ID A0A1Y1S8N7_9MICR Unreviewed; 568 AA.
AC A0A1Y1S8N7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 08-NOV-2023, entry version 26.
DE RecName: Full=Chromatin elongation factor SPT5 {ECO:0000256|ARBA:ARBA00029865};
DE AltName: Full=Chromatin elongation factor spt5 {ECO:0000256|ARBA:ARBA00031006};
GN Name=SPT5 {ECO:0000313|EMBL:ORD94553.1};
GN ORFNames=ECANGB1_547 {ECO:0000313|EMBL:ORD94553.1};
OS Enterospora canceri.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC Enterospora.
OX NCBI_TaxID=1081671 {ECO:0000313|EMBL:ORD94553.1, ECO:0000313|Proteomes:UP000192639};
RN [1] {ECO:0000313|EMBL:ORD94553.1, ECO:0000313|Proteomes:UP000192639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB1 {ECO:0000313|EMBL:ORD94553.1,
RC ECO:0000313|Proteomes:UP000192639};
RX PubMed=28345194; DOI=10.1111/1462-2920.13734;
RA Wiredu Boakye D., Jaroenlak P., Prachumwat A., Williams T.A., Bateman K.S.,
RA Itsathitphaisarn O., Sritunyalucksana K., Paszkiewicz K.H., Moore K.A.,
RA Stentiford G.D., Williams B.A.;
RT "Decay of the glycolytic pathway and adaptation to intranuclear parasitism
RT within Enterocytozoonidae microsporidia.";
RL Environ. Microbiol. 19:2077-2089(2017).
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
CC gene. {ECO:0000256|ARBA:ARBA00024691}.
CC -!- SIMILARITY: Belongs to the SPT5 family.
CC {ECO:0000256|ARBA:ARBA00006956}.
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:ORD94553.1}.
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DR EMBL; LWDP01000016; ORD94553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1S8N7; -.
DR VEuPathDB; MicrosporidiaDB:ECANGB1_547; -.
DR Proteomes; UP000192639; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006354; P:DNA-templated transcription elongation; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd09888; NGN_Euk; 1.
DR Gene3D; 2.30.30.30; -; 2.
DR Gene3D; 3.30.70.940; NusG, N-terminal domain; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR005100; NGN-domain.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR039385; NGN_Euk.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR005825; Ribosomal_uL24_CS.
DR InterPro; IPR039659; SPT5.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11125; SUPPRESSOR OF TY 5; 1.
DR PANTHER; PTHR11125:SF7; TRANSCRIPTION ELONGATION FACTOR SPT5; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR SMART; SM00739; KOW; 4.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR PROSITE; PS01108; RIBOSOMAL_L24; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000192639}.
FT DOMAIN 158..185
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 258..285
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 371..398
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 518..545
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 64283 MW; BA8F7F31203C75E3 CRC64;
MEAESSEEEI NSDVTSEDLD GFVEPDYGRE RRDLYGEKVS ELEQKYAKYV EREDESTTEE
IRPQIRPFPT SMDPLLFLVR VKFGKEKSIA NRIIEQAKGV GDVTAVVQKD GLKGYIYVEA
FKRTAVDEAV QRVKNVYKNK ISAIPFSEMI DALSCRKDYI VNDYARVKSG KYKDDVVQVL
ENYEDCCQIK AVPRLNDRRR LFDPEEFRAQ VTAKNGGFYY NRDFFRDGFL IKTVLKMSLD
FDIQPTFDDL KQLDTERPVR LNDAVRVVKG DLKNFTGKVV SVAGSTCVVS DGTSTFDVDA
GCLEKRVEVG DVFSYAGENG VVLQKEGNRV VLGIREMQDE VSVHINDLEG RVVERPKTTK
TRPQTPKKRL DLLVNKNVRI VAGAYKGLVG IVKEVHRERC RVQLMSNLES VHVYKNDIRE
IAPTQQAQAS ATPGYKTPGS KTPGYTTPGY KTPGYTTPGY RTPGYAPPET EIQAASVYYG
MKILIDGSEK TVSRMEESIY YTTDGREVAA TEMVPVRPTN KYDPVFIFRG DHKEKNGVLI
EFEEEIGKVE LMGNEYVRVK LDDMAVKN
//
