Reviewed, UniProtKB/Swiss-Prot Q9WJR5 (POK3_HUMAN)

Names and origin

Protein names

Recommended name:
    HERV-K_19q12 provirus ancestral Pol protein
Alternative name(s):
    HERV-K(C19) Pol protein
Including the following 3 domains:
    1- Recommended name:
            Reverse transcriptase
                Short name=RT
              EC=2.7.7.49
    2- Recommended name:
            Ribonuclease H
                Short name=RNase H
              EC=3.1.26.4
    3- Recommended name:
            Integrase
                Short name=IN

Gene names

Name:

ERVK6

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	959 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Early post-infection, the reverse transcriptase converts the viral RNA genome into double-stranded viral DNA. The RNase H domain of the reverse transcriptase performs two functions. It degrades the RNA template and specifically removes the RNA primer from the RNA/DNA hybrid. Following nuclear import, the integrase catalyzes the insertion of the linear, double-stranded viral DNA into the host cell chromosome. Endogenous Pol proteins may have kept, lost or modified their original function during evolution.
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). Endonucleolytic cleavage to 5'-phosphomonoester.
Domain	The LPQG and YXDD motifs are catalytically important and conserved among many retroviruses.
Miscellaneous	Exact N-terminus of this protein has not been formally described.
Sequence similarities	Belongs to the beta type-B retroviral polymerase family. HERV class-II K(HML-2) subfamily. Contains 1 integrase catalytic domain. Contains 1 integrase-type DNA-binding domain. Contains 1 integrase-type zinc finger. Contains 1 reverse transcriptase domain. Contains 1 RNase H domain.
Sequence caution	The sequence AC112702 differs from that shown. Reason: Frameshift at position 562. The frameshift results from the integration of a SINE element AluYa5.

Ontologies

Keywords
Biological process	DNA integration DNA recombination
Coding sequence diversity	Ribosomal frameshifting
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Endonuclease Hydrolase Nuclease Nucleotidyltransferase RNA-directed DNA polymerase Transferase
Technical term	Complete proteome ERV Multifunctional enzyme Transposable element
Gene Ontology (GO)
Biological process	DNA integration Inferred from electronic annotation. Source: UniProtKB-KW DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW RNA-dependent DNA replication Inferred from electronic annotation. Source: InterPro
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: InterPro RNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW integrase activity Inferred from electronic annotation. Source: InterPro ribonuclease H activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by ribosomal frameshifting. [Select]

Note: This protein is synthesized as Gag-Pro and Gag-Pro-Pol polyprotein precursors. These polyproteins are thought, by similarity with type-B retroviruses, to be generated by -1 frameshifts occurring at the Gag-Pro and Pro-Pol genes boundaries.

