POK25_HUMAN
ID POK25_HUMAN Reviewed; 954 AA.
AC P63136;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Endogenous retrovirus group K member 25 Pol protein;
DE AltName: Full=HERV-K_11q22.1 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-25;
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].
RA Hattori M., Ishii K., Toyoda A., Taylor T.D., Hong-Seog P., Fujiyama A.,
RA Yada T., Totoki Y., Watanabe H., Sakaki Y.;
RL Submitted (NOV-1999) 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 -!- 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 -!- 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; AP000776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P63136; -.
DR SMR; P63136; -.
DR GlyGen; P63136; 2 sites.
DR BioMuta; HGNC:39039; -.
DR DMDM; 52000774; -.
DR MassIVE; P63136; -.
DR PeptideAtlas; P63136; -.
DR PRIDE; P63136; -.
DR GeneCards; ERVK-25; -.
DR HGNC; HGNC:39039; ERVK-25.
DR neXtProt; NX_P63136; -.
DR PhylomeDB; P63136; -.
DR Pharos; P63136; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P63136; 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 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..954
FT /note="Endogenous retrovirus group K member 25 Pol protein"
FT /id="PRO_0000186772"
FT DOMAIN 57..245
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 460..588
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 640..801
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 585..626
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 809..857
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 862..888
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 868..882
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 515
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 580
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 594
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 598
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 622
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 625
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
SQ SEQUENCE 954 AA; 107472 MW; 545C6BCD401CB4C1 CRC64;
NKSKKRRNRV 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 TLKALNDFQK LLGDINWIRP TLGIPTYAMS NLFSILRGDS
DLNSKRMLTP EATKEIKLVE EKIQSAQINR IDPLAPLQLL IFATAHSPTG IIIQNTDLVE
WSFLPHSTVK TFTLYLDQIA TLIGQTRLRI IKLCGNDPDK IVVPLTKEQV RQAFINSGAW
QIGLANFVGI IDNHYPKTKI FQFLKLTTWI LPKITRREPL ENALTVFTDG SSNGKAAYTG
PKERVIKTPY QSAQRAELVA VITVLQDFDI NIISDSAYVV QATRDVETAL IKYSMDDQLN
QLFNLLQQTV RKRNFPFYIT HIRAHTNLPG PLTKANKQAD LLVSSALIKA QELHALTHVN
AAGLKNKFDV TWKLAKDIVQ HCTQCQVLHL PTQEAGVNPR GLCPNALWQM DVTHVPSFGR
LSYVHVTVDT YSHFIWATCH TGESTSHVKK HLLSCFAVMG VPEKIKTDNG PGYCSKAFQK
FLSQWKISHT TGIPYNSQGQ AIVERTNRTL KTQLVKQKEG GDSKECTTPQ MQLNLALYTL
NFLNIYRNQT TTSAEQHLTG KKNSPHEGKL IWWKDNKNKT WEIGKVITWG RGFACVSPGE
NQLPVWIPTR HLKFYNEPIR DAKKSTSAET ETPQSSTVDS QDEQNGDVRR TDEVAIHQEG
RAANLGTTKE ADAVSYKISR EHKGDTNPRE YAACSLDDCI NGGKSPYACR SSCS
