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Gag-Pol polyprotein (Pr170Gag-Pol) [Cleaved into: Matrix protein p16 (MA); p2L; Capsid protein p26 (CA); p3; Transframe peptide (p11); Protease (EC 3.4.23.-) (P119) (Retropepsin); Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (P72); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

 POL_BIV29               Reviewed;        1475 AA.
P19560; P19561; Q65593;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
30-AUG-2017, entry version 137.
RecName: Full=Gag-Pol polyprotein;
AltName: Full=Pr170Gag-Pol;
Contains:
RecName: Full=Matrix protein p16;
Short=MA;
Contains:
RecName: Full=p2L;
Contains:
RecName: Full=Capsid protein p26;
Short=CA;
Contains:
RecName: Full=p3;
Contains:
RecName: Full=Transframe peptide;
AltName: Full=p11;
Contains:
RecName: Full=Protease;
EC=3.4.23.-;
AltName: Full=P119;
AltName: Full=Retropepsin;
Contains:
RecName: Full=Reverse transcriptase/ribonuclease H;
Short=RT;
EC=2.7.7.49;
EC=2.7.7.7;
EC=3.1.26.13;
AltName: Full=Exoribonuclease H;
EC=3.1.13.2;
AltName: Full=P72;
Contains:
RecName: Full=Integrase;
Short=IN;
EC=2.7.7.- {ECO:0000250|UniProtKB:P04585};
EC=3.1.-.- {ECO:0000250|UniProtKB:P04585};
Name=gag-pol;
Bovine immunodeficiency virus (strain R29) (BIV) (Bovine
immunodeficiency-like virus).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Bovine lentivirus group.
NCBI_TaxID=417296;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate R29-106, and Isolate R29-127;
PubMed=2183467; DOI=10.1016/0042-6822(90)90424-P;
Garvey K.J., Oberste M.S., Elser J.E., Braun M.J., Gonda M.A.;
"Nucleotide sequence and genome organization of biologically active
proviruses of the bovine immunodeficiency-like virus.";
Virology 175:391-409(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Isolate R29-Nadin;
Nadin-Davis S.A., Chang S.C., Roth J.A., Carpenter S.;
"Isolation and characterization of cDNAs encoding rev and tat of
bovine immunodeficiency-like virus.";
Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
[3]
RIBOSOMAL FRAMESHIFT, AND PROTEOLYTIC PROCESSING OF POLYPROTEIN.
STRAIN=Isolate R29-127;
PubMed=1331499;
Battles J.K., Hu M.Y., Rasmussen L., Tobin G.J., Gonda M.A.;
"Immunological characterization of the gag gene products of bovine
immunodeficiency virus.";
J. Virol. 66:6868-6877(1992).
[4]
FUNCTION, AND INTERACTION WITH HOST DYNLL1.
PubMed=20148896; DOI=10.1111/j.1462-5822.2010.01453.x;
Su Y., Qiao W., Guo T., Tan J., Li Z., Chen Y., Li X., Li Y., Zhou J.,
Chen Q.;
"Microtubule-dependent retrograde transport of bovine immunodeficiency
virus.";
Cell. Microbiol. 12:1098-1107(2010).
-!- FUNCTION: Matrix protein p16 forms the outer shell of the core of
the virus, lining the inner surface of the viral membrane.
{ECO:0000250}.
-!- FUNCTION: Capsid protein p26 forms the conical core of the virus
that encapsulates the genomic RNA-nucleocapsid complex.
Interaction between incoming particle-associated Gag proteins and
host dynein allows intracellular microtubule-dependent virus
transport toward the perinuclear region, prior to nucleus
translocation and integration into host genome.
{ECO:0000269|PubMed:20148896}.
-!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of
Gag and Gag-Pol polyproteins during or shortly after the release
of the virion from the plasma membrane. Cleavages take place as an
ordered, step-wise cascade to yield mature proteins. This process
is called maturation. Displays maximal activity during the budding
process just prior to particle release from the cell.
{ECO:0000255|PROSITE-ProRule:PRU00275}.
-!- FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a
multifunctional enzyme that converts the viral RNA genome into
dsDNA in the cytoplasm, shortly after virus entry into the cell.
