ID A0A7R9LGB2_9ACAR Unreviewed; 1065 AA.
AC A0A7R9LGB2;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 02-APR-2025, entry version 15.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN ORFNames=ONB1V03_LOCUS2236 {ECO:0000313|EMBL:CAD7639833.1};
OS Oppiella nova.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Oribatida; Brachypylina; Oppioidea; Oppiidae;
OC Oppiella.
OX NCBI_TaxID=334625 {ECO:0000313|EMBL:CAD7639833.1};
RN [1] {ECO:0000313|EMBL:CAD7639833.1}
RP NUCLEOTIDE SEQUENCE.
RA Tran Van P.;
RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
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; OC915312; CAD7639833.1; -; Genomic_DNA.
DR EMBL; CAJPVJ010000487; CAG2162644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7R9LGB2; -.
DR OrthoDB; 28901at2759; -.
DR Proteomes; UP000728032; Unassembled WGS sequence.
DR GO; GO:0032044; C:DSIF complex; IEA:TreeGrafter.
DR GO; GO:0003729; F:mRNA binding; IEA:TreeGrafter.
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; cd06086; KOW_Spt5_6; 1.
DR CDD; cd09888; NGN_Euk; 1.
DR FunFam; 2.30.30.30:FF:000013; Transcription elongation factor SPT5; 1.
DR FunFam; 2.30.30.30:FF:000016; Transcription elongation factor SPT5; 1.
DR FunFam; 3.30.70.940:FF:000005; Transcription elongation factor SPT5; 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; 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; 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; PF00467; KOW; 1.
DR Pfam; PF23042; KOW1_SPT5; 1.
DR Pfam; PF23284; KOW2_Spt5; 1.
DR Pfam; PF23291; KOW4_SPT5; 1.
DR Pfam; PF23290; KOW5_SPT5; 1.
DR Pfam; PF23288; KOW6_SPT5; 1.
DR Pfam; PF23287; KOW7_SPT5; 1.
DR Pfam; PF23037; KOWx_SPT5; 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; 6.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036945};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000728032};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 164..255
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 260..287
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 409..436
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 461..488
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 583..610
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 689..716
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 762..884
FT /note="Spt5 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01104"
FT DOMAIN 1011..1038
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..65
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..83
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..859
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..929
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1065 AA; 117769 MW; 1A7281A2834C6CBE CRC64;
MSDSEESNRD SDNDNEAEEV EREEPEVADE EEPEGEDLDE DDYDDEEDED DLSGRRRRKR
KKPRHGGFIL DEAEVDDEIE DDEEWEDGAD EIIEKNKHLD DSSQRDMESH RRIHMMWNSQ
KEDEIEDYYR RKYAETSAAE KGYDGDVDLP DDITQQALMP GVKDPNLWMI KCKIGEEKAT
VLQLMRKFIA FSTTDEPLPI KSVVAPEGIK GYIYIEAFKQ THVKQAIQGM GNLRLGIYRQ
TMVPINEMTD VLRVTKDNSQ IKVNQWVRLK RGLYKDDLGQ VDYVDTAQNQ VHLKLIPRID
YTRLRGALRA ASNENDSQKR KRMKRPLPKL FDMDAIRAIG GEVTNDGDFI IFEANRYRRG
FLYKAFTTTA LLIDGVKPTL SELEKFEEHP EGIELQLSES TVAEDKGHSF SPGDTVEVCE
GELAHLQGKI ITIDGNKITM IPKHEDLTDP LDFQAHELRK YFKMGDHVKV IAGRYEGDTG
LIVRVEDTQI VLFSDLTMHE LKVLPKDLQL CADMATGVDT MGQFQWGDLV QMDAQTVGVI
VRLEKENFQI LNQNGKLVHV KHQAVSKKRD SRRAVALDSE QNQIQVKDHV KVIDGPHSGR
QGEIKHLYRN AAFLYSRMML ENGGIFVCKT RHLILAGGSR PLSASGVMNT SAGYMSPRIQ
SPAHPSSGGG GGQNRQFSGS KGGRDRSDLE LIGKTIKITQ GTYKGYIGIV KDAIGTTARV
ELHATCQTIT VDKTRIVVVG SGGADKGSGG VSTYARNTPM YGSQTPMYGT GSRTPMYGGA
NTPLHDGSRT PAYGGGGATP MHDGSRTPVH TSSIWDPTAS TTPRPDFDYD EPSPSPSNPS
YMNPPTPGYP NPETPPGGPY TPQTPGMYAS SDHSYSPYGP AATPSPSTYS VPGTAPSPAS
AGYMTPSPAY NGPHSVGPSP SPTGYGYSPM TPGVSSPHFN PQTPGAGMEQ SFSVEWQTTD
IEVRIKDCHD DDDLIGQTGI VRGISGGMCA VFLLKEDRVV NILSEHLEPV QPGPEDKFKV
IFGEDRENTG TLLSIDGNEG VVSFNSGDSD DIKMLPLRYL CKMKK
//