Isoform 1 (identifier: Q9WJR5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 959	959	HERV-K_19q12 provirus ancestral Pol protein		PRO_0000186763
Regions
	Domain	57 – 248	192	Reverse transcriptase
	Domain	464 – 593	130	RNase H
	Domain	645 – 806	162	Integrase catalytic
	Zinc finger	590 – 631	42	Integrase-type
	DNA binding	814 – 862	49	Integrase-type
	Motif	164 – 167	4	LPQG
	Motif	198 – 201	4	YXDD
Experimental info
	Sequence conflict	15	1	A → V in AC112702. Ref.2
	Sequence conflict	208	1	M → T in AC112702. Ref.2
	Sequence conflict	245	1	E → G in AC112702. Ref.2
	Sequence conflict	339	1	P → T in AC112702. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 13, 2004. Version 2. Checksum: 60276896681286A9	FASTA	959	108,106
	10 20 30 40 50 60 NKSKKRRNRV SFLGAATVEP PKPIPLTWKT EKPVWVNQWP LPKQKLEALH LLANEQLEKG 70 80 90 100 110 120 HIEPSFSPWN SPVFVIQKKS GKWRMLTDLR AVNAVNAVIQ PMGPLQPGLP SLAMIPKDWP 130 140 150 160 170 180 LIIIDLKDCF FTIPLAEQDC EKFAFTIPAI NNKEPATRFQ WKVLPQGMLN SPTICQTFVG 190 200 210 220 230 240 RALQPVREKF SDCYIIHYID DILCAAEMKD KLIDCYTFLQ AEVANAGLAI ASDKIQTSTP 250 260 270 280 290 300 FHYLEMQIEN RKIKPPKIEI RKDTLKTLND FQKLLGDINW IRPTLGIPTY AMSNLFSILR 310 320 330 340 350 360 GDSDLNSKRM LTPEATKEIK LVEEKIQSAQ INRIDPLAPL QLLIFATAHS PTGIIIQNTD 370 380 390 400 410 420 LVEWSFLPHS TVKTFTLYLD QMATLIGQTR LRIIKLCGND PDKIVVPLTK EQVRQAFINS 430 440 450 460 470 480 GAWQIGLANF VGIIDNHYPK TKIFQFLKMT TWILPKITRR EPLENALTVF TDGSSNGKAA 490 500 510 520 530 540 YTGPKERVIK TQYQSAQRAE LVAVITVLQD FDQPINIISD SAYVVQATRD VETALIKYSM 550 560 570 580 590 600 DDQLNQLFNL LQQTVRKRNF PFYITHIRAH TNLPGPLTKA NEQADLLVSS ALIKAQELHA 610 620 630 640 650 660 LTHVNVAGLK NKFDVTWKQA KDIVQHCTQC QVLHLPTQEA GVNPRGLCPN ALWQMDVTHV 670 680 690 700 710 720 SSFGRLSYIH VTVDTYSHFI WATCQTGEST SHVKKHLLSC FAVMGVPEKI KTDNGPGYCS 730 740 750 760 770 780 KAFQKFLSQW KISHTTGIPY NSQGQAIVER TNRTLKTQLV KQKEGGDSKE CTTPQMQLNL 790 800 810 820 830 840 ALYTLNFLNI YRNQTTTSAE QHLTGKKNSP HEGKLIWWKD NKNKTWEIGK VITWGRGFAC 850 860 870 880 890 900 VSPGENQLPV WIPTRHLKFY NEPIGDAKKS TSAETETPQS STVDSQDEQN GDVRRTDEVA 910 920 930 940 950 IHQESRAADL GTTKEADAVS YKISREHKGD TNPREYAACG LDDCINGGKS PYACRSSCS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome wide screening, cloning, chromosomal assignment and expression of full-length human endogenous retrovirus type K (HERV-K)." Toenjes R.R., Czauderna F., Kurth R. J. Virol. 73:9187-9195(1999) [PubMed: 10516026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Evolutionary relationships within a subgroup of HERV-K-related human endogenous retroviruses." Zsiros J., Jebbink M.F., Lukashov V.V., Voute P.A., Berkhout B. J. Gen. Virol. 79:61-70(1998) [PubMed: 9460924] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 75-275. Tissue: Bone marrow.

Web resources

Human Endogenous Retrovirus Database (HERVd)

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y17833 Genomic DNA. Translation: CAA76882.1. Different initiation. AC112702 Genomic DNA. No translation available. U87592 mRNA. Translation: AAB63115.1.
IPI	IPI00456600.
3D structure databases
SMR	Q9WJR5. Positions 23-426, 592-632, 646-788.
ModBase	Search...
Proteomic databases
PRIDE	Q9WJR5.
Organism-specific databases
GeneCards	GC07U990291.
HGNC	HGNC:13915. ERVK6.
MIM	605626. gene.
GenAtlas	Search...
Phylogenomic databases
eggNOG	maNOG23829.
HOVERGEN	Q9WJR5.
Enzyme and pathway databases
BRENDA	2.7.7.49. 247. 3.1.26.4. 247.
Gene expression databases
Genevestigator	Q9WJR5.
Family and domain databases
InterPro	IPR001037. Integrase_C_retrovir. IPR001584. Integrase_cat-core. IPR003308. Integrase_Zn-bd_dom_N. IPR012337. PolynucTfrase_RNaseH_fold. IPR000477. Reverse_transcriptase. IPR002156. RNase_H. IPR010661. RVT_thumb. [Graphical view]
Pfam	PF00552. Integrase. 1 hit. PF02022. Integrase_Zn. 1 hit. PF00075. RnaseH. 1 hit. PF00665. rve. 1 hit. PF00078. RVT_1. 1 hit. PF06817. RVT_thumb. 1 hit. [Graphical view]
PROSITE	PS50994. INTEGRASE. 1 hit. PS51027. INTEGRASE_DBD. 1 hit. PS50879. RNASE_H. 1 hit. PS50878. RT_POL. 1 hit. PS50876. ZF_INTEGRASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

POK3_HUMAN

Accession

Primary (citable) accession number: Q9WJR5
Secondary accession number(s): O15312

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	September 13, 2004
Last modified:	January 19, 2010
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.