ID G0SWQ5_RHOT2 Unreviewed; 674 AA.
AC G0SWQ5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Spindle pole body protein {ECO:0000313|EMBL:EGU12979.1};
GN ORFNames=RTG_01020 {ECO:0000313|EMBL:EGU12979.1};
OS Rhodosporidium toruloides (strain ATCC 204091 / IIP 30 / MTCC 1151) (Yeast)
OS (Rhodotorula glutinis (strain ATCC 204091)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1001064 {ECO:0000313|EMBL:EGU12979.1, ECO:0000313|Proteomes:UP000006141};
RN [1] {ECO:0000313|EMBL:EGU12979.1, ECO:0000313|Proteomes:UP000006141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204091 / IIP 30 / MTCC 1151
RC {ECO:0000313|Proteomes:UP000006141};
RX PubMed=24526636; DOI=10.1128/genomeA.00046-14;
RA Paul D., Magbanua Z., Arick M.II., French T., Bridges S.M., Burgess S.C.,
RA Lawrence M.L.;
RT "Genome sequence of the oleaginous yeast Rhodotorula glutinis ATCC
RT 204091.";
RL Genome Announc. 2:E0004614-E0004614(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:EGU12979.1}.
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DR EMBL; AEVR02000008; EGU12979.1; -; Genomic_DNA.
DR AlphaFoldDB; G0SWQ5; -.
DR MEROPS; C19.972; -.
DR HOGENOM; CLU_016848_2_1_1; -.
DR InParanoid; G0SWQ5; -.
DR Proteomes; UP000006141; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR CDD; cd02669; Peptidase_C19M; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR033809; USP39.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646:SF16; U4_U6.U5 TRI-SNRNP-ASSOCIATED PROTEIN 2; 1.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00513; SAP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006141};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 176..273
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 298..633
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 49..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 74435 MW; FA165FA9D35A846E CRC64;
MATQYSKLKV AELKATYTDE HHTKQELLKE RDLPVSGLKA DLVARLAESD AASPATAKPA
DQPAPIADIP DADAAVETVA DGGKEGNEAG GMGDSLPSTD GLNLAAKRAL EDEAVEEEVK
RVKRDEEMAD AVPPAAEKDS ALPPPAPAPT FDSAPALGGD LPNRSLALKE EDGGRPADLY
LDTINRAALD FDFERLCSVT LSHNHIYACL VCGKYFQGRG KSTPAYAHAL NEDHHVYINL
DTRKVYVLPD GYEVDDASLA DIKYLLYPTF TPQMLEKIDH QTQPELDLAR KEYYPGFVGL
NNMKHNSYMN AVLQLLLHVP PLRDYLILQL DPSSTSSRPT SELTTRLGLL ARKLWNPHAF
KSQVSPHEFL QEVANASGGK FKITEQGDPL EFLKWLLNQV HRDLGGGRKP RSSIVYSAFQ
GEVRVDDQQI IKTGEFGTKP KFDIDREIKS TKTPFLFLAL DLPPPPLFQD AVETNIIPQV
PISAVLSKYD GSTTREDTQA GVLKRSKITR LPPFLIVYYK RFLSNRFLEE KNPTIVNFPL
KGVDMSEYVD SAETLAAHYD LTANLSLQSS TSTGTTATSP SAEWKVHVHL RNAEKGKEDE
GEKWFEVQDL NVREIEKGMV PLAETYIQIW ERRTPNGKWD DLVKVDPPKS HKAKAGGAPQ
ANGKKAEKPA PAAK
//
