ID C0NU76_AJECG Unreviewed; 735 AA.
AC C0NU76;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=AMP dependent synthetase and ligase {ECO:0000313|EMBL:EEH04956.1};
GN ORFNames=HCBG_06907 {ECO:0000313|EMBL:EEH04956.1};
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH04956.1, ECO:0000313|Proteomes:UP000001631};
RN [1] {ECO:0000313|Proteomes:UP000001631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC {ECO:0000313|Proteomes:UP000001631};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. {ECO:0000256|ARBA:ARBA00004021}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL13 family.
CC {ECO:0000256|ARBA:ARBA00006227, ECO:0000256|RuleBase:RU003877}.
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DR EMBL; GG663372; EEH04956.1; -; Genomic_DNA.
DR AlphaFoldDB; C0NU76; -.
DR STRING; 447093.C0NU76; -.
DR VEuPathDB; FungiDB:I7I50_12254; -.
DR VEuPathDB; FungiDB:I7I50_12255; -.
DR HOGENOM; CLU_000022_59_5_1; -.
DR InParanoid; C0NU76; -.
DR OrthoDB; 2596785at2759; -.
DR Proteomes; UP000001631; Unassembled WGS sequence.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd00392; Ribosomal_L13; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 6.10.250.3250; -; 1.
DR Gene3D; 3.90.1180.10; Ribosomal protein L13; 1.
DR HAMAP; MF_01366; Ribosomal_L13; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR005822; Ribosomal_uL13.
DR InterPro; IPR023563; Ribosomal_uL13_CS.
DR InterPro; IPR005755; Ribosomal_uL13_euk/arc.
DR InterPro; IPR036899; Ribosomal_uL13_sf.
DR NCBIfam; TIGR01077; L13_A_E; 1.
DR PANTHER; PTHR43859; ACYL-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR43859:SF4; BUTANOATE--COA LIGASE AAE1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00572; Ribosomal_L13; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF52161; Ribosomal protein L13; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS00783; RIBOSOMAL_L13; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:EEH04956.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001631};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU003877};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|RuleBase:RU003877}.
FT DOMAIN 222..590
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 641..717
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 735 AA; 82140 MW; 667F9B89B7DE9472 CRC64;
MSTFEPVVVI DGKGHLLGRL ASIVAKQLLN GQKIVVVRCE ALNISGEFFR AKLKYHAYLR
KITRFNPTRG GPFHFRAPSR IFYKAVRGMI PHKSARGAAA MERLKVFEGV PPPYDKKKRV
VVPQALRVLR LKPGRKYCTV GRLSHEVGWK YQDVVARLEE RRKVKGSAYY ERKKAARRQL
VQAQKTANVD QKTKTQLAEG GQLWRLKAQA IYHVTTNNKV LRRSYIETAD RARGFAYYLK
RHGFKRVGIL CPNTPAFLES IFAIAAAGAV NVAVNYRLKP EDISYIFNHS EVDAIVVDEE
FVPLLNEFKK QNGHVPLIID TDTDAVEGEL SGPFDQAVLE GLHFDASSGN RGWQGLEAQT
PDEDVLIALA YTSGTTSRPK GVEYIHRGCY LAALANVIES GLNFNQGRCR YLWTLPMFHA
MGWTFPWAVT AARGTHYCLR KVDYSLIWRL LKEEGVTHYC AAPTVNTVLC NSKEAEVLPS
PVRVTVAASP PTPHLFEQMA KLNLQPVHVY GLTETYGPIT KGYYLPQWDT IPAEDKYKKM
ARQGHGFLTS LPVRVIKTDV PEGTIIDVEK NGEETGEVVF VGNICAKGYY KNVDDTKKLF
SGGVLHSGDL AVWHPDGAIQ ILDRAKDIII SGGENISSVA LESMLATHPD VFEVGVVAVP
DSHWGERPKA FITVRDGKKL DGKDVIEWAK HVGGISRFMV PREVEAVREL PKTSTGKVKK
NVLRRWAKGT DRSLE
//
