ID A0A4U0V8Z0_9PEZI Unreviewed; 1026 AA.
AC A0A4U0V8Z0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 02-APR-2025, entry version 18.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN ORFNames=B0A54_05180 {ECO:0000313|EMBL:TKA44436.1};
OS Friedmanniomyces endolithicus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Friedmanniomyces.
OX NCBI_TaxID=329885 {ECO:0000313|EMBL:TKA44436.1, ECO:0000313|Proteomes:UP000310066};
RN [1] {ECO:0000313|EMBL:TKA44436.1, ECO:0000313|Proteomes:UP000310066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5311 {ECO:0000313|EMBL:TKA44436.1,
RC ECO:0000313|Proteomes:UP000310066};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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:TKA44436.1}.
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DR EMBL; NAJP01000015; TKA44436.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U0V8Z0; -.
DR STRING; 329885.A0A4U0V8Z0; -.
DR OrthoDB; 28901at2759; -.
DR Proteomes; UP000310066; 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:0006368; P:transcription elongation by RNA polymerase II; IEA:TreeGrafter.
DR CDD; cd06081; KOW_Spt5_1; 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 FunFam; 2.30.30.30:FF:000018; 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; IPR041976; KOW_Spt5_3.
DR InterPro; IPR041977; KOW_Spt5_4.
DR InterPro; IPR041978; KOW_Spt5_5.
DR InterPro; IPR005100; NGN-domain.
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; 2.
DR Pfam; PF23042; KOW1_SPT5; 1.
DR Pfam; PF23291; KOW4_SPT5; 1.
DR Pfam; PF23290; KOW5_SPT5; 1.
DR Pfam; PF23037; KOWx_SPT5; 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 SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036945};
KW Reference proteome {ECO:0000313|Proteomes:UP000310066};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 331..358
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 493..520
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 548..576
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 671..696
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 763..790
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 842..1023
FT /note="Spt5 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01104"
FT REGION 1..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..120
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..133
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..159
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1026 AA; 110503 MW; 02DD08777AF21452 CRC64;
MASLLDQNFP DEDDDDFNPA PEVGSDDEGE SKAKVVKGAS GAPPSTDRSR SRPKNADDDL
KNGDGDEGGL VGFGREDEVE ADGDGEDDRQ VGENGAEGVE EDDEEEEEDE EEEEEDDDIE
GQPSRKRRKK HPRNQFIDVE AEVDEEEDEE PEEDEDQPGE EMHPDDLQEL PPGADRDDRK
HRELDRQRDA QYQLDAEQEA ARLKERYGRQ SRATGTGTAI VPQKLLMPTQ DDPRIWRMRC
KPGKEKEVII SLQARVHERA GGREPIQIFS AFERSKGAGD PMAGMLYVEA KRVDDVVTAL
EGIKNVFMSH KPFMVPMEEM PDLLKVTKDK QLEPGMYVRI RRGLYQGDLA QVDAVETNGA
EVTVRLVPRL DYGLNEDVNG PMEAPLPNGQ KRKRPVTQRP PPRLFSEVEA KKRHGKYLTR
VGGLSGATWT YQSKEYTDGF LVDTLKSSAL QTSDVNPTLE EVTRFATSGG EDGTENLDLA
ALAATLKTSS SNEFLPGDKV EVVRGEQKGV SGVSVEVYGE VVKIKVDPGN GALSGVIMST
PVRDLRKLFR EGDHVKVIGG SKYTDEVGMV VRTRDDCVTL LTDAEQKEIT VFSKDLREAT
DSGGAAADSK YDLFDLVQMD AATVGIVIRV DRESLRVLDQ NGSNRILLPS NISNKIDKRR
NAVATDRDGN EMKNDDTVKE VGGELKTGRV LHLHRNYVFA QNRERSENSG VWVGRHSNVL
VVAAKGGKTN NSGPDLTKMN PALKQNGGRA PSPMPPPQSK GRDRLIGKTV KIRMGPMKGM
IGIVKDAAGE EAKVELHAKN KIVPVKKEML SLIDSKDGKV IQGGIQSLSM GRPPPASASA
IPGRTPAYAA QGGRTPAYAM GGRTPAYASA ASARTPAWKQ DAGARTPAYA AGGGQTAYGG
GGLGGQTAYG GATSYGGATS YGGGSVWGGA SGAQSTWNAN TGGRTPAPSG SKTPAYSGVL
EAPTPGYASA PTPGGYEDRP TPGGFRDQQV ASTGNYGRTP AAQTPGGYAP ETPGQWDDGG
EGPRYD
//
