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Database: UniProt
Entry: A0A1B8FSP2_9PEZI
LinkDB: A0A1B8FSP2_9PEZI
Original site: A0A1B8FSP2_9PEZI 
ID   A0A1B8FSP2_9PEZI        Unreviewed;      1058 AA.
AC   A0A1B8FSP2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, 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=VE02_04437 {ECO:0000313|EMBL:OBT86621.1};
OS   Pseudogymnoascus sp. 03VT05.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1622148 {ECO:0000313|EMBL:OBT86621.1};
RN   [1] {ECO:0000313|EMBL:OBT86621.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03VT05 {ECO:0000313|EMBL:OBT86621.1};
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT   white-nose syndrome of bats.";
RL   Submitted (MAR-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}.
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DR   EMBL; KV459418; OBT86621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8FSP2; -.
DR   Proteomes; UP000091872; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 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   SMART; SM00738; NGN; 1.
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   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR036945}.
FT   DOMAIN          224..318
FT                   /note="NusG-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00738"
FT   DOMAIN          322..350
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          481..508
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          534..562
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          657..682
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          750..777
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          867..1006
FT                   /note="Spt5 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01104"
FT   REGION          1..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          799..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          944..1058
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..36
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..104
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..143
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        944..971
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1058 AA;  113082 MW;  A484704C5A7ED482 CRC64;
     MSTANFLDQH FSDSEDEGDF NPAPADLSDE EGADDDNSSP APPKNRGSSV SNRQQEDSDE
     ETSPARKSKS RSRTPADRGD NNDEDTGAGQ DDEDEDEDED EEEEEVTGHR RKRRRERRNQ
     FLDVEAEVDE SEDENDDDDD ELNELKDNFI ADTHPDDAFD LPAGGDADDR RHRELDRRRE
     MESSLDAEKQ AEILRQRYAK TRSAKLGGDS AVVPKRLLLP SVDDPSIWAV KCKEGKEREV
     VFSITKRLEE RFGTKDELSI ISAFERANAT APIKGYIYVE AQRQAEIESA LDGLMNVYPR
     TKMLLVEIKE MPDLLRVSKT APLEPGAYMR LKRPAKYAGD LAQVVDVTEN GLEVRVRFVP
     RLDYGLHEDM NTPGLDAQGK RKRANAGPRP PPRLFSDVEA KKRHARYLTG NPQTKIWNYM
     GDEYNNGYCE KDVKIQQIQV KDVNPTLEEV TRFASGADDG TENLDLNALA ASLKASTANA
     SYLPGDIVEV YEGEQKGVFG KAIAIQADIV TMAVTDGVLK GKTIEVPTKG LRKRFRQGDH
     VKVIGGSRFR DEVGMVVKIV QDRVTLLTDQ GNNEVTVFSK DLRESSDSGG AGSLGQFELW
     DLVQLDPATV ACIIKVDRES LTVLDQNEQT RTVMPSQIAN KLERRKFAVA TDRNGSEVRT
     DDVVKEIGDG GRQGKIMHIH RSFLFLHSAE QNENAGVFVV RTTNIATISA TGGRIIASAG
     PDLSSMNPAM KLNPQGGNME MPPPKFVGRD RSIGQTVTIK KGPYKGLLGI VKETTDTTAR
     VELHTKGKTV NVPKDALAFK DPRTGNTIDP NARGGYRGGG GGSRGGRGGG FGGATTSGGW
     DGGRTPGGAG GSDRTPAWGR AAASNGGGRT PAWKAAADAG GRTPAWQDGS RTVAYGAGNR
     TPAWQAGGKT PAYGGFGSGS DGFAAGSKTP AYGGGGSDAW GSGSKTPAYS SNEPTNTSSW
     GANSYDAPTP GAQVTAPTPG GLNAPTPGAY SAPTPGASGA ASAPTPAGWG GGGWGGAPEN
     APTPGALAAP TPGGWGAPTP GEWGADGSNE DGPRYTDE
//
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