POK11_HUMAN
ID POK11_HUMAN Reviewed; 969 AA.
AC Q9UQG0; Q6KH06; Q86YP3;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Endogenous retrovirus group K member 11 Pol protein;
DE AltName: Full=HERV-K_3q27.2 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-11;
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=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-597.
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 138-864.
RA Hirschl S., Muster T.;
RT "Melanoma associated endogenous retrovirus.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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=Q9UQG0-1; 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 -!- MISCELLANEOUS: The 102 C-terminal amino acids differ from HERV-K(HML-2)
CC Pol prototype due to a frameshift in position 867.
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; AC099661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF080229; AAC63290.1; -; mRNA.
DR EMBL; AF080232; AAC63292.1; -; mRNA.
DR EMBL; AY186778; AAO27434.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9UQG0; -.
DR SMR; Q9UQG0; -.
DR BioMuta; HGNC:39006; -.
DR DMDM; 52000846; -.
DR MassIVE; Q9UQG0; -.
DR PeptideAtlas; Q9UQG0; -.
DR PRIDE; Q9UQG0; -.
DR GeneCards; ERVK-11; -.
DR HGNC; HGNC:39006; ERVK-11.
DR neXtProt; NX_Q9UQG0; -.
DR PhylomeDB; Q9UQG0; -.
DR Pharos; Q9UQG0; Tdark.
DR PRO; PR:Q9UQG0; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9UQG0; 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 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..969
FT /note="Endogenous retrovirus group K member 11 Pol protein"
FT /id="PRO_0000186773"
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 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 149
FT /note="N -> Y (in Ref. 2; AAC63292)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="S -> N (in Ref. 2; AAC63290)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="I -> V (in Ref. 2; AAC63290)"
FT /evidence="ECO:0000305"
FT CONFLICT 304..305
FT /note="SK -> CQ (in Ref. 2; AAC63290)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="D -> G (in Ref. 2; AAC63292)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="I -> T (in Ref. 2; AAC63292)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="M -> L (in Ref. 2; AAC63290/AAC63292)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="T -> NP (in Ref. 2; AAC63290)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="R -> E (in Ref. 2; AAC63290)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="R -> C (in Ref. 2; AAC63292)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="E -> G (in Ref. 2; AAC63290)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="E -> G (in Ref. 2; AAC63290)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="I -> L (in Ref. 2; AAC63290)"
FT /evidence="ECO:0000305"
FT CONFLICT 862
FT /note="G -> R (in Ref. 3; AAO27434)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 969 AA; 109665 MW; D6F8D03A7D6EFC87 CRC64;
NKSRKRRNRV SFLGAATVEP PKPIPLTWKT EKPVWVNQWP LPKQKLEALH LLANEQLEKG
HIEPSFSPWN SPVFVIQKKS GKWRMLTDLR AVNAVIQPMG PLQPGLPSPA MIPKDWPLII
IDLKDCFFTI PLAEQDCEKF AFTIPAINNK EPATRFQWKV LPQGMLNSPT ICQTFVGRAL
QPVREKFSDC YIIHYIDDIL CAAETKDKLI DCYTFLQAEV ANAGLAIASD KIQTSTPFHY
LGMQIENRKI KPQKIEIRKD TLKTLNDFQK LLGDINWIRP TLGIPTYAMS NLFSILRGDS
DLNSKRILTP EATKEIKLVE EKIQSAQINR IDPLAPLQLL IFATAHSPTG IIIQNTDLVE
WSFLPHSTVK TFTLYLDQIA TLIGQTRLRI IKLCGNDPDK IVVPLTKEQV RQAFINSGAW
QIGLANFVGI IDNHYPKTKI FQFLKMTTWI LPKITRREPL ENALTVFTDG SSNGKAAYTG
PKERVIKTPY QSAQRAELVA VITVLQDFDQ PINIISDSAY VVQATRDVET ALIKYSMDDQ
LNQLFNLLQQ TVRKRNFPFY ITHIRAHTNL PGPLTKANEE 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 IGDAKKRAST EMVTPVTWMD NPIEVYVNDS VWVPGPTDDR
CPAKPEEEGM MINISIGYRY PPICLGRAPG CLMPTVQNWL VEVPIVSPIC RFTYHMVSGM
SLRPRVNYL
