ID E2E2J3_9RETR Unreviewed; 1134 AA.
AC E2E2J3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Pol polyprotein {ECO:0000256|ARBA:ARBA00023479};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ADK35828.1};
OS Equine infectious anemia virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11665 {ECO:0000313|EMBL:ADK35828.1};
RN [1] {ECO:0000313|EMBL:ADK35828.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FDDV-9 {ECO:0000313|EMBL:ADK35828.1};
RX PubMed=21136127; DOI=10.1007/s00705-010-0877-8;
RA Wang X., Wang S., Lin Y., Jiang C., Ma J., Zhao L., Lv X., Wang F.,
RA Shen R., Kong X., Zhou J.;
RT "Genomic comparison between attenuated Chinese equine infectious anemia
RT virus vaccine strains and their parental virulent strains.";
RL Arch. Virol. 156:353-357(2011).
CC -!- FUNCTION: During replicative cycle of retroviruses, the reverse-
CC transcribed viral DNA is integrated into the host chromosome by the
CC viral integrase enzyme. RNase H activity is associated with the reverse
CC transcriptase. {ECO:0000256|ARBA:ARBA00023429}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA
CC hybrid.; EC=3.1.13.2; Evidence={ECO:0000256|ARBA:ARBA00000379};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different
CC cleavage modes: 1. sequence-specific internal cleavage of RNA. Human
CC immunodeficiency virus type 1 and Moloney murine leukemia virus
CC enzymes prefer to cleave the RNA strand one nucleotide away from the
CC RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides
CC from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides
CC away from the primer terminus.; EC=3.1.26.13;
CC Evidence={ECO:0000256|ARBA:ARBA00023415};
CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000256|ARBA:ARBA00009555, ECO:0000256|RuleBase:RU004064}.
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DR EMBL; GU385359; ADK35828.1; -; Genomic_DNA.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004533; F:exoribonuclease H activity; IEA:UniProtKB-EC.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 1.10.10.200; -; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR Gene3D; 3.30.70.270; -; 3.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR Gene3D; 2.30.30.10; Integrase, C-terminal domain superfamily, retroviral; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR InterPro; IPR017856; Integrase-like_N.
DR InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
DR InterPro; IPR001037; Integrase_C_retrovir.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR003308; Integrase_Zn-bd_dom_N.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR010659; RVT_connect.
DR InterPro; IPR010661; RVT_thumb.
DR PANTHER; PTHR41694; ENDOGENOUS RETROVIRUS GROUP K MEMBER POL PROTEIN; 1.
DR PANTHER; PTHR41694:SF5; RIBONUCLEASE H; 1.
DR Pfam; PF00692; dUTPase; 1.
DR Pfam; PF00552; IN_DBD_C; 1.
DR Pfam; PF02022; Integrase_Zn; 1.
DR Pfam; PF00075; RNase_H; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF06815; RVT_connect; 1.
DR Pfam; PF06817; RVT_thumb; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF50122; DNA-binding domain of retroviral integrase; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF51283; dUTPase-like; 1.
DR SUPFAM; SSF46919; N-terminal Zn binding domain of HIV integrase; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 2.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS51027; INTEGRASE_DBD; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50876; ZF_INTEGRASE; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU004064};
KW DNA integration {ECO:0000256|ARBA:ARBA00022908};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004064};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004064};
KW RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Viral genome integration {ECO:0000256|ARBA:ARBA00023195};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00450}.
FT DOMAIN 88..162
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 218..407
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 605..728
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT DOMAIN 866..907
FT /note="Integrase-type"
FT /evidence="ECO:0000259|PROSITE:PS50876"
FT DOMAIN 909..1066
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 1084..1132
FT /note="Integrase-type"
FT /evidence="ECO:0000259|PROSITE:PS51027"
FT DNA_BIND 1084..1132
FT /note="Integrase-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00506"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADK35828.1"
SQ SEQUENCE 1134 AA; 127977 MW; 663EB66DE4E755C7 CRC64;
KCSKKRETRG SGEAPETNFP CAEGVNGQNT KGRETARDLI SRFESDETGI QDQGRGKSGG
FQSEQFVGVT YNLEKRPTTI VLINDTPLNV LLDTGADTSV LTIAHYNRLK YRGRKYQGTG
IVGVGGNVET FSTPVTVKKK GKQIKTRMLV ADIPVTILGR DILQELGAQL IMAQLSKEIT
PREIKLKTGT VGPKVPQWPL TKEKLLGAKE IVKKLLDEGK ISEASDDNPY NSPIFVIKKK
SGKWRLLQDL RELNKVVQVG TEISRGLPHP GGLIKCNHMT VLDIGDAYFT IPLDPKFRQY
TAFTAPSINH QEPDKRYVWN CLPQGFVLSP YIYQKTLQDI LQAFRERHPD VQLYQYMDDL
FIGSNESKRQ HKELVEELRA ILLEKGFEMP EDKLQEEAPY NWLGYQLSPG NWKVQKMQLE
LVKEPTLNDV QKLMGIITWM SSGVPGLTVK QIAATTKGCL DLNQKVVWTE EAQKELEENN
KKIQEAQGLQ YYNPEEEVIC EIEITKNYEA TYIIKQSQGI LWAGKKIMRA NKGWSAARNL
MLLLQHVATE SIVRIGTCPK FKVPFTKEQV KWEMEKGWYY SWLPDMIYSH QVVHDDWRLK
LVEQPTSGIT IYTDGGKQDE EGVAAYVTSN GKTKQKRLGP VTHQTAERIA IQMALEDTEE
TLVNIVTDSY YCWKNITEGL GLEGPDSPWW PIIQNIRAKE MVYFAWVPGH KGIYGNQLAD
EATKITEEIM LAYQGTQIKE KGDEDAGFDL CIPYDMIIPV SETKVIPTDV KIQVPHKCFG
WVTGKSSMAK QGLLINGGII DEGYTGEIQV ICTNIGKSNI KLREGQKFAQ LIILQHRSND
KQIWDENKTS QRGDKGFGST GIFWVENIQE ALDEHENWHT SPKILAKRYG LPLTVAKQIT
QECPHCTKQG SGPAGCVMRS PNHWQADCTH LENRIIMTFV ESNSGYIHAT LLSKENALCT
SLAILEWVRL FSPKSLHTDN GTNFVAESVA NLLKFLKVTH TTGIPYHPES QGIVERANRT
LKEKIKSHRE NTQTLEAALQ LALITCNKGR ESMGGQTPWE VFITNQAQTI HEELLLQQAQ
SSKKFCFYKI PGEHNWKGPT RVLWKGDGAV VVNDEEKGII AVPLTRTKLL IRPN
//
