ID R9P635_PSEHS Unreviewed; 962 AA.
AC R9P635;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 08-NOV-2023, entry version 42.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN ORFNames=PHSY_004296 {ECO:0000313|EMBL:GAC96712.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC96712.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
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}.
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DR EMBL; DF238805; GAC96712.1; -; Genomic_DNA.
DR RefSeq; XP_012190299.1; XM_012334909.1.
DR AlphaFoldDB; R9P635; -.
DR STRING; 1305764.R9P635; -.
DR GeneID; 24109578; -.
DR eggNOG; KOG1999; Eukaryota.
DR HOGENOM; CLU_003537_1_0_1; -.
DR OrthoDB; 24955at2759; -.
DR Proteomes; UP000014071; 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; 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; 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:UP000014071};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 194..286
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 291..318
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 457..484
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 510..537
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 632..660
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 733..760
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..77
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..119
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 104397 MW; B4DBCA214C42A3FE CRC64;
MEDDPDIKRE DQIKRSSTAN VDETPRVQHG GKRPIDPFAE DDEDDEDERA ARDDDDDEDD
DEDDDDDDDD DDDDDEDDTA RGHRRRAKKQ RRNRFLDVEA EVDDDEEDLD EEEEELARED
GFIEEDIPDD TEDVQRRAAA DNQRLDRFRR QEEDTNAEAL AEELRQRYGK SARYAAQSDY
AEVPQRLLMP SVEDPSLWGV PCKPGRERDI VMTLVRKAMA ENFTSNPMRI ISAFCRDSIP
GRVYVEARRA DDVVKACNGL AGAYARQTTS LHLIPISEMA DLLKLQKVQN EIQVGGWVRI
KRGKYAGDLA QVLDVSENGE EVGLKMIPRI DLNPKDSGLY TDSLGRKRKK GAGSSATTVA
FRPPQRFFNP EEVQKAYPRD TPTKRGTQWV FQNDSYREGY LEKDVRVTGI ITENVNPTLD
EITKFAGESS LEDGINKLAA VDLSLIADAS KKATEALIQP KDQVEIFEGE QAGVYGIVKA
INNEVITIQL EHEDLMDQIV EVPARSVRKR FKPGDHIKVM SGKHADETGL VVKVEDNVTT
FLSDLSMQEV SVFSKDIRQA AEVGSGVNVI SGYELHNLVQ LDAQTVGIIF NIERESFRVL
DQTGQVVTVK PHQISSKKDT SRAFALDHDG NEIRSGDMVK EVAGPFSRLR QGQVLHIYQS
MIVFLHNREY TENGGVFIAR ARSLEPLAPK SVSTKTKKDG GDLSKMNPAL SSLSSGGAND
VRVEGVRRMG GRDMHKGKNV AIIKGPYKTY RGRITETTGN MARIELTSVS KPITVSLDWL
VEKDPITGRS TKLNASGFGG GSGRGGSGRG GYSGSTGGAS SNPYSSGGSS MGGASGYNPY
GGSQPVSAGG GYGGASNGGA GGYGGYSQPV ATSAAAGGGY GGAGGIGGRT PAYNPYAGDG
GKTPAYNPYG DGGKTPAYNP YGDGGKTPAY NPLGDGGKTP AYNAAADGGR TPGYNPYAGD
GW
//
