POK6_HUMAN
ID POK6_HUMAN Reviewed; 956 AA.
AC Q9BXR3; Q6KH04; Q9BXR4; Q9UKH5; Q9UP31; Q9WIK9; Q9WJR4;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Endogenous retrovirus group K member 6 Pol protein;
DE AltName: Full=HERV-K(C7) Pol protein;
DE AltName: Full=HERV-K(HML-2.HOM) Pol protein;
DE AltName: Full=HERV-K108 Pol protein;
DE AltName: Full=HERV-K_7p22.1 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=ERVK-6; Synonyms=ERVK6;
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=10080172; DOI=10.1038/6766;
RA Mayer J., Sauter M., Racz A., Scherer D., Mueller-Lantzsch N., Meese E.U.;
RT "An almost-intact human endogenous retrovirus K on human chromosome 7.";
RL Nat. Genet. 21:257-258(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10469592; DOI=10.1016/s0960-9822(99)80390-x;
RA Barbulescu M., Turner G., Seaman M.I., Deinard A.S., Kidd K.K., Lenz J.;
RT "Many human endogenous retrovirus K (HERV-K) proviruses are unique to
RT humans.";
RL Curr. Biol. 9:861-868(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11401447; DOI=10.1006/geno.2000.6488;
RA Reus K., Mayer J., Sauter M., Scherer D., Mueller-Lantzsch N., Meese E.U.;
RT "Genomic organization of the human endogenous retrovirus HERV-K(HML-2.HOM)
RT (ERVK6) on chromosome 7.";
RL Genomics 72:314-320(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10516026; DOI=10.1128/jvi.73.11.9187-9195.1999;
RA Toenjes R.R., Czauderna F., Kurth R.;
RT "Genome wide screening, cloning, chromosomal assignment and expression of
RT full-length human endogenous retrovirus type K (HERV-K).";
RL J. Virol. 73:9187-9195(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-589.
RC TISSUE=Bone marrow;
RX PubMed=9971820; DOI=10.1128/jvi.73.3.2365-2375.1999;
RA Berkhout B., Jebbink M., Zsiros J.;
RT "Identification of an active reverse transcriptase enzyme encoded by a
RT human endogenous HERV-K retrovirus.";
RL J. Virol. 73:2365-2375(1999).
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 -!- PTM: Cleavage sites that yield the mature proteins remain to be
CC determined.
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: Two human-specific proviruses are inserted as tandem
CC repeats with a shared LTR in most individuals tested. The telomeric
CC copy is referred here as 'provirus 41574'. The centromeric copy is
CC referred here as 'provirus 41575'.
CC -!- SIMILARITY: Belongs to the beta type-B retroviral polymerase family.
CC HERV class-II K(HML-2) pol subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD51797.1; Type=Frameshift; Note=A -1 frameshift presumed to occur at the N-terminus at the Pro-Pol gene boundary.; Evidence={ECO:0000305};
CC Sequence=CAA76879.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA76885.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF074086; AAD21097.1; -; Genomic_DNA.
DR EMBL; AF074086; AAF88167.1; -; Genomic_DNA.
DR EMBL; AF164614; AAD51797.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF298587; AAK11553.1; -; Genomic_DNA.
DR EMBL; AF298588; AAK11554.1; -; Genomic_DNA.
DR EMBL; Y17832; CAA76879.1; ALT_INIT; Genomic_DNA.
DR EMBL; Y17834; CAA76885.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC072054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF080233; AAC63293.1; -; mRNA.
DR AlphaFoldDB; Q9BXR3; -.
DR SMR; Q9BXR3; -.
DR GlyGen; Q9BXR3; 1 site.
DR BioMuta; HGNC:13915; -.
DR DMDM; 52000839; -.
DR MassIVE; Q9BXR3; -.
DR PeptideAtlas; Q9BXR3; -.
DR PRIDE; Q9BXR3; -.
DR GeneCards; ERVK-6; -.
DR HGNC; HGNC:13915; ERVK-6.
DR MIM; 605626; gene.
DR neXtProt; NX_Q9BXR3; -.
DR PhylomeDB; Q9BXR3; -.
DR Pharos; Q9BXR3; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9BXR3; protein.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0035613; F:RNA stem-loop binding; IBA:GO_Central.
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 2: Evidence at transcript level;
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 6 Pol protein"
FT /id="PRO_0000186762"
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 865..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 870..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"
FT CONFLICT 32
FT /note="K -> R (in Ref. 3; AAK11554)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="A -> P (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="S -> N (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="C -> Y (in Ref. 3 and 5; in provirus 41576)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="F -> L (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="S -> P (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="R -> Q (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="T -> A (in Ref. 4; CAA76885)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="G -> E (in Ref. 3; AAK11554)"
FT /evidence="ECO:0000305"
FT CONFLICT 818
FT /note="N -> S (in Ref. 4; CAA76879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 956 AA; 107688 MW; E6872987ADCAE41A CRC64;
NKSRKRRNRE SLLGAATVEP PKPIPLTWKT EKPVWVNQWP LPKQKLEALH LLANEQLEKG
HIEPSFSPWN SPVFVIQKKS GKWRMLTDLR AVNAVIQPMG PLQPGLPSPA MIPKDWPLII
IDLKDCFFTI PLAEQDCEKF AFTIPAINNK EPATRFQWKV LPQGMLNSPT ICQTFVGRAL
QPVREKFSDC YIIHCIDDIL CAAETKDKLI DCYTFLQAEV ANAGLAIASD KIQTSTPFHY
LGMQIENRKI KPQKIEIRKD TLKTLNDFQK LLGDINWIRP TLGIPTYAMS NLFSILRGDS
DLNSKRMLTP EATKEIKLVE EKIQSAQINR IDPLAPLQLL IFATAHSPTG IIIQNTDLVE
WSFLPHSTVK TFTLYLDQIA TLIGQTRLRI IKLCGNDPDK IVVPLTKEQV RQAFINSGAW
KIGLANFVGI IDNHYPKTKI FQFLKLTTWI LPKITRREPL ENALTVFTDG SSNGKAAYTG
PKERVIKTPY 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 PQMQLNLALY
TLNFLNIYRN QTTTSAEQHL TGKKNSPHEG KLIWWKDNKN KTWEIGKVIT WGRGFACVSP
GENQLPVWIP TRHLKFYNEP IRDAKKSTSA ETETSQSSTV DSQDEQNGDV RRTDEVAIHQ
EGRAANLGTT KEADAVSYKI SREHKGDTNP REYAACSLDD CINGGKSPYA CRSSCS
