ID F0X6C0_CRYPV Unreviewed; 128 AA.
AC F0X6C0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Cgd7_2280 protein {ECO:0000313|EMBL:BAJ78141.1};
GN Name=cgd7_2280 {ECO:0000313|EMBL:BAJ78141.1};
GN ORFNames=CPATCC_003408 {ECO:0000313|EMBL:QOY40545.1};
OS Cryptosporidium parvum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=5807 {ECO:0000313|EMBL:BAJ78141.1};
RN [1] {ECO:0000313|EMBL:BAJ78141.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HNJ-1 {ECO:0000313|EMBL:BAJ78141.1};
RA Yamagishi J., Wakaguri H., Sugano S., Kawano S., Fujisaki K., Sugimoto C.,
RA Watanabe J., Suzuki Y., Kimata I., Xuan X.;
RT "Construction and analysis of full-length cDNA library of Cryptosporidium
RT parvum.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QOY40545.1, ECO:0000313|Proteomes:UP000593906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IOWA-ATCC {ECO:0000313|EMBL:QOY40545.1,
RC ECO:0000313|Proteomes:UP000593906};
RA Baptista R.P., Li Y., Sateriale A., Ansell B., Jex A., Sanders M.,
RA Brooks K., Tracey A., Berriman M., Striepen B., Cotton J.A.,
RA Kissinger J.C.;
RT "Consistent, comparative and evidence-based genome assembly and annotation
RT for Cryptosporidium parvum, C. hominis and C. tyzzeri.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the 60S subunit of the ribosome.
CC {ECO:0000256|ARBA:ARBA00002241}.
CC -!- FUNCTION: Exists either covalently attached to another protein, or free
CC (unanchored). When covalently bound, it is conjugated to target
CC proteins via an isopeptide bond either as a monomer (monoubiquitin), a
CC polymer linked via different Lys residues of the ubiquitin
CC (polyubiquitin chains) or a linear polymer linked via the initiator Met
CC of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains,
CC when attached to a target protein, have different functions depending
CC on the Lys residue of the ubiquitin that is linked: Lys-48-linked is
CC involved in protein degradation via the proteasome. Linear polymer
CC chains formed via attachment by the initiator Met lead to cell
CC signaling. Ubiquitin is usually conjugated to Lys residues of target
CC proteins, however, in rare cases, conjugation to Cys or Ser residues
CC has been observed. When polyubiquitin is free (unanchored-
CC polyubiquitin), it also has distinct roles, such as in activation of
CC protein kinases, and in signaling. {ECO:0000256|ARBA:ARBA00029384}.
CC -!- SUBUNIT: Part of the 60S ribosomal subunit.
CC {ECO:0000256|ARBA:ARBA00035124}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC ribosomal protein eL40 family. {ECO:0000256|ARBA:ARBA00010570}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC {ECO:0000256|ARBA:ARBA00008373}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FX116038; BAJ78141.1; -; mRNA.
DR EMBL; CP044416; QOY40545.1; -; Genomic_DNA.
DR AlphaFoldDB; F0X6C0; -.
DR VEuPathDB; CryptoDB:cgd7_2280; -.
DR VEuPathDB; CryptoDB:CPATCC_0008070; -.
DR Proteomes; UP000593906; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 4.10.1060.50; -; 1.
DR InterPro; IPR001975; Ribosomal_eL40_dom.
DR InterPro; IPR038587; Ribosomal_eL40_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:SF515; POLYUBIQUITIN-B; 1.
DR PANTHER; PTHR10666; UBIQUITIN; 1.
DR Pfam; PF01020; Ribosomal_L40e; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM01377; Ribosomal_L40e; 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 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
SQ SEQUENCE 128 AA; 14667 MW; 52B9313C63B4CE5F CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGVIEP SLANLARQYN CEKMICRKCY ARLPPRATNC RKRKCGRTSQ
IRPKKKLK
//