This enzyme displays a DNA polymerase activity that can copy
either DNA or RNA templates, and a ribonuclease H (RNase H)
activity that cleaves the RNA strand of RNA-DNA heteroduplexes in
a partially processive 3' to 5' endonucleasic mode. Conversion of
viral genomic RNA into dsDNA requires many steps. A tRNA binds to
the primer-binding site (PBS) situated at the 5'-end of the viral
RNA. RT uses the 3' end of the tRNA primer to perform a short
round of RNA-dependent minus-strand DNA synthesis. The reading
proceeds through the U5 region and ends after the repeated (R)
region which is present at both ends of viral RNA. The portion of
the RNA-DNA heteroduplex is digested by the RNase H, resulting in
a ssDNA product attached to the tRNA primer. This ssDNA/tRNA
hybridizes with the identical R region situated at the 3' end of
viral RNA. This template exchange, known as minus-strand DNA
strong stop transfer, can be either intra- or intermolecular. RT
uses the 3' end of this newly synthesized short ssDNA to perform
the RNA-dependent minus-strand DNA synthesis of the whole
template. RNase H digests the RNA template except for a polypurine
tract (PPT) situated at the 5'-end of the genome. It is not clear
if both polymerase and RNase H activities are simultaneous. RNase
H probably can proceed both in a polymerase-dependent (RNA cut
into small fragments by the same RT performing DNA synthesis) and
a polymerase-independent mode (cleavage of remaining RNA fragments
by free RTs). Secondly, RT performs DNA-directed plus-strand DNA
synthesis using the PPT that has not been removed by RNase H as
primer. PPT and tRNA primers are then removed by RNase H. The 3'
and 5' ssDNA PBS regions hybridize to form a circular dsDNA
intermediate. Strand displacement synthesis by RT to the PBS and
PPT ends produces a blunt ended, linear dsDNA copy of the viral
genome that includes long terminal repeats (LTRs) at both ends (By
similarity). {ECO:0000250}.
-!- FUNCTION: Integrase catalyzes viral DNA integration into the host
chromosome, by performing a series of DNA cutting and joining
reactions. This enzyme activity takes place after virion entry
into a cell and reverse transcription of the RNA genome in dsDNA
(By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- 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.
-!- CATALYTIC ACTIVITY: 3'-end directed exonucleolytic cleavage of
viral RNA-DNA hybrid.
-!- SUBUNIT: Interacts with host light chain cytoplasmic dynein
DYNLL1; this interaction is critical for intracellular
microtubule-dependent viral genome transport.
{ECO:0000269|PubMed:20148896}.
-!- SUBCELLULAR LOCATION: Matrix protein p16: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein p26: Virion {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Comment=This strategy of translation probably allows the virus
to modulate the quantity of each viral protein.;
Name=Gag-Pol polyprotein;
IsoId=P19560-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the gag-pol genes
boundary.;
Name=Gag polyprotein;
IsoId=P19558-1; Sequence=External;
Note=Produced by conventional translation.;
-!- PTM: Specific enzymatic cleavages by the viral protease yield
mature proteins. The protease is released by autocatalytic
cleavage. The polyprotein is cleaved during and after budding,
this process is termed maturation (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: The reverse transcriptase is an error-prone enzyme
that lacks a proof-reading function. High mutations rate is a
direct consequence of this characteristic. RT also displays
frequent template switching leading to high recombination rate.
Recombination mostly occurs between homologous regions of the two
copackaged RNA genomes. If these two RNA molecules derive from
different viral strains, reverse transcription will give rise to
highly recombinated proviral DNAs (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: The sequence shown is that of isolate R29-127.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M32690; AAA91271.1; ALT_SEQ; Genomic_RNA.
EMBL; L04972; AAA42767.1; ALT_SEQ; Genomic_DNA.
PIR; B34742; GNLJBT.
PDB; 3KKR; X-ray; 2.45 A; A=1257-1405.
PDB; 3KKS; X-ray; 2.20 A; A/B=1257-1405.
PDBsum; 3KKR; -.
PDBsum; 3KKS; -.
ProteinModelPortal; P19560; -.
SMR; P19560; -.
MEROPS; A02.005; -.
EvolutionaryTrace; P19560; -.
PRO; PR:P19560; -.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004533; F:exoribonuclease H activity; IEA:UniProtKB-EC.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-KW.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-KW.
Gene3D; 1.10.10.200; -; 1.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.30.30.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 3.30.420.10; -; 2.
Gene3D; 4.10.60.10; -; 3.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR000721; Gag_p24.
InterPro; IPR001037; Integrase_C_retrovir.
InterPro; IPR001584; Integrase_cat-core.
InterPro; IPR017856; Integrase_Zn-bd_dom-like_N.
InterPro; IPR003308; Integrase_Zn-bd_dom_N.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom.
InterPro; IPR018061; Retropepsins.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR012337; RNaseH-like_dom.
InterPro; IPR002156; RNaseH_domain.
InterPro; IPR000477; RT_dom.
InterPro; IPR010661; RVT_thumb.
InterPro; IPR001878; Znf_CCHC.
