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Pol polyprotein [Cleaved into: Protease (Retropepsin) (EC 3.4.23.-); Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

 POL_EIAVY               Reviewed;        1145 AA.
P03371;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
20-JUN-2018, entry version 136.
RecName: Full=Pol polyprotein;
Contains:
RecName: Full=Protease;
AltName: Full=Retropepsin;
EC=3.4.23.-;
Contains:
RecName: Full=Reverse transcriptase/ribonuclease H;
Short=RT;
EC=2.7.7.49;
EC=3.1.26.13;
AltName: Full=Exoribonuclease H;
EC=3.1.13.2;
Contains:
RecName: Full=Integrase;
Short=IN;
EC=2.7.7.- {ECO:0000250|UniProtKB:P04585};
EC=3.1.-.- {ECO:0000250|UniProtKB:P04585};
Name=pol;
Equine infectious anemia virus (strain Wyoming) (EIAV).
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
NCBI_TaxID=11672;
NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
NCBI_TaxID=9796; Equus caballus (Horse).
[1]
NUCLEOTIDE SEQUENCE.
PubMed=3003905; DOI=10.1126/science.3003905;
Stephens R.M., Casey J.W., Rice N.R.;
"Equine infectious anemia virus gag and pol genes: relatedness to
visna and AIDS virus.";
Science 231:589-594(1986).
[2]
NUCLEOTIDE SEQUENCE OF 1029-1145.
PubMed=2431539; DOI=10.1016/0042-6822(86)90195-9;
Rushlow K., Olsen K., Stiegler G., Payne S.L., Montelaro R.C.,
Issel C.J.;
"Lentivirus genomic organization: the complete nucleotide sequence of
the env gene region of equine infectious anemia virus.";
Virology 155:309-321(1986).
-!- 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.
-!- CATALYTIC ACTIVITY: 3'-end directed exonucleolytic cleavage of
viral RNA-DNA hybrid.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
-!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
{ECO:0000305}.
-!- CAUTION: The original EMBL accession numbers (M11337 and M14855)
assigned to this isolate (isolate Wyoming) have been made
secondary to M16575 which is from a different isolate (clone
1365). {ECO:0000305}.
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PIR; A03970; GNLJEV.
ProteinModelPortal; P03371; -.
SMR; P03371; -.
DrugBank; DB03413; Deoxyuridine-5'-Diphosphate.
PRIDE; P03371; -.
BRENDA; 3.4.23.B3; 2115.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004533; F:exoribonuclease H activity; IEA:UniProtKB-EC.
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: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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
CDD; cd07557; trimeric_dUTPase; 1.
Gene3D; 1.10.10.200; -; 1.
Gene3D; 2.30.30.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 2.70.40.10; -; 1.
Gene3D; 3.30.420.10; -; 2.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR029054; dUTPase-like.
InterPro; IPR036157; dUTPase-like_sf.
InterPro; IPR033704; dUTPase_trimeric.
InterPro; IPR017856; Integrase-like_N.
InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
InterPro; IPR001037; Integrase_C_retrovir.
InterPro; IPR001584; Integrase_cat-core.
InterPro; IPR003308; Integrase_Zn-bd_dom_N.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
InterPro; IPR018061; Retropepsins.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR002156; RNaseH_domain.
InterPro; IPR036397; RNaseH_sf.
InterPro; IPR000477; RT_dom.
InterPro; IPR010659; RVT_connect.
InterPro; IPR010661; RVT_thumb.
Pfam; PF00692; dUTPase; 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; PF06815; RVT_connect; 1.
Pfam; PF06817; RVT_thumb; 1.
SUPFAM; SSF46919; SSF46919; 1.
SUPFAM; SSF50122; SSF50122; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF51283; SSF51283; 1.
SUPFAM; SSF53098; SSF53098; 2.
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; PS50876; ZF_INTEGRASE; 1.
