POK19_HUMAN
ID POK19_HUMAN Reviewed; 959 AA.
AC Q9WJR5; O15312;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Endogenous retrovirus group K member 19 Pol protein;
DE AltName: Full=HERV-K(C19) Pol protein;
DE AltName: Full=HERV-K_19q11 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-19;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-275.
RC TISSUE=Bone marrow;
RX PubMed=9460924; DOI=10.1099/0022-1317-79-1-61;
RA Zsiros J., Jebbink M.F., Lukashov V.V., Voute P.A., Berkhout B.;
RT "Evolutionary relationships within a subgroup of HERV-K-related human
RT endogenous retroviruses.";
RL J. Gen. Virol. 79:61-70(1998).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=1;
CC Comment=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 Name=1;
CC IsoId=Q9WJR5-1; Sequence=Displayed;
CC -!- DOMAIN: The LPQG and YXDD motifs are catalytically important and
CC conserved among many retroviruses.
CC -!- MISCELLANEOUS: Exact N-terminus of this protein has not been formally
CC described.
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=AC112702; Type=Frameshift; Note=The frameshift results from the integration of a SINE element AluYa5.; Evidence={ECO:0000305};
CC Sequence=CAA76882.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y17833; CAA76882.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC112702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U87592; AAB63115.1; -; mRNA.
DR AlphaFoldDB; Q9WJR5; -.
DR SMR; Q9WJR5; -.
DR IntAct; Q9WJR5; 4.
DR BioMuta; HGNC:39026; -.
DR MassIVE; Q9WJR5; -.
DR PeptideAtlas; Q9WJR5; -.
DR PRIDE; Q9WJR5; -.
DR GeneCards; ERVK-19; -.
DR HGNC; HGNC:39026; ERVK-19.
DR neXtProt; NX_Q9WJR5; -.
DR InParanoid; Q9WJR5; -.
DR PhylomeDB; Q9WJR5; -.
DR PathwayCommons; Q9WJR5; -.
DR SignaLink; Q9WJR5; -.
DR Pharos; Q9WJR5; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9WJR5; 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; Ribosomal frameshifting;
KW RNA-directed DNA polymerase; Transferase; Transposable element; Zinc;
KW Zinc-finger.
FT CHAIN 1..959
FT /note="Endogenous retrovirus group K member 19 Pol protein"
FT /id="PRO_0000186763"
FT DOMAIN 57..248
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 463..593
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 645..806
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 590..631
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 814..862
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 867..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 164..167
FT /note="LPQG"
FT MOTIF 198..201
FT /note="YXDD"
FT COMPBIAS 868..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
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 520
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 585
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 599
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 603
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 BINDING 630
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT CONFLICT 15
FT /note="A -> V (in Ref. 2; AC112702)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="M -> T (in Ref. 2; AC112702)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="E -> G (in Ref. 2; AC112702)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="P -> T (in Ref. 2; AC112702)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 959 AA; 108106 MW; 60276896681286A9 CRC64;
NKSKKRRNRV SFLGAATVEP PKPIPLTWKT EKPVWVNQWP LPKQKLEALH LLANEQLEKG
HIEPSFSPWN SPVFVIQKKS GKWRMLTDLR AVNAVNAVIQ PMGPLQPGLP SLAMIPKDWP
LIIIDLKDCF FTIPLAEQDC EKFAFTIPAI NNKEPATRFQ WKVLPQGMLN SPTICQTFVG
RALQPVREKF SDCYIIHYID DILCAAEMKD KLIDCYTFLQ AEVANAGLAI ASDKIQTSTP
FHYLEMQIEN RKIKPPKIEI RKDTLKTLND FQKLLGDINW IRPTLGIPTY AMSNLFSILR
GDSDLNSKRM LTPEATKEIK LVEEKIQSAQ INRIDPLAPL QLLIFATAHS PTGIIIQNTD
LVEWSFLPHS TVKTFTLYLD QMATLIGQTR LRIIKLCGND PDKIVVPLTK EQVRQAFINS
GAWQIGLANF VGIIDNHYPK TKIFQFLKMT TWILPKITRR EPLENALTVF TDGSSNGKAA
YTGPKERVIK TQYQSAQRAE LVAVITVLQD FDQPINIISD SAYVVQATRD VETALIKYSM
DDQLNQLFNL LQQTVRKRNF PFYITHIRAH TNLPGPLTKA NEQADLLVSS ALIKAQELHA
LTHVNVAGLK NKFDVTWKQA KDIVQHCTQC QVLHLPTQEA GVNPRGLCPN ALWQMDVTHV
SSFGRLSYIH VTVDTYSHFI WATCQTGEST SHVKKHLLSC FAVMGVPEKI KTDNGPGYCS
KAFQKFLSQW KISHTTGIPY NSQGQAIVER TNRTLKTQLV KQKEGGDSKE CTTPQMQLNL
ALYTLNFLNI YRNQTTTSAE QHLTGKKNSP HEGKLIWWKD NKNKTWEIGK VITWGRGFAC
VSPGENQLPV WIPTRHLKFY NEPIGDAKKS TSAETETPQS STVDSQDEQN GDVRRTDEVA
IHQESRAADL GTTKEADAVS YKISREHKGD TNPREYAACG LDDCINGGKS PYACRSSCS
