POL_FENV1
ID POL_FENV1 Reviewed; 1046 AA.
AC P31792; Q28415;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Pol polyprotein;
DE Contains:
DE RecName: Full=Reverse transcriptase/ribonuclease H;
DE Short=RT;
DE EC=2.7.7.49;
DE EC=2.7.7.7;
DE EC=3.1.26.4;
DE Contains:
DE RecName: Full=Integrase;
DE Short=IN;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P03355};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P03355};
DE Flags: Fragment;
GN Name=pol;
OS Feline endogenous virus ECE1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC unclassified Gammaretrovirus.
OX NCBI_TaxID=11766;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Moehring R., Drescher B., Riedel H., Bauer D., Rohde K., Beyer W.,
RA Rosenthal S.;
RT "The exogenous RD-114 and the related endogenous proviral element ECE1 of
RT domestic cat differ in their env genes.";
RL Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases.
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=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 -!- 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=2.7.7.7; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000305}.
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DR EMBL; X51929; CAB38566.1; -; Genomic_DNA.
DR PIR; S12813; GNMVCE.
DR SMR; P31792; -.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
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: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 Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR040643; MLVIN_C.
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; IPR041577; RT_RNaseH_2.
DR InterPro; IPR015416; Znf_H2C2_histone_UAS-bd.
DR Pfam; PF18697; MLVIN_C; 1.
DR Pfam; PF00075; RNase_H; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF09337; zf-H2C2; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW DNA integration; DNA recombination; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW RNA-directed DNA polymerase; Transferase; Viral genome integration;
KW Virus entry into host cell.
FT CHAIN <1..647
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000040980"
FT CHAIN 648..1046
FT /note="Integrase"
FT /id="PRO_0000040981"
FT DOMAIN 55..248
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 491..637
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 757..915
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT BINDING 500
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 500
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 559
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 629
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT NON_TER 1
SQ SEQUENCE 1046 AA; 117101 MW; 84556FC1BF29E4A9 CRC64;
LQDFPQAWAE TGGLGRAKCQ VPIIIDLKPT AMPVSIRQYP MSKEAHMGIQ PHITRFLELG
VLRPCRSPWN TPLLPVKKPG TRDYRPVQDL REVNKRTMDI HPTVPNPYNL LSTLSPDRTW
YTVLDLKDAF FCLPLAPQSQ ELFAFEWRDP ERGISGQLTW TRLPQGFKNS PTLFDEALHR
DLTDFRTQHP EVTLLQYVDD LLLAAPTKEA CIRGTKHLLR ELGDKGYRAS AKKAQICQTK
VTYLGYILSE GKRWLTPGRI ETVAHIPPPQ NPREVREFLG TAGFCRLWIP GFAELAAPLY
ALTKESAPFT WQEKHQSAFE ALKEALLSAP ALGLPDTSKP FTLFIDEKQG IAKGVLTQKL
GPWKRPVAYL SKKLDPVAAG WPPCLRIMAA TAMLVKDSAK LTLGQPLTVI TPHALEAIVR
QTPDRWITNA RLTHYQALLL DTDRIQFGPP VTLNPATLLP APEDQQSAHD CRQVLAETHG
TREDLKDQEL PDADHSWYTD GSSYIDSGTR RAGAAVVDGH HIIWAQSLPP GTSAQKAELI
ALTKALELSE GKKANIYTDS RYAFATAHTH GSIYERRGLL TSEGKEIKNK AEIIALLKAL
FLPRKVAIIH CPGHQKGQDP IATGNRQADQ VARQVAVAET LTLTTKLEET NLTTNKYAYT
PEDQEEAKAI GAILNQDTKD WEKEGKIVLP RKEALAMIQQ MHAWTHLSNQ KLKLLIEKTD
FLIPKAGTLI EQVTSACKVC QQVNAGATRV PEGKRTRGNR PGVYWEIDFT EVKPHYAGYK
YLLVFVDTFS GWVEAYPTRQ ETAHMVAKKI LEEIFPRFGL PKVIGSDNGP AFVSQVSQGL
ARTLGINWKL HCAYRPQSSG QVERMNRTIK ETLTKLTLET GLKDWRRLLS LALLRARNTP
NRFGLTPYEI LYGGPPPLST LLNSFSPSDP KTDLQARLKG LQAVQAQIWT PLAELYRPGH
PQTSYPFQVG DSVYVRWHRS QGLEPRWKGP YIVLLTTPTA IKVDGIAAWI HASHAKAAPK
TPGPETPKTW KLHRSENPLK IRLSRV