3: Inferred from homology;
Aspartyl protease; Cleavage on pair of basic residues;
DNA integration; DNA recombination; DNA-binding; Endonuclease;
Hydrolase; Metal-binding; Multifunctional enzyme; Nuclease;
Nucleotidyltransferase; Protease; RNA-directed DNA polymerase;
Transferase; Viral genome integration; Virus entry into host cell;
Zinc; Zinc-finger.
CHAIN 1 195 Protease.
/FTId=PRO_0000038835.
CHAIN 196 913 Reverse transcriptase/ribonuclease H.
/FTId=PRO_0000038836.
CHAIN 914 1145 Integrase.
/FTId=PRO_0000038837.
DOMAIN 100 174 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
DOMAIN 230 418 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
DOMAIN 616 739 RNase H. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
DOMAIN 920 1077 Integrase catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00457}.
ZN_FING 877 918 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00450}.
DNA_BIND 1095 1143 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00506}.
ACT_SITE 105 105 {ECO:0000255|PROSITE-ProRule:PRU10094}.
SEQUENCE 1145 AA; 129520 MW; EE723380950D5D9E CRC64;
TAWTFLKAMQ KCSKKREARG SREAPETNFP DTTEESAQQI CCTRDSSDSK SVPRSERNKK
GIQCQGEGSS RGSQPGQFVG VTYNLEKRPT TIVLINDTPL NVLLDTGADT SVLTTAHYNR
LKYRGRKYQG TGIIGVGGNV ETFSTPVTIK KKGRHIKTRM LVADIPVTIL GRDILQDLGA
KLVLAQLSKE IKFRKIELKE GTMGPKIPQW PLTKEKLEGA KETVQRLLSE GKISEASDNN
PYNSPIFVIK KRSGKWRLLQ DLRELNKTVQ VGTEISRGLP HPGGLIKCKH MTVLDIGDAY
FTIPLDPEFR PYTAFTIPSI NHQEPDKRYV WKCLPQGFVL SPYIYQKTLQ EILQPFRERY
PEVQLYQYMD DLFVGSNGSK KQHKELIIEL RAILQKGFET PDDKLQEVPP YSWLGYQLCP
ENWKVQKMQL DMVKNPTLND VQKLMGNITW MSSGVPGLTV KHIAATTKGC LELNQKVIWT
EEAQKELEEN NEKIKNAQGL QYYNPEEEML CEVEITKNYE ATYVIKQSQG ILWAGKKIMK
ANKGWSTVKN LMLLLQHVAT ESITRVGKCP TFKVPFTKEQ VMWEMQKGWY YSWLPEIVYT
HQVVHDDWRM KLVEEPTSGI TIYTDGGKQN GEGIAAYVTS NGRTKQKRLG PVTHQVAERM
AIQMALEDTR DKQVNIVTDS YYCWKNITEG LGLEGPQNPW WPIIQNIREK EIVYFAWVPG
HKGIYGNQLA DEAAKIKEEI MLAYQGTQIK EKRDEDAGFD LCVPYDIMIP VSDTKIIPTD
VKIQVPPNSF GWVTGKSSMA KQGLLINGGI IDEGYTGEIQ VICTNIGKSN IKLIEGQKFA
QLIILQHHSN SRQPWDENKI SQRGDKGFGS TGVFWVENIQ EAQDEHENWH TSPKILARNY
KIPLTVAKQI TQECPHCTKQ GSGPAGCVMR SPNHWQADCT HLDNKIILHF VESNSGYIHA
TLLSKENALC TSLAILEWAR LFSPKSLHTD NGTNFVAEPV VNLLKFLKIA HTTGIPYHPE
SQGIVERANR TLKEKIQSHR DNTQTLEAAL QLALITCNKG RESMGGQTPW EVFITNQAQV
IHEKLLLQQA QSSKKFCFYK IPGEHDWKGP TRVLWKGDGA VVVNDEGKGI IAVPLTRTKL
LIKPN


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