ID A0A0E9NQD1_SAICN Unreviewed; 676 AA.
AC A0A0E9NQD1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=SWIM-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=G7K_5967-t1 {ECO:0000313|EMBL:GAO51876.1};
OS Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS / NRRL Y-17804).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Taphrinomycotina incertae sedis; Saitoella.
OX NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO51876.1, ECO:0000313|Proteomes:UP000033140};
RN [1] {ECO:0000313|EMBL:GAO51876.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO51876.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=21914972; DOI=10.2323/jgam.57.243;
RA Nishida H., Hamamoto M., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL J. Gen. Appl. Microbiol. 57:243-246(2011).
RN [2] {ECO:0000313|EMBL:GAO51876.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO51876.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=24646756; DOI=10.2323/jgam.60.7;
RA Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT "The early diverging ascomycetous budding yeast Saitoella complicata has
RT three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT lineages.";
RL J. Gen. Appl. Microbiol. 60:7-12(2014).
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000256|ARBA:ARBA00010531}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAO51876.1}.
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DR EMBL; BACD03000054; GAO51876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E9NQD1; -.
DR STRING; 698492.A0A0E9NQD1; -.
DR Proteomes; UP000033140; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00403; Ribosomal_L1; 1.
DR CDD; cd16494; RING-CH-C4HC3_ZSWM2; 1.
DR Gene3D; 3.30.190.20; -; 1.
DR Gene3D; 3.40.50.790; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR023674; Ribosomal_uL1-like.
DR InterPro; IPR028364; Ribosomal_uL1/biogenesis.
DR InterPro; IPR016095; Ribosomal_uL1_3-a/b-sand.
DR InterPro; IPR023673; Ribosomal_uL1_CS.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR007527; Znf_SWIM.
DR InterPro; IPR039903; Zswim2.
DR PANTHER; PTHR21540:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZSWIM2; 1.
DR PANTHER; PTHR21540; RING FINGER AND SWIM DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF00687; Ribosomal_L1; 1.
DR Pfam; PF04434; SWIM; 1.
DR SUPFAM; SSF56808; Ribosomal protein L1; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS01199; RIBOSOMAL_L1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000033140};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 216..256
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 345..398
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..139
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 676 AA; 74760 MW; BD973A1C35FF28C8 CRC64;
MTAIQASSAT GTAMAARAPS TRKRKTPVKY EEEQSSDLEA RAAPVKRTRR VQVKKEEAED
TDLVSAPVAK KARGRPRKVK SEIKEEESME TTPALPEVKT EETASTRRTR SRKPKDELHQ
LLSLPPPPTK KPRTKKPAPP APDLSAYLSY PPTLLPTFLP PHVRDRPTPF LRHCPPAVES
RIARVISQRL FLVHTELPSS SNYAIFHVLG STGNVYLTTL QQRPHCTCPD YAFSGRRRDG
RGVMCKHVLF VLVKVCKVRG ALCWQSGFGR EEVEGMVEGL RGRAREGDEA GIRVSREVRE
FYLGRETTPE GGVVKSEVKS EEGRAEEEGV EVHNGAHRKP LTGDCPICYE DLSSSTPSPS
STVWCKAACG NNIHAECFGE WAKSLKRSSK SVTCVYCRTE WVGPENEKKK GSGRGRGGSA
VVGNGRVVRN GGWSASAGVY CRFLVQHQHS RSIHQFRQVK MSKVSVSSVR ENIQNLLAAS
EEKKRNFTET IELQIGLKNY DPQRDKRFSG TVRLPNVPRP NMALCILGDA HDIDRAKNGG
IDAMSVDDLK KLNKNKKLVK KLAKKYDAFI ASEVLIKQIP RLLGPGLSKA GKFPTPVSHA
DNLGDRVTEV KSTVKFQLKK VLCLGVAVGN VGMTEDELVA NIMLSINFLV SLLKKAWQNV
GSLVIKSSMG KPFRLY
//