Pfam; PF00607; Gag_p24; 1.
Pfam; PF00552; IN_DBD_C; 1.
Pfam; PF02022; Integrase_Zn; 1.
Pfam; PF00075; RNase_H; 1.
Pfam; PF00665; rve; 1.
Pfam; PF00077; RVP; 1.
Pfam; PF00078; RVT_1; 1.
Pfam; PF06817; RVT_thumb; 1.
Pfam; PF00098; zf-CCHC; 2.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF46919; SSF46919; 1.
SUPFAM; SSF47353; SSF47353; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF50122; SSF50122; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF53098; SSF53098; 2.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50175; ASP_PROT_RETROV; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
PROSITE; PS50994; INTEGRASE; 1.
PROSITE; PS51027; INTEGRASE_DBD; 1.
PROSITE; PS50879; RNASE_H; 1.
PROSITE; PS50878; RT_POL; 1.
PROSITE; PS50158; ZF_CCHC; 2.
PROSITE; PS50876; ZF_INTEGRASE; 1.
1: Evidence at protein level;
3D-structure; Aspartyl protease; Capsid protein; Coiled coil;
Cytoplasmic inwards viral transport; DNA integration;
DNA recombination; DNA-binding; DNA-directed DNA polymerase;
Endonuclease; Host-virus interaction; Hydrolase; Magnesium;
Metal-binding; Microtubular inwards viral transport;
Multifunctional enzyme; Nuclease; Nucleotidyltransferase; Protease;
Repeat; Ribosomal frameshifting; RNA-binding;
RNA-directed DNA polymerase; Transferase; Viral genome integration;
Viral matrix protein; Viral nucleoprotein; Virion; Virion maturation;
Virus entry into host cell; Virus exit from host cell; Zinc;
Zinc-finger.
CHAIN 1 1475 Gag-Pol polyprotein.
/FTId=PRO_0000272324.
CHAIN 1 126 Matrix protein p16. {ECO:0000255}.
/FTId=PRO_0000272325.
PEPTIDE 127 148 p2L. {ECO:0000250}.
/FTId=PRO_0000272326.
CHAIN 149 367 Capsid protein p26. {ECO:0000255}.
/FTId=PRO_0000272327.
PEPTIDE 368 392 p3. {ECO:0000250}.
/FTId=PRO_0000272328.
CHAIN 393 472 Transframe peptide. {ECO:0000255}.
/FTId=PRO_0000272329.
CHAIN 473 562 Protease. {ECO:0000255}.
/FTId=PRO_0000038823.
CHAIN 563 1193 Reverse transcriptase/ribonuclease H.
{ECO:0000255}.
/FTId=PRO_0000038824.
CHAIN 1194 1475 Integrase. {ECO:0000255}.
/FTId=PRO_0000038825.
DOMAIN 492 565 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
DOMAIN 619 806 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
DOMAIN 999 1119 RNase H. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
DOMAIN 1248 1400 Integrase catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00457}.
ZN_FING 403 420 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 421 438 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1199 1240 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00450}.
DNA_BIND 1419 1465 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00506}.
ACT_SITE 497 497 {ECO:0000255|PROSITE-ProRule:PRU10094}.
SITE 126 127 Cleavage; by viral protease.
{ECO:0000255}.
SITE 148 149 Cleavage; by viral protease.
{ECO:0000255}.
SITE 367 368 Cleavage; by viral protease.
{ECO:0000250}.
SITE 392 393 Cleavage; by viral protease.
{ECO:0000250}.
SITE 472 473 Cleavage; by viral protease.
{ECO:0000255}.
SITE 562 563 Cleavage; by viral protease.
{ECO:0000255}.
SITE 1193 1194 Cleavage; by viral protease.
{ECO:0000255}.
VARIANT 17 17 P -> L (in strain: Isolate R29-106 and
Isolate R29-Nadin).
VARIANT 117 117 D -> E (in strain: Isolate R29-106).
VARIANT 454 454 T -> I (in strain: Isolate R29-Nadin).
VARIANT 577 577 V -> I (in strain: Isolate R29-Nadin).
VARIANT 645 645 R -> K (in strain: Isolate R29-Nadin).
VARIANT 729 729 V -> I (in strain: Isolate R29-Nadin).
VARIANT 1095 1095 V -> I (in strain: Isolate R29-Nadin).
VARIANT 1226 1226 K -> R (in strain: Isolate R29-106 and
Isolate R29-Nadin).
VARIANT 1244 1244 T -> A (in strain: Isolate R29-106 and
Isolate R29-Nadin).
STRAND 1257 1265 {ECO:0000244|PDB:3KKS}.
