SPT5_EMENI
ID SPT5_EMENI Reviewed; 1016 AA.
AC Q5BCN2; C8VNU8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Transcription elongation factor spt5;
DE AltName: Full=Chromatin elongation factor spt5;
GN Name=spt5; ORFNames=AN1698;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF85391.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000026; EAA64818.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF85391.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_659302.1; XM_654210.1.
DR AlphaFoldDB; Q5BCN2; -.
DR SMR; Q5BCN2; -.
DR STRING; 162425.CADANIAP00008341; -.
DR EnsemblFungi; EAA64818; EAA64818; AN1698.2.
DR GeneID; 2875573; -.
DR KEGG; ani:AN1698.2; -.
DR VEuPathDB; FungiDB:AN1698; -.
DR eggNOG; KOG1999; Eukaryota.
DR HOGENOM; CLU_003537_1_1_1; -.
DR InParanoid; Q5BCN2; -.
DR OrthoDB; 828863at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0032044; C:DSIF complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
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; Transcription.
FT CHAIN 1..1016
FT /note="Transcription elongation factor spt5"
FT /id="PRO_0000238561"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..130
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1016 AA; 109412 MW; C06DE37C26E5F734 CRC64;
MSRNLMDQDF GSEEEDDDFN PAPAEESDNE EAHHDKTRKP DRDSDARNGS DDEGADEAGE
EDEEENEEGG EGEGDEEEDE EEDEDDDDVS KPRKRRKGHG GLSAFIDYEA GVDEEEDEVE
DEEEEEGYGL EQHPDDVLPA GAETDDRQHR RLDRERELAA TLDAEKQAQL LKERYGRNRA
AATDAVIVPK RLLLPSVDDP SIWGVRCKAG KEREVVFSIQ KRIEDRPPGS RNPIKIISAF
ERGGAMSGYI YVEARRQADV MDALQDMSNV YPRTKMILVP VKEMPDLLRV QKSEELNPGG
WVRIKRGKYM NDLAQIEEVE TNGLAVTVRL VPRLDYGMNE DSGAPIMDPK RKRPGANPAV
ARPPQRLFSE AEAKKKHSKY LTATAGLGAK SWNYLGETYI DGFLIKDMKV QHLITKNVNP
RLEEVTMFAR DSENGTSNLD LASLAETLKN STAEESYLPG DPVEVFKGEQ QGLVGRTSST
RGDIVTILVT EGELAGQTIE APVKTLRKRF REGDHVKVIG GSRYQDELGM VVQVRDDTVT
LLSDMSMQEI TVFSKDLRLS AETGVDGKLG MFDVHDLVQL DAATVACIVK VDRESLRVLD
QNGSIRTILP SQVTNKITPR RDAVATDRNG AEIRHGDTVR EVYGEQRSGV ILHIHRSFLF
IHNKAQAENA GIVVVRTTNV VTVSAKGGRP TGPDLSKMNP ALMRNGAPGG MMAPPPSKTF
GRDRLLGKTV LVKKGPFKGL LGIVKDTTDV QARVELHSKN KLVTIPKELL VVKDPVTGQT
IDIGRGRGGP RVPQNSAAPS SGWQGGRTPM AAADSSRTPA WGAAMSSRTP AWSGAGLGSR
TPAWKADGSR TAYGGAGSRT PAWNAGARTP YGGGFGSGSG NSDFDAFAAG SRTPAWGAAS
GSRTPAWSAS ANTTSRNDNK AYDAPTPGAT YSAPTPGAYG GAPTPGLSAP TPGAWADSAP
TPGAYNAPTP ADFGEGSRPY DAPTPAMGGA AATPGAGAYG DTDDGAPRYE EGTPSP