ALBA2_AERPE
ID ALBA2_AERPE Reviewed; 102 AA.
AC Q9YAX2;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=DNA/RNA-binding protein Alba 2;
GN Name=albA2; OrderedLocusNames=APE_1823;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
CC -!- FUNCTION: Binds double-stranded DNA tightly but without sequence
CC specificity. It is distributed uniformly and abundantly on the
CC chromosome, suggesting a role in chromatin architecture. However, it
CC does not significantly compact DNA. Binds rRNA and mRNA in vivo. May
CC play a role in maintaining the structural and functional stability of
CC RNA, and, perhaps, ribosomes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome
CC {ECO:0000250}.
CC -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase may
CC regulate its activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone-like Alba family. {ECO:0000305}.
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DR EMBL; BA000002; BAA80826.1; -; Genomic_DNA.
DR PIR; E72567; E72567.
DR PDB; 2H9U; X-ray; 2.00 A; A=1-102.
DR PDB; 3U6Y; X-ray; 2.00 A; A/C=1-102.
DR PDBsum; 2H9U; -.
DR PDBsum; 3U6Y; -.
DR AlphaFoldDB; Q9YAX2; -.
DR SMR; Q9YAX2; -.
DR STRING; 272557.APE_1823; -.
DR EnsemblBacteria; BAA80826; BAA80826; APE_1823.
DR KEGG; ape:APE_1823; -.
DR eggNOG; arCOG01753; Archaea.
DR OMA; QFNEGAK; -.
DR EvolutionaryTrace; Q9YAX2; -.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.110.20; -; 1.
DR HAMAP; MF_01122; AlbA; 1.
DR InterPro; IPR036882; Alba-like_dom_sf.
DR InterPro; IPR013795; DNA/RNA-bd_Alba.
DR InterPro; IPR002775; DNA/RNA-bd_Alba-like.
DR Pfam; PF01918; Alba; 1.
DR PIRSF; PIRSF028732; Alba; 1.
DR SUPFAM; SSF82704; SSF82704; 1.
DR TIGRFAMs; TIGR00285; TIGR00285; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; Cytoplasm; DNA-binding;
KW Reference proteome; RNA-binding.
FT CHAIN 1..102
FT /note="DNA/RNA-binding protein Alba 2"
FT /id="PRO_0000151695"
FT MOD_RES 14
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2H9U"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:2H9U"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:2H9U"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:2H9U"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:2H9U"
FT STRAND 62..77
FT /evidence="ECO:0007829|PDB:2H9U"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:3U6Y"
FT STRAND 83..97
FT /evidence="ECO:0007829|PDB:2H9U"
SQ SEQUENCE 102 AA; 11380 MW; F3F5103D9E775D10 CRC64;
MACEGAPEVR IGRKPVMNYV LAILTTLMEQ GTNQVVVKAR GRNINRAVDA VEIVRKRFAK
NIEIKDIKID SQEIEVQTPE GQTRTRRVSS IEICLEKAGE SA