POK10_HUMAN
ID POK10_HUMAN Reviewed; 1014 AA.
AC P10266; P87890; Q14273;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Endogenous retrovirus group K member 10 Pol protein;
DE AltName: Full=HERV-K10 Pol protein;
DE AltName: Full=HERV-K107 Pol protein;
DE AltName: Full=HERV-K_5q33.3 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-10;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-740.
RX PubMed=3021993; DOI=10.1128/jvi.60.2.589-598.1986;
RA Ono M., Yasunaga T., Miyata T., Ushikubo H.;
RT "Nucleotide sequence of human endogenous retrovirus genome related to the
RT mouse mammary tumor virus genome.";
RL J. Virol. 60:589-598(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-740.
RX PubMed=9217052; DOI=10.1006/viro.1997.8614;
RA Toenjes R.R., Boller K., Limbach R., Lugert R., Kurth R.;
RT "Characterization of human endogenous retrovirus type K (HERV-K) virus-like
RT particles generated from recombinant baculoviruses.";
RL Virology 233:280-291(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-830.
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).
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: Has a type 1 genome. The HERV-K(HML-2) family contains
CC type 1 and type 2 genomes depending on the absence or presence of 292
CC nucleotides at the 5'-end of the env gene. Type 1 genomes lack a pol
CC stop codon, leading to expression of a fusion protein containing a
CC portion of the Env sequence.
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=AAD51796.1; Type=Frameshift; Note=A -1 frameshift presumed to occur at the N-terminus at the Pro-Pol gene boundary.; Evidence={ECO:0000305};
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DR EMBL; AC016577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M14123; AAA88033.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Y10391; CAA71417.1; -; Genomic_DNA.
DR EMBL; AF164613; AAD51796.1; ALT_SEQ; Genomic_DNA.
DR PIR; D24483; GNHUER.
DR AlphaFoldDB; P10266; -.
DR SMR; P10266; -.
DR IntAct; P10266; 1.
DR BioMuta; HGNC:39004; -.
DR MassIVE; P10266; -.
DR PeptideAtlas; P10266; -.
DR PRIDE; P10266; -.
DR GeneCards; ERVK-10; -.
DR HGNC; HGNC:39004; ERVK-10.
DR neXtProt; NX_P10266; -.
DR PhylomeDB; P10266; -.
DR PathwayCommons; P10266; -.
DR SignaLink; P10266; -.
DR Pharos; P10266; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P10266; 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; IPR029104; HERV-K_env.
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; PF13804; HERV-K_env_2; 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; 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..1014
FT /note="Endogenous retrovirus group K member 10 Pol protein"
FT /id="PRO_0000186769"
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 MOTIF 161..164
FT /note="LPQG"
FT MOTIF 195..198
FT /note="YXDD"
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 1
FT /note="N -> M (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="D -> A (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="Y -> H (in Ref. 4; AAD51796)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="S -> SYS (in Ref. 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1014 AA; 114827 MW; 7E320F8F5DEE19FE CRC64;
NKSRKRRNRV SFLGAVTVEP PKPIPLTWKT EKPVWVNQWP LPKQKLEALH LLANEQLEKG
HIEPSFSPWN SPVFVIQKKS GKWHTLTDLR AVNAVIQPMG PLQPGLPSPA MIPKDWPLII
IDLKDCFFTI PLAEQDCEKF AFTIPAINNK EPATRFQWKV LPQGMLNSPT ICQTFVGRAL
QPVREKFSDC YIIHYIDDIL CAAETKDKLI DCYTFLQAEV ANAGLAIASD KIQTSTPFHY
LGMQIENRKI KPQKIEIRKD TLKTLNDFQK LLGDINWIRP TLGIPTYAMS NLFSILRGDS
DLNSQRILTP EATKEIKLVE EKIQSAQINR IDPLAPLQLL IFATAHSPTG IIIQNTDLVE
WSFLPHSTVK TFTLYLDQIA TLIGQTRLRI TKLCGNDPDK IVVPLTKEQV RQAFINSGAW
QIGLANFVGL IDNHYPKTKI FQFLKLTTWI LPKITRREPL ENALTVFTDG SSNGKAAYTG
PKERVIKTPY QSAQRDELVA VITVLQDFDQ PINIISDSAY VVQATRDVET ALIKYSMDDQ
LNQLFNLLQQ TVRKRNFPFY ITYIRAHTNL 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
GENQLPVWLP TRHLKFYNEP IGDAKKRAST EMVTPVTWMD NPIEVYVNDS IWVPGPIDDR
CPAKPEEEGM MINISIGYRY PPICLGRAPG CLMPAVQNWL VEVPTVSPIS RFTYHMVSGM
SLRPRVNYLQ DFSYQRSLKF RPKGKPCPKE IPKESKNTEV LVWEECVANS AVIL
