PIWI_ARCFU
ID PIWI_ARCFU Reviewed; 427 AA.
AC O28951;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Piwi protein AF_1318;
DE AltName: Full=AfAgo {ECO:0000305};
DE AltName: Full=AfPiwi {ECO:0000303|PubMed:15565169};
DE AltName: Full=PIWI/MID domain protein {ECO:0000303|PubMed:19187762};
GN OrderedLocusNames=AF_1318;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2] {ECO:0007744|PDB:1W9H}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), RNA-BINDING, AND MUTAGENESIS OF
RP LEU-427.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=15565169; DOI=10.1038/sj.emboj.7600488;
RA Parker J.S., Roe S.M., Barford D.;
RT "Crystal structure of a PIWI protein suggests mechanisms for siRNA
RT recognition and slicer activity.";
RL EMBO J. 23:4727-4737(2004).
RN [3] {ECO:0007744|PDB:2BGG}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN A COMPLEX WITH SIRNA DUPLEX AND
RP METAL, COFACTOR, AND RNA-BINDING.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=15800628; DOI=10.1038/nature03462;
RA Parker J.S., Roe S.M., Barford D.;
RT "Structural insights into mRNA recognition from a PIWI domain-siRNA guide
RT complex.";
RL Nature 434:663-666(2005).
RN [4] {ECO:0007744|PDB:1YTU}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN A COMPLEX WITH SIRNA DUPLEX AND
RP METAL, COFACTOR, DNA-BINDING, RNA-BINDING, AND MUTAGENESIS OF TYR-123;
RP LYS-127; GLN-137 AND LYS-163.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=15800629; DOI=10.1038/nature03514;
RA Ma J.-B., Yuan Y.-R., Meister G., Pei Y., Tuschl T., Patel D.J.;
RT "Structural basis for 5'-end-specific recognition of guide RNA by the A.
RT fulgidus Piwi protein.";
RL Nature 434:666-670(2005).
RN [5] {ECO:0007744|PDB:2W42}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH DUPLEX DNA AND
RP METAL, COFACTOR, DNA-BINDING, AND RNA-BINDING.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=19187762; DOI=10.1016/j.molcel.2008.12.012;
RA Parker J.S., Parizotto E.A., Wang M., Roe S.M., Barford D.;
RT "Enhancement of the seed-target recognition step in RNA silencing by a
RT PIWI/MID domain protein.";
RL Mol. Cell 33:204-214(2009).
CC -!- FUNCTION: Might play a role in defense against invading genetic
CC elements, using short DNA sequences as guides to bind complementary
CC target strands, resulting in slicing of the target nucleic acid (By
CC similarity). Binds nucleic acids with decreasing affinity in the
CC following order; ssDNA, ssRNA, dsDNA, RNA-DNA, RNA-RNA
CC (PubMed:15800629). Association of the 5' seed region of the guide
CC strand (nucleotides 2-7) with AfPiwi increases affinity for the
CC corresponding target strand; the greatest increase in affinity is for
CC guide DNA with target RNA (PubMed:19187762).
CC {ECO:0000250|UniProtKB:Q58717, ECO:0000269|PubMed:15800629,
CC ECO:0000269|PubMed:19187762}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:15800628, ECO:0000269|PubMed:15800629,
CC ECO:0000269|PubMed:19187762};
CC Note=Other ligands are provided by nucleic acid (PubMed:15800628,
CC PubMed:15800629, PubMed:19187762). {ECO:0000269|PubMed:15800628,
CC ECO:0000269|PubMed:15800629, ECO:0000269|PubMed:19187762};
CC -!- MISCELLANEOUS: This is missing the N-terminal and PAZ domains compared
CC to other prokaryotic argonaute proteins. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the argonaute family. Short pAgo subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Despite its similarity to eukaryotic argonaute proteins this
CC protein is probably not involved in RNA-mediated gene silencing (RNAi),
CC as that process is not known to exist in prokaryotes. {ECO:0000305}.
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DR EMBL; AE000782; AAB89939.1; -; Genomic_DNA.
DR PIR; E69414; E69414.
DR PDB; 1W9H; X-ray; 1.95 A; A=1-427.
DR PDB; 1YTU; X-ray; 2.50 A; A/B=1-427.
DR PDB; 2BGG; X-ray; 2.20 A; A/B=1-427.
DR PDB; 2W42; X-ray; 1.90 A; A/B=1-427.
DR PDB; 6T5T; X-ray; 1.70 A; A=1-427.
DR PDB; 6TUO; X-ray; 1.80 A; A=1-427.
DR PDB; 6XU0; X-ray; 1.90 A; A/B=1-427.
DR PDB; 6XUP; X-ray; 1.90 A; A/B=1-427.
DR PDBsum; 1W9H; -.
DR PDBsum; 1YTU; -.
DR PDBsum; 2BGG; -.
DR PDBsum; 2W42; -.
DR PDBsum; 6T5T; -.
DR PDBsum; 6TUO; -.
DR PDBsum; 6XU0; -.
DR PDBsum; 6XUP; -.
