ID R0HA68_9BRAS Unreviewed; 990 AA.
AC R0HA68;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|PIRNR:PIRNR036945};
GN ORFNames=CARUB_v10024589mg {ECO:0000313|EMBL:EOA26299.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA26299.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
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}.
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DR EMBL; KB870808; EOA26299.1; -; Genomic_DNA.
DR RefSeq; XP_006293401.1; XM_006293339.1.
DR AlphaFoldDB; R0HA68; -.
DR STRING; 81985.R0HA68; -.
DR eggNOG; KOG1999; Eukaryota.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; 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:0140673; P:transcription elongation-coupled chromatin remodeling; IEA:InterPro.
DR GO; GO:0006412; P:translation; 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; cd06086; KOW_Spt5_6; 1.
DR CDD; cd09888; NGN_Euk; 1.
DR Gene3D; 2.30.30.30; -; 4.
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; IPR041980; KOW_Spt5_6.
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; IPR005825; Ribosomal_uL24_CS.
DR InterPro; IPR039659; SPT5.
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:SF17; TRANSCRIPTION ELONGATION FACTOR SPT5 HOMOLOG 2-RELATED; 1.
DR Pfam; PF00467; KOW; 2.
DR Pfam; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 1.
DR SMART; SM00739; KOW; 6.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 2.
DR PROSITE; PS01108; RIBOSOMAL_L24; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036945};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 158..245
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 250..277
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 402..429
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 454..481
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 578..605
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 682..709
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 938..965
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 990 AA; 110553 MW; D4374A80EDC438B1 CRC64;
MSDDDHYEDE DYTSDDDSEE EEEEYEPRSS RKGSSGKKRG RSNSGSDGRR GGSKKKTSGS
AFIDWEVEVD DDVEDDDNDI EVEDNEFIVS GETDLPTEDA DDRRQFYQRR FNPDHEEDVD
DFEKRYIARL SRMHAQDDYE LEEVNEVDQQ ALLPSVRDPK LWLVKCAIGR EREVAVCLMQ
KIIDRESEFK IRSAIALDHL QNYIYIEADK EAHVKEAIKG MRNIFAYHKI LLVPIKEMTD
VLAVESKAID LSRDTWVRMK LGIYKGDLAQ VVDVDNVRKR VTVKLIPRID LQALANKLEG
RENVKKKDFA PPPRFMNIDE ARELHIRVEH RRDTMTGDYF ENIDNMLFKD GFLYKKVSTK
SIVAQNITPT VDELERFKRS SENGEIDFAD LSTLFANRKK GHFMKGDAVI VIKGDLKNLK
GWIEKVDEEN VLIRSEMKGL PNPLAVNERE LCKYFEPGNF VKVVSGINEG ATGMVVKVDQ
HMLIILSDTT KEHIRVFADH VVKSEEVTNG VTKIGYHELH DLVLLSDLSF GVIIKLDSEA
IQILKGVPDR PEVAIVKASE IKYKIMRKTN AQDRYKKVIT VKDVVKVIEG PSKGKQGPVV
KIYKGVLFIH DRHNLEHTGF ICTKSSSCVL VGADRIVDSF SKFGSLKTPG QVPPSPRRCQ
GADMGYNAGA GGRHRGERRD DNLLVGTYVK IRLGPFKGYR GRLVEVKEKT VRVELEAKIV
TVDREAISDI TDNVATPSQY NMGSQTTLHP SRTPLRPCMT PMRDSGATPI HDGMRTPMRG
KAWNPYMPMT PHRDSWEDGN PGSWGTSSHP YDAATPGSGW ANSTPSRSSY SDAGTPISNA
NAPSPMTPSS ASYLANTPGG QQPMTPGTDL DVMSPDIDGD AETRFMPGIL VNVHKAGEGR
NPGVIRDVLP DGSCIVALGY RGGGEKVMAT QSEVRLVSPR KSERVKILGG KYGGSTAKVI
GLDGSEGIVR LDDSLDVKIM NLARLGKLVL
//
