITE

PS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50994. INTEGRASE. 1 hit.
PS51027. INTEGRASE_DBD. 1 hit.
PS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
PS50876. ZF_INTEGRASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

POL_EIAV9

Accession

Primary (citable) accession number: P11204

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	December 14, 2011
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 3 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents