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Database: UniProt
Entry: D5GKM7_TUBMM
LinkDB: D5GKM7_TUBMM
Original site: D5GKM7_TUBMM 
ID   D5GKM7_TUBMM            Unreviewed;       524 AA.
AC   D5GKM7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Pre-mRNA-processing protein 45 {ECO:0000256|ARBA:ARBA00022160, ECO:0000256|RuleBase:RU367140};
GN   ORFNames=GSTUM_00009646001 {ECO:0000313|EMBL:CAZ85070.1};
OS   Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ85070.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ85070.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ85070.1,
RC   ECO:0000313|Proteomes:UP000006911};
RX   PubMed=20348908; DOI=10.1038/nature08867;
RA   Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA   Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA   Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA   Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA   Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA   Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA   Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA   Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA   Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA   Ottonello S., Wincker P.;
RT   "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT   of symbiosis.";
RL   Nature 464:1033-1038(2010).
CC   -!- FUNCTION: Involved in pre-mRNA splicing.
CC       {ECO:0000256|RuleBase:RU367140}.
CC   -!- SUBUNIT: Associated with the spliceosome.
CC       {ECO:0000256|RuleBase:RU367140}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367140}.
CC   -!- SIMILARITY: Belongs to the SNW family. {ECO:0000256|ARBA:ARBA00010197,
CC       ECO:0000256|RuleBase:RU367140}.
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DR   EMBL; FN430340; CAZ85070.1; -; Genomic_DNA.
DR   RefSeq; XP_002840879.1; XM_002840833.1.
DR   AlphaFoldDB; D5GKM7; -.
DR   STRING; 656061.D5GKM7; -.
DR   EnsemblFungi; CAZ85070; CAZ85070; GSTUM_00009646001.
DR   GeneID; 9184732; -.
DR   KEGG; tml:GSTUM_00009646001; -.
DR   eggNOG; KOG2441; Eukaryota.
DR   HOGENOM; CLU_006601_2_0_1; -.
DR   InParanoid; D5GKM7; -.
DR   OMA; YGQRRGW; -.
DR   OrthoDB; 5490078at2759; -.
DR   Proteomes; UP000006911; Unassembled WGS sequence.
DR   GO; GO:0071014; C:post-mRNA release spliceosomal complex; IEA:EnsemblFungi.
DR   GO; GO:0000974; C:Prp19 complex; IEA:EnsemblFungi.
DR   GO; GO:0060090; F:molecular adaptor activity; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IEA:EnsemblFungi.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:EnsemblFungi.
DR   InterPro; IPR017862; SKI-int_prot_SKIP.
DR   InterPro; IPR004015; SKI-int_prot_SKIP_SNW-dom.
DR   PANTHER; PTHR12096; NUCLEAR PROTEIN SKIP-RELATED; 1.
DR   PANTHER; PTHR12096:SF0; SNW DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF02731; SKIP_SNW; 1.
PE   3: Inferred from homology;
KW   mRNA processing {ECO:0000256|RuleBase:RU367140};
KW   mRNA splicing {ECO:0000256|RuleBase:RU367140};
KW   Nucleus {ECO:0000256|RuleBase:RU367140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW   Spliceosome {ECO:0000256|RuleBase:RU367140}.
FT   DOMAIN          188..345
FT                   /note="SKI-interacting protein SKIP SNW"
FT                   /evidence="ECO:0000259|Pfam:PF02731"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  57856 MW;  64F5E52D8948C65F CRC64;
     MTSLAAGLSK ALPAPKYSAE EDVTASRKPT ARVLGGGDPD QQGLILKRTG PPPYGRRSAW
     RPRSADDFGD GGAFPEVPMA QYPLDMGRKR SGTSKALTLQ VDNEGKVKYD AIARQGHNDK
     RIVHASFKDL IPLRQRADVG EISLERPSEE DVAATTEKTR QALARLVSGA VAAQKPKNVK
     GTNRKDAQYV RYTPSNQLGD TTKRSDKIIK IVERQQDPME PPKFKHKKIP RGPPSPPPPV
     MHSPPRKLTA ADQEAWTIPP PVSNWKNPKG YTVPLDKRLA ADGRGLQDVT INDKFAQFAE
     ALFTADRHAR EEIKQRALMQ QKLAEKEKSQ KEEHLRMLAQ KAREAAHTDS RSDDEARKMQ
     MLAREQGRDI GEKIALGLAK PTQSQETMWD SRLFNQSSAF GAGSGFNEDQ PYDKPLFAAQ
     EAANSIYRPK VSVDDDDEDT ARSEMDRIKR NSRFEVLGKA QQGFRGAADA EARDGPVQFE
     KDAADPFGVE AFVKAAGEKA GTKHGLQERD SSPGGSKRSR ANYM
//
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