DR AlphaFoldDB; O28951; -.
DR SASBDB; O28951; -.
DR SMR; O28951; -.
DR IntAct; O28951; 1.
DR EnsemblBacteria; AAB89939; AAB89939; AF_1318.
DR KEGG; afu:AF_1318; -.
DR eggNOG; arCOG03890; Archaea.
DR HOGENOM; CLU_643412_0_0_2; -.
DR EvolutionaryTrace; O28951; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR003165; Piwi.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF02171; Piwi; 1.
DR SMART; SM00950; Piwi; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50822; PIWI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Metal-binding; Reference proteome; RNA-binding.
FT CHAIN 1..427
FT /note="Piwi protein AF_1318"
FT /id="PRO_0000378146"
FT DOMAIN 110..406
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 118..124
FT /note="Binds 5'-phosphorylated end of guide DNA"
FT /evidence="ECO:0000269|PubMed:19187762,
FT ECO:0007744|PDB:2W42"
FT REGION 147..148
FT /note="Binds target DNA"
FT /evidence="ECO:0000269|PubMed:19187762,
FT ECO:0007744|PDB:2W42"
FT REGION 150..155
FT /note="Binds guide DNA"
FT /evidence="ECO:0000269|PubMed:19187762,
FT ECO:0007744|PDB:2W42"
FT BINDING 159
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0007744|PDB:1YTU, ECO:0007744|PDB:2BGG,
FT ECO:0007744|PDB:2W42"
FT BINDING 427
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0007744|PDB:1YTU, ECO:0007744|PDB:2BGG,
FT ECO:0007744|PDB:2W42"
FT MUTAGEN 123
FT /note="Y->A: Reduced binding affinity for siRNA."
FT /evidence="ECO:0000269|PubMed:15800629"
FT MUTAGEN 127
FT /note="K->A: Reduced binding affinity for siRNA."
FT /evidence="ECO:0000269|PubMed:15800629"
FT MUTAGEN 137
FT /note="Q->A: Reduced binding affinity for siRNA."
FT /evidence="ECO:0000269|PubMed:15800629"
FT MUTAGEN 163
FT /note="K->A: Reduced binding affinity for siRNA."
FT /evidence="ECO:0000269|PubMed:15800629"
FT MUTAGEN 427
FT /note="L->LG: Reduced binding to siRNA."
FT /evidence="ECO:0000269|PubMed:15565169"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1YTU"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6T5T"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:6TUO"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:6T5T"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:6T5T"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:6T5T"
FT HELIX 59..74
FT /evidence="ECO:0007829|PDB:6T5T"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:6T5T"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:6T5T"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:6T5T"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:6T5T"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:6T5T"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:6T5T"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:6T5T"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:2W42"
FT HELIX 149..163
FT /evidence="ECO:0007829|PDB:6T5T"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6TUO"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1W9H"
FT STRAND 180..202
FT /evidence="ECO:0007829|PDB:6T5T"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:6T5T"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:6T5T"
FT HELIX 222..240
FT /evidence="ECO:0007829|PDB:6T5T"
FT STRAND 248..256
FT /evidence="ECO:0007829|PDB:6T5T"
FT HELIX 261..277
FT /evidence="ECO:0007829|PDB:6T5T"
FT STRAND 286..294
FT /evidence="ECO:0007829|PDB:6T5T"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:6T5T"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:1YTU"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:6TUO"
FT STRAND 315..325
FT /evidence="ECO:0007829|PDB:6T5T"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:1YTU"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:1YTU"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:6T5T"
FT STRAND 346..353
FT /evidence="ECO:0007829|PDB:6T5T"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:6T5T"
FT HELIX 360..374
FT /evidence="ECO:0007829|PDB:6T5T"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:6T5T"
FT HELIX 389..406
FT /evidence="ECO:0007829|PDB:6T5T"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:2BGG"
FT HELIX 418..422
FT /evidence="ECO:0007829|PDB:6T5T"
SQ SEQUENCE 427 AA; 49244 MW; F925081F3AFB47CD CRC64;
MMEYKIVENG LTYRIGNGAS VPISNTGELI KGLRNYGPYE VPSLKYNQIA LIHNNQFSSL
INQLKSQISS KIDEVWHIHN INISEFIYDS PHFDSIKSQV DNAIDTGVDG IMLVLPEYNT
PLYYKLKSYL INSIPSQFMR YDILSNRNLT FYVDNLLVQF VSKLGGKPWI LNVDPEKGSD
IIIGTGATRI DNVNLFCFAM VFKKDGTMLW NEISPIVTSS EYLTYLKSTI KKVVYGFKKS
NPDWDVEKLT LHVSGKRPKM KDGETKILKE TVEELKKQEM VSRDVKYAIL HLNETHPFWV
MGDPNNRFHP YEGTKVKLSS KRYLLTLLQP YLKRNGLEMV TPIKPLSVEI VSDNWTSEEY
YHNVHEILDE IYYLSKMNWR GFRSRNLPVT VNYPKLVAGI IANVNRYGGY PINPEGNRSL
QTNPWFL
