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SPT5_ASPOR
ID   SPT5_ASPOR              Reviewed;        1026 AA.
AC   Q2UGU3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Transcription elongation factor spt5;
DE   AltName: Full=Chromatin elongation factor spt5;
GN   Name=spt5; ORFNames=AO090023000710;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- FUNCTION: The spt4-spt5 complex mediates both activation and inhibition
CC       of transcription elongation, and plays a role in pre-mRNA processing.
CC       This complex seems to be important for the stability of the RNA
CC       polymerase II elongation machinery on the chromatin template but not
CC       for the inherent ability of this machinery to translocate down the gene
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the spt4-spt5 complex. Interacts with RNA
CC       polymerase II (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SPT5 family. {ECO:0000305}.
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DR   EMBL; AP007157; BAE59222.1; -; Genomic_DNA.
DR   RefSeq; XP_001821224.1; XM_001821172.1.
DR   AlphaFoldDB; Q2UGU3; -.
DR   SMR; Q2UGU3; -.
DR   STRING; 510516.Q2UGU3; -.
DR   EnsemblFungi; BAE59222; BAE59222; AO090023000710.
DR   GeneID; 5993226; -.
DR   KEGG; aor:AO090023000710; -.
DR   VEuPathDB; FungiDB:AO090023000710; -.
DR   HOGENOM; CLU_003537_1_1_1; -.
DR   OMA; VGYMNTP; -.
DR   Proteomes; UP000006564; Chromosome 3.
DR   GO; GO:0032044; C:DSIF complex; IEA:EnsemblFungi.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0060195; P:negative regulation of antisense RNA transcription; IEA:EnsemblFungi.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   CDD; cd06081; KOW_Spt5_1; 1.
DR   CDD; cd06082; KOW_Spt5_2; 1.
DR   CDD; cd06083; KOW_Spt5_3; 1.
DR   CDD; cd06084; KOW_Spt5_4; 1.
DR   CDD; cd06085; KOW_Spt5_5; 1.
DR   CDD; cd09888; NGN_Euk; 1.
DR   Gene3D; 2.30.30.30; -; 3.
DR   Gene3D; 3.30.70.940; -; 1.
DR   InterPro; IPR005824; KOW.
DR   InterPro; IPR041973; KOW_Spt5_1.
DR   InterPro; IPR041975; KOW_Spt5_2.
DR   InterPro; IPR041976; KOW_Spt5_3.
DR   InterPro; IPR041977; KOW_Spt5_4.
DR   InterPro; IPR041978; KOW_Spt5_5.
DR   InterPro; IPR005100; NGN-domain.
DR   InterPro; IPR006645; NGN_dom.
DR   InterPro; IPR036735; NGN_dom_sf.
DR   InterPro; IPR039385; NGN_Euk.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR039659; SPT5.
DR   InterPro; IPR024945; Spt5_C_dom.
DR   InterPro; IPR022581; Spt5_N.
DR   InterPro; IPR017071; TF_Spt5_eukaryote.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR11125; PTHR11125; 1.
DR   Pfam; PF03439; Spt5-NGN; 1.
DR   Pfam; PF11942; Spt5_N; 1.
DR   PIRSF; PIRSF036945; Spt5; 1.
DR   SMART; SM01104; CTD; 1.
DR   SMART; SM00739; KOW; 5.
DR   SMART; SM00738; NGN; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
PE   3: Inferred from homology;
KW   mRNA processing; Nucleus; Reference proteome; Repeat; Transcription.
FT   CHAIN           1..1026
FT                   /note="Transcription elongation factor spt5"
FT                   /id="PRO_0000238556"
FT   DOMAIN          305..338
FT                   /note="KOW 1"
FT   DOMAIN          519..553
FT                   /note="KOW 2"
FT   REGION          1..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          905..1026
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..93
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..136
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        905..930
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1026 AA;  111285 MW;  646958E269E2E583 CRC64;
     MSRNMLDHDF GSDEEDDDFN PAPAYDSDNE DARPTHQDRD DDDDEEDVKP SRRAERRVGS
     EEADDNEDAD GHDDEEEDEN DDDDEEEEDE DEEGAVSRPK KRRRKGGVAH FFEEEAGVDE
     DEDEAEDEED EMAELGGEMH PDDMDALPVG AETDDRRHRQ LDRQRELEAS MDAEKQAQLL
     KERYGRNRAA ASDAVVVPKR LLLPSVEDPS IWGVRCKPGK EREVIFAIQK RIEERPMGSR
     NPMKIISAFE RGGAMSGYIY VEARRQADVM DALQDMSNVY PRTKMILVPV REMPDLLRVQ
     KSEELLPGGW VRIKRGKYQN DLAQIEEVET NGLAVTVRLV PRLDYGMNED IGAPFMDPKR
     KRPGMNPAVA RPPQRLFSEA EAKKKHGKYL SATSGLGGKS WSYLGETYVD GFLIKDMKVQ
     HLITKNVSPR LEEVTMFARG SEDGTANLDL ASLAETLKNS TAEDSYLPGD PVEVFRGEQQ
     GLIGRTTSTR GDIVTLQVTE GDLAGQHIDA PVKSLRKRFR EGDHVKVIGG SRYQDELGMV
     VQVKDDTVTL LSDMSMQEIT VFSKDLRLSA ETGVDGKLGM FDVHDLVQLD AATVACIVKV
     DRESLRVLDQ NGSIRTILPT QVTNKITPRR DAVATDRNGA EIRHGDTVRE VYGEQRNGVI
     LHIHRSFLFL HNKAQAENSG ITVVRTTNVV TVSAKGGRST GPDLTKMNPA LMSRGGPSGM
     MGPPKSFGRD RMIGKTVMVR KGPFKGLVGI VKDAGDVQAR VELHSKNKLV SIPKELLVVK
     DPVTGQTIEM GRGRGGPRVP SAAPPSGWQG GRTPMAAADS SRTPAWGGAS SARTPAWAGM
     GGSRTPAWKN DGSRTSNPYD GSRTAYGGFG SRTPAWNAGA RTPYGGSGSG QSDFDAFAAG
     SRTPAWNANS GSRTPAWSGA TASNGSKDSR GYDAPTPGGA YSAPTPGAYA SAPTPGVSAP
     TPGAWADSAP TPGAFNAPTP GGPSKKPYDA PTPAAWDSRP YDAPTPAMGG DGDDAGPRYE
     DGTPSP
 
 
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