ID A0A1Y2VC79_9PEZI Unreviewed; 822 AA.
AC A0A1Y2VC79;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Large ribosomal subunit protein uL30m {ECO:0000256|ARBA:ARBA00035281};
DE EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
GN ORFNames=M434DRAFT_29223 {ECO:0000313|EMBL:OTA95189.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA95189.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA95189.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA95189.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL30 family.
CC {ECO:0000256|ARBA:ARBA00007594, ECO:0000256|RuleBase:RU003734}.
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DR EMBL; KZ112446; OTA95189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2VC79; -.
DR STRING; 1001938.A0A1Y2VC79; -.
DR Proteomes; UP000194361; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd06100; CCL_ACL-C; 1.
DR CDD; cd01658; Ribosomal_L30; 1.
DR Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1.
DR Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.1390.20; Ribosomal protein L30, ferredoxin-like fold domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR InterPro; IPR002020; Citrate_synthase.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR036919; Ribo_uL30_ferredoxin-like_sf.
DR InterPro; IPR005996; Ribosomal_uL30_bac-type.
DR InterPro; IPR018038; Ribosomal_uL30_CS.
DR InterPro; IPR016082; Ribosomal_uL30_ferredoxin-like.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR NCBIfam; TIGR01308; rpmD_bact; 1.
DR PANTHER; PTHR23118; ATP-CITRATE SYNTHASE; 1.
DR PANTHER; PTHR23118:SF42; ATP-CITRATE SYNTHASE; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR Pfam; PF02629; CoA_binding; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR Pfam; PF00327; Ribosomal_L30; 1.
DR SUPFAM; SSF48256; Citrate synthase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55129; Ribosomal protein L30p/L7e; 1.
DR PROSITE; PS00634; RIBOSOMAL_L30; 1.
DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000194361};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU003734};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|RuleBase:RU003734};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 41..146
FT /note="CoA-binding"
FT /evidence="ECO:0000259|Pfam:PF02629"
FT DOMAIN 206..328
FT /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00549"
FT DOMAIN 740..790
FT /note="Large ribosomal subunit protein uL30-like
FT ferredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF00327"
FT REGION 702..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 822 AA; 90150 MW; 88A57643E5AEE15F CRC64;
MASNGVNGAT KGGLSANDNI ARFAAPSRPL SPLPPHALFT NKTRCFVYGL QNRAVQGMLD
FDFICKRQTP SVAGIIYTFG GQFVSKMYWG TSETLLPVYQ ETSKAMAKHP DVDVVVNFAS
SRSVYSSTME LMQYPQIKTI AIIAEGVPER RAREIAHVAR QKGVTIIGPA TVGGIKPGSF
KIGNTGGMMD NIVASKLYRR GSVGYVSKSG GMSNELNNII SQTTDGVYEG IAIGGDRYPG
TTFIDHMLRY QQDPDCKILL LLGEVGGVEE YKVIDAVKQG IITKPIVAWA IGTCASMFKT
EVQFGHAGSF ANSQLETAAM KNKQMKEAGF HVPDTFEDLP NVLASVYQKL VEEKTIVPQP
EPVVPKIPID YSWAQELGLI RKPAAFISTI SDDRGQELLY AGMPISDVFK EDIGIGGVMS
LLWFRRRLPD YASKFLEMVL MLTADHGPAV SGAMNTIITT RAGKDLISSL VSGLLTIGSR
FGGALDGAAE EFTKAADNGL TPREFVDSMR KQNKLIPGIG HRIKSRNNPD LRVELVKEYV
LAKFPSHKLL DYALAVETVT TSKKDNLILN VDGCVAVCFV DLMRSCGAFS PEEAEDYMKM
GVLNGLFVLG RSIGLIAHYL DQKRLRTSLY RHPWDDITYL LPTLSNTGPV ALAFSKFPRP
STNKLYSVKS TQDDETAKSL LRPVERSILS AISFLAGSCP SPIRQTKATD RAPPPFPTPS
FHPHSTKPHK KGRQTDMSFF RVTLHRSAIG LPRRTRGVLA ALGLRKRSQT VFHPVSAQSA
GMILQVKELV KVAEVDRALT PKEMRDERRP EPGFWIEKAV PR
//
