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SQS1_LODEL
ID   SQS1_LODEL              Reviewed;         792 AA.
AC   A5DSB5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Protein SQS1;
GN   Name=SQS1; ORFNames=LELG_00251;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: May be involved in splicing. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SQS1 family. {ECO:0000305}.
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DR   EMBL; CH981524; EDK42073.1; -; Genomic_DNA.
DR   RefSeq; XP_001527731.1; XM_001527681.1.
DR   AlphaFoldDB; A5DSB5; -.
DR   SMR; A5DSB5; -.
DR   STRING; 379508.A5DSB5; -.
DR   EnsemblFungi; EDK42073; EDK42073; LELG_00251.
DR   GeneID; 5234878; -.
DR   KEGG; lel:LELG_00251; -.
DR   VEuPathDB; FungiDB:LELG_00251; -.
DR   eggNOG; KOG0154; Eukaryota.
DR   HOGENOM; CLU_021974_1_0_1; -.
DR   InParanoid; A5DSB5; -.
DR   OMA; PVFMRID; -.
DR   OrthoDB; 941249at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd02646; R3H_G-patch; 1.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR034082; R3H_G-patch.
DR   Pfam; PF01585; G-patch; 1.
DR   SMART; SM00443; G_patch; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome.
FT   CHAIN           1..792
FT                   /note="Protein SQS1"
FT                   /id="PRO_0000324998"
FT   DOMAIN          619..683
FT                   /note="R3H"
FT   DOMAIN          750..792
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..206
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..313
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..518
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..723
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   792 AA;  90793 MW;  A88B1EF762AE1608 CRC64;
     MPKRGNRRTR GSRGGSRGGS RNLLKNRTRG NKRKSPSSNT YNRLSSSQYQ ELMDLDSIYI
     PNGEMAEVGR NMGRRRYGKL AEEAAYTESH RYEDFASKTF RNRPIEFIKA KEVYDPNVIL
     HKLTQEKKTQ YGDIIDEEFK SISLDDSEAD SEADDDDEEE EEEEEEEKDG QEMENENETD
     DANEEADEQS SELWNDEEEG DSQEDWDEEE LRKVLDKKLV QLQKELDLEQ DVGIVEKNEK
     DIIDKEDKES DVDDSILNAD KENSEQFVNI GKNQSEIESE DEDGDEEEEQ DLDENNDFED
     DSDDDLDDAS IEDINGEEFA KQNDVSSISY LDENNIYSEK LSRDESLDSI PGSKNVDNSS
     SLEEITVKSK PKDLVKNATN NFINCNERTG KDKPESEPEY GFLEEDYEFD VSKIEVSNVR
     FGISNQYYVK CAELTGTTVD EFFWFDEEDV IDYVLANGVK EHRLAKFLSF VTKGMVGGNE
     SESQEDLDAF TIDVNGLDDD DESDDDEDDD EDEDENKFAS GQDDYPYDSE DGLEDLIAYT
     RNSTQGLVPM LDRDFSRNIP AKSRSTFDDL DIDPDLQSSL TRQLKNYNHN KREKRKARKD
     REVEEAVLRN DMLIKYPEKI LIKEIRAEFE ALLKDESRHS MSFPTLDSHG HHTIKNMADC
     YHMTTDKCGK QGVRHYLKVS KTKSTFKYFP NYKRVNAIMR GRPIFHRIDR KPNPKDKKTK
     TISGRGSDSG GRAKFKEGDI VGAEAPEIDQ NNLGRQMLER LGWSKGMGLG LSGRGINEPI
     VAKVKMSKTG IK
 
 
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