ID   NAC_METTM               Reviewed;         117 AA.
AC   P0C0K9; D9PVH7;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Nascent polypeptide-associated complex protein {ECO:0000255|HAMAP-Rule:MF_00814};
GN   Name=nac {ECO:0000255|HAMAP-Rule:MF_00814}; OrderedLocusNames=MTBMA_c06300;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS)
RP   OF 19-117, AND SUBUNIT.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=15665334; DOI=10.1074/jbc.m500160200;
RA   Spreter T., Pech M., Beatrix B.;
RT   "The crystal structure of archaeal nascent polypeptide-associated complex
RT   (NAC) reveals a unique fold and the presence of a ubiquitin-associated
RT   domain.";
RL   J. Biol. Chem. 280:15849-15854(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/jb.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA   Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
CC   -!- FUNCTION: Contacts the emerging nascent chain on the ribosome.
CC       {ECO:0000255|HAMAP-Rule:MF_00814}.
CC   -!- SUBUNIT: Homodimer. Interacts with the ribosome. Binds ribosomal RNA.
CC       {ECO:0000255|HAMAP-Rule:MF_00814, ECO:0000269|PubMed:15665334}.
CC   -!- SIMILARITY: Belongs to the NAC-alpha family. {ECO:0000255|HAMAP-
CC       Rule:MF_00814}.
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DR   EMBL; CP001710; ADL58225.1; -; Genomic_DNA.
DR   RefSeq; WP_013295449.1; NC_014408.1.
DR   PDB; 1TR8; X-ray; 2.27 A; A/B=19-117.
DR   PDBsum; 1TR8; -.
DR   AlphaFoldDB; P0C0K9; -.
DR   SMR; P0C0K9; -.
DR   STRING; 79929.MTBMA_c06300; -.
DR   EnsemblBacteria; ADL58225; ADL58225; MTBMA_c06300.
DR   GeneID; 9704338; -.
DR   KEGG; mmg:MTBMA_c06300; -.
DR   PATRIC; fig|79929.8.peg.614; -.
DR   HOGENOM; CLU_146475_0_0_2; -.
DR   OMA; PRKMKQM; -.
DR   OrthoDB; 105165at2157; -.
DR   EvolutionaryTrace; P0C0K9; -.
DR   Proteomes; UP000000345; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.20.70.30; -; 1.
DR   HAMAP; MF_00814; NAC_arch; 1.
DR   IDEAL; IID90013; -.
DR   InterPro; IPR044034; NAC-like_UBA.
DR   InterPro; IPR038187; NAC_A/B_dom_sf.
DR   InterPro; IPR005231; NAC_arc.
DR   InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR   InterPro; IPR009060; UBA-like_sf.
DR   Pfam; PF19026; HYPK_UBA; 1.
DR   Pfam; PF01849; NAC; 1.
DR   SMART; SM01407; NAC; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   TIGRFAMs; TIGR00264; TIGR00264; 1.
DR   PROSITE; PS51151; NAC_AB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Protein transport; RNA-binding; Transport.
FT   CHAIN           1..117
FT                   /note="Nascent polypeptide-associated complex protein"
FT                   /id="PRO_0000135600"
FT   DOMAIN          9..77
FT                   /note="NAC-A/B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00814"
FT   CONFLICT        41
FT                   /note="K -> R (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50
FT                   /note="R -> K (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55
FT                   /note="D -> E (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71..72
FT                   /note="CD -> RS (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77..78
FT                   /note="VK -> ME (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        81
FT                   /note="D -> E (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        93
FT                   /note="V -> A (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="E -> D (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   STRAND          27..29
FT                   /evidence="ECO:0007829|PDB:1TR8"
FT   STRAND          34..38
FT                   /evidence="ECO:0007829|PDB:1TR8"
FT   STRAND          40..48
FT                   /evidence="ECO:0007829|PDB:1TR8"
FT   STRAND          50..56
FT                   /evidence="ECO:0007829|PDB:1TR8"
FT   STRAND          59..66
FT                   /evidence="ECO:0007829|PDB:1TR8"
FT   STRAND          68..76
FT                   /evidence="ECO:0007829|PDB:1TR8"
FT   HELIX           81..91
FT                   /evidence="ECO:0007829|PDB:1TR8"
FT   HELIX           95..104
FT                   /evidence="ECO:0007829|PDB:1TR8"
FT   TURN            105..107
FT                   /evidence="ECO:0007829|PDB:1TR8"
FT   HELIX           109..115
FT                   /evidence="ECO:0007829|PDB:1TR8"
SQ   SEQUENCE   117 AA;  13242 MW;  EA09DB09F0E785D9 CRC64;
     MIPGMGMNPK QLKQMQRAMK QMGMDMKDLR GVEEVVIKLK KKEIIIKNPR VNVMDFMGQK
     TYQVTGKARE CDLEAEVKIP DDDIELVMNQ TGVSREEATR ALQETGGDLA EAIMRLS