ID C5M5V9_CANTT Unreviewed; 980 AA.
AC C5M5V9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN ORFNames=CTRG_01240 {ECO:0000313|EMBL:EER34379.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER34379.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER34379.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
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}.
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DR EMBL; GG692396; EER34379.1; -; Genomic_DNA.
DR RefSeq; XP_002546934.1; XM_002546888.1.
DR AlphaFoldDB; C5M5V9; -.
DR STRING; 294747.C5M5V9; -.
DR EnsemblFungi; CTRG_01240-t43_1; CTRG_01240-t43_1-p1; CTRG_01240.
DR GeneID; 8297512; -.
DR KEGG; ctp:CTRG_01240; -.
DR VEuPathDB; FungiDB:CTRG_01240; -.
DR eggNOG; KOG1999; Eukaryota.
DR HOGENOM; CLU_003537_1_0_1; -.
DR OrthoDB; 24955at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0032044; C:DSIF complex; IEA:EnsemblFungi.
DR GO; GO:0033553; C:rDNA heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:EnsemblFungi.
DR GO; GO:0001042; F:RNA polymerase I core binding; IEA:EnsemblFungi.
DR GO; GO:0001179; F:RNA polymerase I general transcription initiation factor binding; IEA:EnsemblFungi.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IEA:EnsemblFungi.
DR GO; GO:0019843; F:rRNA binding; IEA:EnsemblFungi.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:EnsemblFungi.
DR GO; GO:0070990; F:snRNP binding; IEA:EnsemblFungi.
DR GO; GO:0003711; F:transcription elongation factor activity; IEA:EnsemblFungi.
DR GO; GO:0030619; F:U1 snRNA binding; IEA:EnsemblFungi.
DR GO; GO:0030620; F:U2 snRNA binding; IEA:EnsemblFungi.
DR GO; GO:0030621; F:U4 snRNA binding; IEA:EnsemblFungi.
DR GO; GO:0030623; F:U5 snRNA binding; IEA:EnsemblFungi.
DR GO; GO:0017070; F:U6 snRNA binding; IEA:EnsemblFungi.
DR GO; GO:0008298; P:intracellular mRNA localization; IEA:EnsemblFungi.
DR GO; GO:2001208; P:negative regulation of transcription elongation by RNA polymerase I; IEA:EnsemblFungi.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:EnsemblFungi.
DR GO; GO:2001209; P:positive regulation of transcription elongation by RNA polymerase I; IEA:EnsemblFungi.
DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:2000232; P:regulation of rRNA processing; IEA:EnsemblFungi.
DR GO; GO:0090262; P:regulation of transcription-coupled nucleotide-excision repair; IEA:EnsemblFungi.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:EnsemblFungi.
DR GO; GO:0140673; P:transcription elongation-coupled chromatin remodeling; IEA:InterPro.
DR CDD; cd06081; KOW_Spt5_1; 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; 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:UP000002037};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 193..282
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 288..315
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 441..468
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 497..524
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 622..648
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 715..742
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..74
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..112
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 106824 MW; C801674119C03D93 CRC64;
MSDSEDQNQI GSEPGVPQED DLTFDEEFRR AADQEDGEET QQSKRPRENE EVDEEDQEEE
EEEEEEDDDE DDEEDEVSHK RKRRRGANQF FDIEAEVDDE DEDDDEDDEE AEMLREEFIT
DDHAPIETVE RVDTDDRLHR QFDNRRQKVQ DEDAEKIAEE LKQRYRKSHT AYRGETSASG
TVSQKLLMPS INDPSIYAIR VSPGKEKELV RKLYKKKRTL ERQGTPLDIL TVFQRDAFTG
YIYIEAKRPD AIDRALEGMV NVFMRDKLLV PVKEYPDLLK QVKTTDVEVV PGIYVRIKRG
AYKGDLAIVD NLSENGLDVR CKVVPRLDYG VNDTLDKNGK RVKSKIRPQQ ALFSEHKART
YDPEKLQNGS GRGHFRYANN DYIDGFLYKD FRIQFLQTQD VHPSLEELDK LQIKTDEDGL
NLAAIAATLK NNKGDGKSST AFQPGDKVEI RRGEQAKTIG LVTEAALTEV TIKVTDSGDP
KFVNQRLTVP ASDLRKIFNE GDHVRVVEGR HLDETGLVIK IDGDSVIFVS DQTREDVKVF
ANYLIKATDA SSNVDQMKSN YDIKDLVELS SLTVGVIVKA EKNIFGVLTT DGRLIDVKPS
GIASKIIQSR REQVATDRHG MTIRVGDTVK ELLGDKSREG AIVHIYKNSL FIKSTEVIEN
LGIFVANRMN VTTVSTKDAM VSKSLGPDLT SMNPNLRLPN PSAMAGLKTR IGGRDKLIYK
DVQVTSGSYK GLKGKVTDAD DEFARIELHT KSKKIKVRKQ HLNVMVHGEP VPYMRFIGAA
PDERFGAPAM PPTFSSGGRS TWGGATPAVA GGVSNGGASS WGGDRAGGAS TWGGKTPAYG
SAGGKTPAYG SAAAGGASTW GGAGAGGAST WGGAGGASSW GGNRGGGAST WGGNRGGASA
WGGNRGGASA WGGNKGNTSA WGGNQERGNT SKWGSNNGGS GNSGAESAWG GNGGASAWGG
GGNSTWGSKK GNNSTWEGNN
//
