GLYR1_AEDAE
ID GLYR1_AEDAE Reviewed; 559 AA.
AC Q175F8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cytokine-like nuclear factor N-PAC;
DE Short=NPAC;
DE AltName: Full=Glyoxylate reductase 1 homolog;
DE AltName: Full=Nuclear protein NP60 homolog;
DE AltName: Full=Putative oxidoreductase GLYR1 homolog;
GN ORFNames=AAEL006684;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
CC -!- FUNCTION: Nucleosome-destabilizing factor that is recruited to genes
CC during transcriptional activation and colocalizes with a subset of
CC trimethylated 'Lys-36' histone H3 (H3K36me3)-enriched regions.
CC {ECO:0000250|UniProtKB:Q49A26, ECO:0000250|UniProtKB:Q8T079}.
CC -!- SUBUNIT: Binds to mononucleosomes. {ECO:0000250|UniProtKB:Q8T079}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q8T079}.
CC -!- DOMAIN: The PWWP domain is a H3 reader and strongly binds DNA.
CC {ECO:0000250|UniProtKB:Q49A26}.
CC -!- DOMAIN: In the dehydrogenase domain, the conserved NAD(P)H-binding
CC sites and sequence similarity to plant dehydrogenases suggest that this
CC protein may have oxidoreductase activity. However, since the active
CC site is not conserved, the dehydrogenase domain seems to serve as a
CC catalytically inert oligomerization module.
CC {ECO:0000250|UniProtKB:Q49A26}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. NP60 subfamily.
CC {ECO:0000305}.
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DR EMBL; CH477401; EAT41711.1; -; Genomic_DNA.
DR RefSeq; XP_001657934.1; XM_001657884.1.
DR AlphaFoldDB; Q175F8; -.
DR SMR; Q175F8; -.
DR STRING; 7159.AAEL006684-PA; -.
DR VEuPathDB; VectorBase:AAEL006684; -.
DR eggNOG; KOG0409; Eukaryota.
DR HOGENOM; CLU_018075_0_0_1; -.
DR InParanoid; Q175F8; -.
DR OMA; ACDITIS; -.
DR OrthoDB; 885724at2759; -.
DR PhylomeDB; Q175F8; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029154; NADP-bd.
DR InterPro; IPR000313; PWWP_dom.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 3: Inferred from homology;
KW Chromosome; Reference proteome.
FT CHAIN 1..559
FT /note="Cytokine-like nuclear factor N-PAC"
FT /id="PRO_0000312128"
FT DOMAIN 9..70
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 106..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..559
FT /note="Dehydrogenase domain"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT COMPBIAS 108..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 277..291
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT BINDING 511
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
SQ SEQUENCE 559 AA; 60883 MW; 29E56644E0A03110 CRC64;
MTDSKGYAVN DLVWAKMKGF SPWPGRISEP PAELRRITVK KNIPVRCIFF FGSNNYAWIE
ETQIKPYQEF KEKLLSSCKS AGFKEAVQQI EEFIASPENF QHLFASEQDN RPDPDVEFNK
LREGGTESGE ETTVNNTSTP AALESVETTP VTAKKSAAKK KVRASLPIKL HVDKVVVFRS
VAASTTKARA IGNKAKAAAA LNDTSSPKRK RKILNDTAGD VSSLDLDTFS PVRRNVPVSH
LLNRPTVARP ATPEIDMTSV SNALQSRNIQ ASNLKFGFLG LGIMGCGMVK NLLNSGHSVV
VWNRTATKCR KFQEAGAEVA DTPSDVIEMT DVTFSCVADP QVAKELVFGN CGVMSANLVG
KGYVEMTGVD PETSHDIAEQ IIAKGGRYLE AQIQGSKNQA EEGTLIILAA GERLLFEECQ
TCFEAISRNS FYMGDVGNAT KMNLVLQMIS GVMLAGIAEG LALADRAGLQ QKDVLEVLEL
TSMSSELVMQ KGNAIIKGEF PPQQALKHMQ KDLKLALNMA EGLEQPLPIT AASNEVYKHA
KRLGYGSHDS SAVYVRARF
