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Database: UniProt
Entry: A0A1J9PU22_9EURO
LinkDB: A0A1J9PU22_9EURO
Original site: A0A1J9PU22_9EURO 
ID   A0A1J9PU22_9EURO        Unreviewed;      1100 AA.
AC   A0A1J9PU22;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN   ORFNames=AJ78_00099 {ECO:0000313|EMBL:OJD19905.1};
OS   Emergomyces pasteurianus Ep9510.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX   NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD19905.1, ECO:0000313|Proteomes:UP000182235};
RN   [1] {ECO:0000313|EMBL:OJD19905.1, ECO:0000313|Proteomes:UP000182235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD19905.1,
RC   ECO:0000313|Proteomes:UP000182235};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA   McEwen J.G.;
RT   "Emmonsia species relationships and genome sequence.";
RL   Submitted (JUL-2015) 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:OJD19905.1}.
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DR   EMBL; LGRN01000002; OJD19905.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9PU22; -.
DR   STRING; 1447872.A0A1J9PU22; -.
DR   VEuPathDB; FungiDB:AJ78_00099; -.
DR   OrthoDB; 24955at2759; -.
DR   Proteomes; UP000182235; 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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000182235};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR036945}.
FT   DOMAIN          242..334
FT                   /note="NusG-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00738"
FT   DOMAIN          338..365
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          499..526
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          552..580
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          675..700
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          767..794
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          876..1030
FT                   /note="Spt5 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01104"
FT   REGION          1..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          825..930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          958..1100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..128
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..170
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        860..910
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1100 AA;  118604 MW;  14AFA76497A7E9C1 CRC64;
     MSNPASKFLN EDFGSEEEDD DFNPVPVEDS DDERPGKREA TSYDDVARRD RSGLGGEGDE
     ENQEEDEPPR RKEKDGDSDN GEEDYGDAEE NEGVRVGGRM DDDEEEEEEE EEEEGEEDDD
     EEEEEEEEQA VAGRPRKRRR RRLNGFVDME AEVDEDDDAE EDDEEMGDGF VAEHPDDHDA
     LPIGAETDDR RHRELDRKRD LEATMDAEKQ AQALKERYGR NRAAAADLVV VPKRLLLPSV
     DDPSIWAVKC RPGKEREAVF NIMKRIEDRP PGSRRPIRIM SAFERGGTMS GYIYVEARKQ
     ADVIDALEDM SNVYTKSKMI LISVKEMPDL LRVTKSEELV PGGWVRIKRG KYQGDLAQLE
     DVETNGLDVT VRLVPRLDYG LNEDMGAPNG DMKRKRPGIN SAIARPPQRP FSEAEAKKKH
     AKYLSATSGL GGKTWSYLGD NYVDGFLIKE MKVQHLITKN VNPQLDEVTK FARGADDGTA
     NLDLAALAAS LKNTTTEDSY LPGDTVEVFQ GEQQGVVGKT VSTRGDIVSI KVTQGELEGQ
     QIDVPIKGLR KRFQEGDHVK VIGGSRFRDE LGMVVRIKDD RVTLLSDMSM QEITVFSKDI
     REAADAGVDG KLGMYDVHDL VQLDQATVGC IIKLDRESMR VIDQNGSVRN VLPSQVMNKI
     SQRRNAVSTD RNGSEIRCGD TVREVTGEQR TGAILHIHRS FLFLNNKDAG DNAGIIVTRA
     SNVTTVATSG GRLASRSAPD FSRMNPAIQK NGMNGSGMPP PKSFGRDRTI GKTVTIRKGP
     FKGLLGIVKD TTDAQARVEL HSKNKVITVD KDMLSIKDPI TGASIDLSRY GGRAGGGAGS
     GRTPYGGSAA PPDWSGSRTP VAAIDSSRTP AWRSSSSRTP AWSSATASGS RTPAWKADGS
     RTSNPYDGNR TAYGGATFGG GRTPAWTSGT KTPYDSNSGF GSSSNSSFDA FAAGSRTPAY
     PGGGSRTPAW APGSAAPPPV GHSSGSKGGY DAPTPGADYS APTPGPYGSA PTPGATAATP
     RGWADSAPTP GAMHAPTPDA SGYSSKRPGE LYDAPTPAAI SMGGGRPYDA PTPAMGMGIP
     ATPSAGDDGG PRYEEGTPSP
//
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