POL_FIVT2
ID POL_FIVT2 Reviewed; 1124 AA.
AC P31822;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Pol polyprotein;
DE Contains:
DE RecName: Full=Protease;
DE EC=3.4.23.-;
DE AltName: Full=Retropepsin;
DE Contains:
DE RecName: Full=Reverse transcriptase/ribonuclease H;
DE Short=RT;
DE EC=2.7.7.49;
DE EC=3.1.26.13;
DE AltName: Full=Exoribonuclease H;
DE EC=3.1.13.2;
DE Contains:
DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE Short=dUTPase;
DE EC=3.6.1.23;
DE Contains:
DE RecName: Full=Integrase;
DE Short=IN;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P04585};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P04585};
GN Name=pol;
OS Feline immunodeficiency virus (isolate TM2) (FIV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=31676;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1649349; DOI=10.1128/jvi.65.8.4539-4542.1991;
RA Kiyomasu T., Miyazawa T., Furuya T., Shibata R., Sakai H., Sakuragi J.I.,
RA Fukasawa M., Maki N., Hasegawa A., Mikami T., Adachi A.;
RT "Identification of feline immunodeficiency virus rev gene activity.";
RL J. Virol. 65:4539-4542(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1312825; DOI=10.1007/bf01317136;
RA Maki N., Miyazawa T., Fukasawa M., Hasegawa A., Hayami M., Miki K.,
RA Mikami T.;
RT "Molecular characterization and heterogeneity of feline immunodeficiency
RT virus isolates.";
RL Arch. Virol. 123:29-45(1992).
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.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA
CC hybrid.; EC=3.1.13.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- PTM: Cleavage sites that yield the mature proteins remain to be
CC determined.
CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000305}.
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DR EMBL; M59418; AAA43071.1; -; Genomic_RNA.
DR PIR; B45557; B45557.
DR SMR; P31822; -.
DR MEROPS; A02.007; -.
DR PRIDE; P31822; -.
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:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
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:0009117; P:nucleotide metabolic process; 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; cd05482; HIV_retropepsin_like; 1.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 1.10.10.200; -; 1.
DR Gene3D; 2.30.30.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 3.
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; IPR034170; Retropepsin-like_cat_dom.
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 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; SSF46919; SSF46919; 1.
DR SUPFAM; SSF50122; SSF50122; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
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; DNA integration; DNA recombination; DNA-binding;
KW Endonuclease; Hydrolase; Metal-binding; Multifunctional enzyme; Nuclease;
KW Nucleotide metabolism; Nucleotidyltransferase; Protease;
KW RNA-directed DNA polymerase; Transferase; Viral genome integration;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT CHAIN 1..153
FT /note="Protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038849"
FT CHAIN 154..709
FT /note="Reverse transcriptase/ribonuclease H"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038850"
FT CHAIN 710..843
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038851"
FT CHAIN 844..1124
FT /note="Integrase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038852"
FT DOMAIN 62..143
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 199..388
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 591..711
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 899..1049
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 848..889
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 1067..1115
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 67
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT BINDING 600
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 600
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 633
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 653
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 703
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 857
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 861
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 885
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 888
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
SQ SEQUENCE 1124 AA; 128101 MW; F287FE90FC978296 CRC64;
ENLGKREGGA SCSPSKPSAA NSTICTSNGG ETIRFINYNT IGTTTTLERR PEIQIFVNGH
PIKFLLDTGA DITILNRKDF QIGNSIENGK QNMIGVGGGK RGTNYINVHL EIRDENYRMQ
CIFGNVCVLE DNSLIQPLLG RDNMIKFNIR LVMAQISEKI PIVKVRMKDP TQGPQVKQWP
LSNEKIEALT DIVERLESEG KVKRADPNNP WNTPVFAIKK KSGKWRMLID FRVLNKLTDK
GAEVQLGLPH PAGLQMKKQV TVLDIGDAYF TIPLDPDYAP YTAFTLPRKN NAGPGRRYVW
CSLPQGWVLS PLIYQSTLNN ILQPFIKQNS ELDIYQYMDD IYIGSNLNKK EHKQKVEELR
KLLLWWGFET PEDKLQEEPP YKWMGYELHP LTWSIQQKQL EIPERPTLNE LQKLAGKINW
ASQTIPDLSI KELTNMMRGD QKLDSIREWT VEAKREVQKA KEAIETQAQL NYYDPNRGLY
AKLSLVGPHQ ICYQVYQKNP EHILWYGKIN RQKKKAENTC DIALRACYKI REESIIRIGK
EPVYEIPASR EAWESNLIRS PYLKAPPPEV EFIHAALSIK RALSMIQDAP IIGAETWYID
GSRKQGKAAR AAYWTNTGKW QIMEIEGSNQ KAEVQALLLA LKAGSEEMNI ITDSQYILNI
LNQQPDLMEG LWQEVLEQME KKIAIFIDWV PGHKGIPGNE EVDKLCQTMM IIEGEGILEK
RSEDAGYDLL AAAQETHFLP GEVRIVPTKT RIMLPKGHWG LIMGKSSIGS KGVDVLGGVI
DEGYRGELGV IMINLTKKSI TILEKQKIAQ LIILPCRHEG LQQGEIQMNS ERGEKGFGSA
GVFSSWVDRI EEAELNHEKF HSDPQYLRTE FNLPRIVAEE IKRKCPLCRI RGEQVGGQLK
IRPGIWQMDC THFNGKIIIV AVHVESGFLW AQIIPQETAD CTVKALLQLI CAHNVTELQT
DNGPNFKNQK MEGLLNYMGI KHKLGIPGNP QSQALVENAN NTLKVWIQKF LPETTSLDNA
LALALHCLNF KQRGRLGRMA PYELYIQQES LRIQDYFSAI PQKLMMQWLY YKDQKDKKWK
GPMRVEYWGQ GSVLLKDEEK GIFLVPRRHI RRVPEPCTLP EGDE