STRAND 1268 1275 {ECO:0000244|PDB:3KKS}.
TURN 1276 1278 {ECO:0000244|PDB:3KKS}.
STRAND 1281 1289 {ECO:0000244|PDB:3KKS}.
HELIX 1291 1304 {ECO:0000244|PDB:3KKS}.
STRAND 1308 1312 {ECO:0000244|PDB:3KKS}.
HELIX 1316 1319 {ECO:0000244|PDB:3KKS}.
HELIX 1321 1329 {ECO:0000244|PDB:3KKS}.
STRAND 1333 1338 {ECO:0000244|PDB:3KKS}.
HELIX 1342 1362 {ECO:0000244|PDB:3KKS}.
HELIX 1363 1365 {ECO:0000244|PDB:3KKS}.
HELIX 1369 1382 {ECO:0000244|PDB:3KKS}.
HELIX 1392 1401 {ECO:0000244|PDB:3KKS}.
SEQUENCE 1475 AA; 168063 MW; 4D249DCBB6158A78 CRC64;
MKRRELEKKL RKVRVTPQQD KYYTIGNLQW AIRMINLMGI KCVCDEECSA AEVALIITQF
SALDLENSPI RGKEEVAIKN TLKVFWSLLA GYKPESTETA LGYWEAFTYR EREARADKEG
EIKSIYPSLT QNTQNKKQTS NQTNTQSLPA ITTQDGTPRF DPDLMKQLKI WSDATERNGV
DLHAVNILGV ITANLVQEEI KLLLNSTPKW RLDVQLIESK VREKENAHRT WKQHHPEAPK
TDEIIGKGLS SAEQATLISV ECRETFRQWV LQAAMEVAQA KHATPGPINI HQGPKEPYTD
FINRLVAALE GMAAPETTKE YLLQHLSIDH ANEDCQSILR PLGPNTPMEK KLEACRVVGS
QKSKMQFLVA AMKEMGIQSP IPAVLPHTPE AYASQTSGPE DGRRCYGCGK TGHLKRNCKQ
QKCYHCGKPG HQARNCRSKN REVLLCPLWA EEPTTEQFSP EQHEFCDPIC TPSYIRLDKQ
PFIKVFIGGR WVKGLVDTGA DEVVLKNIHW DRIKGYPGTP IKQIGVNGVN VAKRKTHVEW
RFKDKTGIID VLFSDTPVNL FGRSLLRSIV TCFTLLVHTE KIEPLPVKVR GPGPKVPQWP
LTKEKYQALK EIVKDLLAEG KISEAAWDNP YNTPVFVIKK KGTGRWRMLM DFRELNKITV
KGQEFSTGLP YPPGIKECEH LTAIDIKDAY FTIPLHEDFR PFTAFSVVPV NREGPIERFQ
WNVLPQGWVC SPAIYQTTTQ KIIENIKKSH PDVMLYQYMD DLLIGSNRDD HKQIVQEIRD
KLGSYGFKTP DEKVQEERVK WIGFELTPKK WRFQPRQLKI KNPLTVNELQ QLVGNCVWVQ
PEVKIPLYPL TDLLRDKTNL QEKIQLTPEA IKCVEEFNLK LKDPEWKDRI REGAELVIKI
QMVPRGIVFD LLQDGNPIWG GVKGLNYDHS NKIKKILRTM NELNRTVVIM TGREASFLLP
GSSEDWEAAL QKEESLTQIF PVKFYRHSCR WTSICGPVRE NLTTYYTDGG KKGKTAAAVY
WCEGRTKSKV FPGTNQQAEL KAICMALLDG PPKMNIITDS RYAYEGMREE PETWAREGIW
LEIAKILPFK QYVGVGWVPA HKGIGGNTEA DEGVKKALEQ MAPCSPPEAI LLKPGEKQNL
ETGIYMQGLR PQSFLPRADL PVAITGTMVD SELQLQLLNI GTEHIRIQKD EVFMTCFLEN
IPSATEDHER WHTSPDILVR QFHLPKRIAK EIVARCQECK RTTTSPVRGT NPRGRFLWQM
DNTHWNKTII WVAVETNSGL VEAQVIPEET ALQVALCILQ LIQRYTVLHL HSDNGPCFTA
HRIENLCKYL GITKTTGIPY NPQSQGVVER AHRDLKDRLA AYQGDCETVE AALSLALVSL
NKKRGGIGGH TPYEIYLESE HTKYQDQLEQ QFSKQKIEKW CYVRNRRKEW KGPYKVLWDG
DGAAVIEEEG KTALYPHRHM RFIPPPDSDI QDGSS


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Genprice Inc, Invoices and accounting
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