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Database: UniProt
Entry: A0A074VQF1_9PEZI
LinkDB: A0A074VQF1_9PEZI
Original site: A0A074VQF1_9PEZI 
ID   A0A074VQF1_9PEZI        Unreviewed;       996 AA.
AC   A0A074VQF1;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   08-NOV-2023, entry version 33.
DE   RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN   ORFNames=M437DRAFT_52118 {ECO:0000313|EMBL:KEQ61394.1};
OS   Aureobasidium melanogenum CBS 110374.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ61394.1, ECO:0000313|Proteomes:UP000030672};
RN   [1] {ECO:0000313|EMBL:KEQ61394.1, ECO:0000313|Proteomes:UP000030672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ61394.1,
RC   ECO:0000313|Proteomes:UP000030672};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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; KL584838; KEQ61394.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074VQF1; -.
DR   STRING; 1043003.A0A074VQF1; -.
DR   HOGENOM; CLU_003537_1_1_1; -.
DR   OrthoDB; 24955at2759; -.
DR   Proteomes; UP000030672; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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; 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; PF03439; Spt5-NGN; 1.
DR   Pfam; PF11942; Spt5_N; 1.
DR   PIRSF; PIRSF036945; Spt5; 1.
DR   SMART; SM00739; KOW; 5.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000313|EMBL:KEQ61394.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036945};
KW   Protein biosynthesis {ECO:0000313|EMBL:KEQ61394.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030672};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR036945}.
FT   DOMAIN          306..333
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          466..493
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          519..547
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          642..667
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          736..763
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   REGION          1..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          796..851
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          919..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..48
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..99
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..142
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   996 AA;  107536 MW;  158F41551E8BDC8D CRC64;
     MSFLNQDFGD ASDDEEEFNP APAVASDDEA DNNDDNDQGQ DDNQDDDDDA QPNARRSSAQ
     ADDQDDDDAP SRRRANNDDD DEEEDDEDEE DDEEDEEDED IGHPRKRRRK GPRNQFLDVE
     AEVDDEDEEE PDEDDEIAGE EMHPDDLLEL PAGAERDDRK HRELDRQRDL AASMDAEKQA
     QALKERYGRN RAANVDSAVV PQRLLLPSVD DPKIWRLKCK PGKEREVVFA IMKRIEDRAG
     TREPLQLISA FERGGVMAGN LYCEALVVEH VTNALEGLQN VYMGTKPMMV PITEMPDLLR
     TRKSKSLEPG MYVRVKRGKY AGDLAQIDEV ESNGTEVTLR LIPRLDYGLN EDINAAVDSK
     RKRGGFGANT GPRPPQRLFS ENEARKRHGR YLTKGTGFTA NTWTYMNDTY VDGFLIKDYK
     ANHLQSEDVN PTLEEVTKFA ADAEDGTENL DLSALAATIK SNSSGAFLPG DHVEIWQGEQ
     RGVVGKAVSV HSDIVRILVS SGELSGQIIE SPVKGLRKLF REGDHVKVIG GSKYFDEVGM
     VVKIVEDRVT ILTDSNQTEI TVFSKDLRVA TDSGGQVGVG KYDLHELVQL DASTVACVIK
     VDRESLRVLD QTGTVRSLLP SNISNKLERR KNAVATDREG SEIHIDDTVK EEGGEGRQGR
     VLHIHRNFLF AHNREQTDNA GVFVVRTNNV KTVAAKGGRV ASAQAGLMKM NPALQRPGAQ
     QAGAQAMPPP RQMGRDRLIG KTCTIRRGPH KGLLGIVKDS TDTHARVEVH GSKKIISISK
     DFLTVRDPVT GAVIQQNAGQ RPGAPPAGGA GGRPPAWGGA TPGRFGATPR ASDGGRTPAW
     KPAAGGRTPA WAGAGAGGRT AYGGSGASSV PAWQRGSGGT TAYGGATTYG GQTSYGGQTS
     YGGSTAYGGG TWNPNTRTPY HGGGTAYESG SKTPAYGMDA PTPGFSAPTP GNLDQPTPGY
     GQYRTPAAAP TPGAFPETPG AWNAETPAGD GGPGYD
//
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