ID K1X017_MARBU Unreviewed; 314 AA.
AC K1X017;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Putative ubiquitin / ribosomal protein S27a {ECO:0000313|EMBL:EKD14218.1};
GN ORFNames=MBM_07448 {ECO:0000313|EMBL:EKD14218.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD14218.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD14218.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD14218.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC ribosomal protein eS31 family. {ECO:0000256|ARBA:ARBA00009891}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC {ECO:0000256|ARBA:ARBA00008373}.
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DR EMBL; JH921446; EKD14218.1; -; Genomic_DNA.
DR RefSeq; XP_007295337.1; XM_007295275.1.
DR AlphaFoldDB; K1X017; -.
DR STRING; 1072389.K1X017; -.
DR GeneID; 18763383; -.
DR KEGG; mbe:MBM_07448; -.
DR eggNOG; KOG0004; Eukaryota.
DR HOGENOM; CLU_885893_0_0_1; -.
DR InParanoid; K1X017; -.
DR OrthoDB; 312211at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd01803; Ubl_ubiquitin; 1.
DR Gene3D; 6.20.50.150; -; 1.
DR InterPro; IPR002906; Ribosomal_eS31.
DR InterPro; IPR038582; Ribosomal_eS31_euk-type_sf.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR PANTHER; PTHR10666; UBIQUITIN; 1.
DR PANTHER; PTHR10666:SF480; UBIQUITIN-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01599; Ribosomal_S27; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM01402; Ribosomal_S27; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000313|EMBL:EKD14218.1}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 159..234
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
SQ SEQUENCE 314 AA; 35384 MW; 793910047F5D1123 CRC64;
MANPRPGTIL KLLLVFAGAI LAWHRDKSIT GVFESVVVVI VVIVVGLVED LIFPNLFPTD
LQGYFILLPG RRVELRLATS SSSLVGLVIV RRLTTLELER ASGRARKPLF SISFASRSSS
PQKTRQLDCK DTNSSLVRYV LRQLLSTEHW KLTLAQAIMQ IFVKTLTGKT ITLEVESSDT
IDNVKSKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR LRGGMAKKRK
KKVYTTPKKI KHKRKKTKLA VLKYYKVDGD GTIERLRREC PTPDCGAGVF MAAMHDRQYC
GRCHLTYIFE DAGK
//
