ID A5DNU2_PICGU Unreviewed; 963 AA.
AC A5DNU2;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN ORFNames=PGUG_04943 {ECO:0000313|EMBL:EDK40845.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK40845.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK40845.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH408160; EDK40845.2; -; Genomic_DNA.
DR RefSeq; XP_001482988.1; XM_001482938.1.
DR AlphaFoldDB; A5DNU2; -.
DR STRING; 294746.A5DNU2; -.
DR GeneID; 5124882; -.
DR KEGG; pgu:PGUG_04943; -.
DR eggNOG; KOG1999; Eukaryota.
DR HOGENOM; CLU_003537_1_0_1; -.
DR InParanoid; A5DNU2; -.
DR OMA; PYPVGYM; -.
DR OrthoDB; 24955at2759; -.
DR Proteomes; UP000001997; 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; 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; PF00467; KOW; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 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:UP000001997};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 219..308
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 314..341
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 459..486
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 515..542
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 639..665
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 724..751
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT REGION 1..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..33
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..104
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 104784 MW; 6898BFBD52D5FF4C CRC64;
MSDFVEHKHP DGEDGYDVDD FDVEAAEVDV ADDGETEPVN RKRSFDEMGS EEAAALKQEE
EQVKEEPRDE EENENEDENE DENENEDDNE DENENEDEND DDEDDDLRSR KRRRANQFVD
IEAEVDDEED EEIDEDDEEA ELLREQFLAD DKEAPETERQ DDRLHREFDR RRQETEDQDA
EALAETLKQR YRKTHSVYRG DSATSGTVSQ KLLMPSINDP SIYAIRCSPG REKELVRKLF
DKKRTLARTG RPLDILTVFQ RDSFKGYIYI EAKRAEAIDR ALAGMVNVYP KNRLLVPVRE
YPDLLKQVKS SDVEIVPGLY VRMTRGKYKG DLAIVDNLSE NGLDVRCKLV PRLDYGKNDT
FDRDGRRIKS KVRPPARLFS EQEARAYDSE FLSPGRGPRT YIYRGDDYVD GFLYKDFKLQ
FINTKDVNPT LAELERFNVG DDGIDVSAVA SMKKEQTSAF QPGDKVEVRR GEQARTVGKV
TASSLNEVTI MVTDSGDPRF VNQELTVVAA DLRKVFAPGD HVRVVAGKHA DETGLVIKLE
GDSVVLLSDQ TKADVRVFAN YLVKATDAST STETGGMYDI KDLVQLNAST VGVIVKADKD
LYELLTSDGR LTTVKPSGIA SKLRMTRREQ IATDKNGNTV QVGDTVRELA TDKKREGVVV
HIFKNSLFIQ SHDVSENLGF FVTNCMNVLA VTRDGPKGPD LTKMNPNKVA GPSPAVTARR
GGRDKLIYKD VIVTGGNHKG LMGKVTDTDD VFARIELHTK SKKIKVNKNN LSVIIRGESI
PYLRFIGANN GPQNSGSSMN NQNRFGPAFS SGGKSAWGNG GATPMVGGGG AGGGTSWGGG
ATAWGKTPGG ASTWGGNANS GASTWGGGNG AASTWGSGAN AGASTWGNAN GGVSTWGSNG
NAGNSTWGDN GAGSTWGAGA GAGAGAGAGA GAGSAWGSGS NSTWGNRGGD KSTWGSGSTW
GNK
//
