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Database: UniProt
Entry: A0A094AEF3_9PEZI
LinkDB: A0A094AEF3_9PEZI
Original site: A0A094AEF3_9PEZI 
ID   A0A094AEF3_9PEZI        Unreviewed;      1060 AA.
AC   A0A094AEF3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN   ORFNames=V493_07312 {ECO:0000313|EMBL:KFY21550.1};
OS   Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY21550.1, ECO:0000313|Proteomes:UP000029327};
RN   [1] {ECO:0000313|EMBL:KFY21550.1, ECO:0000313|Proteomes:UP000029327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFY21550.1}.
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DR   EMBL; JPJV01002548; KFY21550.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094AEF3; -.
DR   STRING; 1420906.A0A094AEF3; -.
DR   HOGENOM; CLU_003537_1_1_1; -.
DR   OrthoDB; 24955at2759; -.
DR   Proteomes; UP000029327; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   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; 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; PF03439; Spt5-NGN; 1.
DR   Pfam; PF11942; Spt5_N; 1.
DR   PIRSF; PIRSF036945; Spt5; 1.
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:UP000029327};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR036945}.
FT   DOMAIN          321..349
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          480..507
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          533..561
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          656..681
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          749..776
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          869..1008
FT                   /note="Spt5 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01104"
FT   REGION          1..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          798..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          940..1060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..103
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..141
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        945..973
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1060 AA;  113100 MW;  8C8262979E470AC6 CRC64;
     MSTANFLDQH FSDSEDEGDF NPAPADLSDD EGADNNNSSP AKNRESSVSN RQQDDSEEET
     SPVRESKSRS RTPGDGGDNN NDEDTGAGQD EEDEDEDEDE EEEEVTGHRR KRRRERRNQF
     LDVEAEVDES EDENDDDDDE LNELKDNFIA DTHPDDAFDL PAGGDADDRR HRELDRRREM
     ESSLDAEKQA EILRQRYAKT RSAKLGGDSA VVPKRLLLPS VDDPSIWAVK CKEGKEREVV
     FSITKRLEER FGTKDELAII SAFERANATA PIKGYIYVEA QRQAEIEAAL DGLMNVYPRT
     KMLLVEIKEM PDLLRVSKTA PLEPGAYVRL KRPVKYSGDL AQVVDVTENG LEVRVRFVPR
     LDYGLHEDMN TPGLDAQGKR KRANAGPRPP PRLFSDVEAK KRHARYLTGN PQTKIWNYMG
     DEYNNGYCEK DVKIQQIQVK DVNPTLEEVT RFASGADDGT ENLDLNALAA SLKASTANAS
     YLPGDIIEVY EGEQKGVFGK AIAIQADIVT MAVTDGPLKG QTIEVPTKGL RKRFRQGDHV
     KVIGGSRFRD EVGMVVKIVQ DRVTLLTDQG NNEITVFSKD LRESSDSGGA GSLGQFELWD
     LVQLDPATVA CIIKVDRESL TVLDQNEQTR TVMPSQIANK LERRKFAVAT DRNGSEVRTD
     DVVKEIGDGG RQGKIMHIHR SFLFLHSAEQ SENAGVFVVR TTNIATISAT GGRIIASAGP
     DLSSMNPAMK LNPAGGNMDM PPPKFTGRDR SIGQTVTIKK GPYKGLLGIV KETTDTTARV
     ELHTKGKTVN VPKDALAFKD PRTGNTIDPN ARGGYRGGGG GSRGGFGGRG GFGGATPSGN
     GWDGGRTPGG SGGSDRTPAW GRAAGSNGGG RTPAWKAAAD AGGRTPAWQD GSRTVAYGAG
     NRTPAWQAGG KTPAYGGFGS GSDGFAAGSK TPAYGGGGSD AWGSGSKTPA YSSNEPSGTS
     SWGASSYDAP TPGAQVTAPT PGGLNAPTPG AYSAPTPGAS GAASAPTPAG WGGGGWGGAP
     ENAPTPGALA APTPGGWGAP TPGEWGADGA NEDGPRYTDE
//
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