PO113_HUMAN
ID PO113_HUMAN Reviewed; 956 AA.
AC P63132;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Endogenous retrovirus group K member 113 Pol protein;
DE AltName: Full=HERV-K113 Pol protein;
DE AltName: Full=HERV-K_19p13.11 provirus ancestral Pol protein;
DE Includes:
DE RecName: Full=Reverse transcriptase;
DE Short=RT;
DE EC=2.7.7.49;
DE Includes:
DE RecName: Full=Ribonuclease H;
DE Short=RNase H;
DE EC=3.1.26.4;
DE Includes:
DE RecName: Full=Integrase;
DE Short=IN;
GN Name=HERVK_113;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11591322; DOI=10.1016/s0960-9822(01)00455-9;
RA Turner G., Barbulescu M., Su M., Jensen-Seaman M.I., Kidd K.K., Lenz J.;
RT "Insertional polymorphisms of full-length endogenous retroviruses in
RT humans.";
RL Curr. Biol. 11:1531-1535(2001).
CC -!- FUNCTION: Early post-infection, the reverse transcriptase converts the
CC viral RNA genome into double-stranded viral DNA. The RNase H domain of
CC the reverse transcriptase performs two functions. It degrades the RNA
CC template and specifically removes the RNA primer from the RNA/DNA
CC hybrid. Following nuclear import, the integrase catalyzes the insertion
CC of the linear, double-stranded viral DNA into the host cell chromosome.
CC Endogenous Pol proteins may have kept, lost or modified their original
CC function during evolution.
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=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
CC -!- DOMAIN: The LPQG and YXDD motifs are catalytically important and
CC conserved among many retroviruses.
CC -!- MISCELLANEOUS: This protein is synthesized as Gag-Pro and Gag-Pro-Pol
CC polyprotein precursors. These polyproteins are thought, by similarity
CC with type-B retroviruses, to be generated by -1 frameshifts occurring
CC at the Gag-Pro and Pro-Pol genes boundaries.
CC -!- MISCELLANEOUS: Exact N-terminus of this protein has not been formally
CC described.
CC -!- MISCELLANEOUS: Insertional polymorphism. Provirus present in 29% of
CC tested individuals.
CC -!- SIMILARITY: Belongs to the beta type-B retroviral polymerase family.
CC HERV class-II K(HML-2) pol subfamily. {ECO:0000305}.
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DR EMBL; AY037928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P63132; -.
DR SMR; P63132; -.
DR BioMuta; HERVK_113; -.
DR MassIVE; P63132; -.
DR PeptideAtlas; P63132; -.
DR PRIDE; P63132; -.
DR neXtProt; NX_P63132; -.
DR PhylomeDB; P63132; -.
DR Pharos; P63132; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P63132; protein.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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: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:0006281; P:DNA repair; IEA:UniProt.
DR Gene3D; 1.10.10.200; -; 1.
DR Gene3D; 2.30.30.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
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; 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; IPR010661; RVT_thumb.
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; PF00078; RVT_1; 1.
DR Pfam; PF06817; RVT_thumb; 1.
DR SUPFAM; SSF46919; SSF46919; 1.
DR SUPFAM; SSF50122; SSF50122; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR SUPFAM; SSF56672; SSF56672; 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 DNA integration; DNA recombination; DNA-binding; Endonuclease; ERV;
KW Hydrolase; Metal-binding; Multifunctional enzyme; Nuclease;
KW Nucleotidyltransferase; Reference proteome; RNA-directed DNA polymerase;
KW Transferase; Transposable element; Zinc; Zinc-finger.
FT CHAIN 1..956
FT /note="Endogenous retrovirus group K member 113 Pol
FT protein"
FT /id="PRO_0000186765"
FT DOMAIN 57..245
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 460..590
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 642..803
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 587..628
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 811..859
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 864..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 161..164
FT /note="LPQG"
FT MOTIF 195..198
FT /note="YXDD"
FT COMPBIAS 865..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 517
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 582
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 596
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 600
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 624
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 627
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
SQ SEQUENCE 956 AA; 107766 MW; EC6A43D4F8F18456 CRC64;
NKSRKRRNRV SFLGAATVEP PKPIPLTWKT EKPVWVNQWP LPKQKLEALH LLANEQLEKG
HIEPSFSPWN SPVFVIQKKS GKWRMLTDLR AVNAVIQPMG PLQPGLPSPA MIPKDWPLII
IDLKDCFFTI PLAEQDCEKF AFTIPAINNK EPATRFQWKV LPQGMLNSPT ICQTFVGRAL
QPVRDKFSDC YIIHYIDDIL CAAETKDKLI DCYTFLQAEV ANAGLAIASD KIQTSTPFHY
LGMQIENRKI KPQKIEIRKD TLKTLNDFQK LLGDINWIRP TLGIPTYVMS NLFSILRGDS
DLNSKRMLTP ETTKEIKLVE EKIQSAQINR IDPLAPLRLL IFATAHSPIG IIIQNTDLVE
WSFLPHSTVK TFTLYLDQIA TLIGQTRLRI IKLCGNDPDK IVVPLTKEQV RQAFINSGAW
QIGLANFVGI IDNHYPKTKI FQFLKLTTWI LPKITRREPL ENALTVFTDG SSNGKAAYTG
LKERVIKTPY QSAQRAELVA VITVLQDFDQ PINIISDSAY VVQATRDVET ALIKYSMDDQ
LNQLFNLLQQ TVRKRNFPFY ITHIRAHTNL PGPLTKANEQ ADLLVSSALI KAQELHALTH
VNAAGLKNKF DVTWKQAKDI VQHCTQCQVL HLPTQEAGVN PRGLCPNALW QMDVTHVPSF
GRLSYVHVTV DTYSHFIWAT CQTGESTSHV KKHLLSCFAV MGVPEKIKTD NGPGYCSKAF
QKFLSQWKIS HTTGIPYNSQ GQAIVERTNR TLKTQLVKQK EGGDSKECTT PQMQLNLAPY
TLNFLNIYRN QTTTSAEQHL TGKKNSPHEG KLIWWKDNKN KTWEIGKVIT WGRGFACVSP
GENQLPVWMP TRHLKFYNEP IGDAKKSTSA ETETPQSSTV DSQDEQNGDV RRTDEVAIHQ
EGRAADLGTT KEADAVSYKI SREHKGDTNP REYAACSLDD CINGGKSPYA CRSSCS
