ID A0A1S9DYX4_ASPOZ Unreviewed; 1026 AA.
AC A0A1S9DYX4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN ORFNames=OAory_01028470 {ECO:0000313|EMBL:OOO14252.1};
OS Aspergillus oryzae (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO14252.1, ECO:0000313|Proteomes:UP000190312};
RN [1] {ECO:0000313|EMBL:OOO14252.1, ECO:0000313|Proteomes:UP000190312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC7051 {ECO:0000313|EMBL:OOO14252.1,
RC ECO:0000313|Proteomes:UP000190312};
RA Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA Jeennor S., Laoteng K.;
RT "Genome sequencing of Aspergillus oryzae BCC7051.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|PIRNR:PIRNR036945}.
CC -!- SUBUNIT: Component of the SPT4-SPT5 complex. Interacts with RNA
CC polymerase II. {ECO:0000256|ARBA:ARBA00025870}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR036945}.
CC -!- SIMILARITY: Belongs to the SPT5 family. {ECO:0000256|ARBA:ARBA00006956,
CC ECO:0000256|PIRNR:PIRNR036945}.
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:OOO14252.1}.
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DR EMBL; MKZY01000001; OOO14252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9DYX4; -.
DR SMR; A0A1S9DYX4; -.
DR VEuPathDB; FungiDB:AO090023000710; -.
DR eggNOG; KOG1999; Eukaryota.
DR OMA; PYPVGYM; -.
DR Proteomes; UP000190312; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003746; F:translation elongation factor activity; 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; IEA:InterPro.
DR GO; GO:0140673; P:transcription elongation-coupled chromatin remodeling; IEA:InterPro.
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; NusG, N-terminal domain; 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-like_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR039385; NGN_Euk.
DR InterPro; IPR014722; Rib_uL2_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; SUPPRESSOR OF TY 5; 1.
DR PANTHER; PTHR11125:SF7; TRANSCRIPTION ELONGATION FACTOR SPT5; 1.
DR Pfam; PF12815; CTD; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 2.
DR SMART; SM01104; CTD; 1.
DR SMART; SM00739; KOW; 5.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000313|EMBL:OOO14252.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036945};
KW Protein biosynthesis {ECO:0000313|EMBL:OOO14252.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000190312};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 208..300
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 304..331
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 465..492
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 518..546
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 641..666
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 730..757
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 831..972
FT /note="Spt5 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01104"
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
//
