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SPT5_CANAL
ID   SPT5_CANAL              Reviewed;         956 AA.
AC   Q5ALX3; A0A1D8PGF9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Transcription elongation factor SPT5;
DE   AltName: Full=Chromatin elongation factor SPT5;
GN   Name=SPT5; OrderedLocusNames=CAALFM_C201480WA;
GN   ORFNames=CaO19.1453, CaO19.9028;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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 gene
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the SPT4-SPT5 complex. Interacts with RNA
CC       polymerase II (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SPT5 family. {ECO:0000305}.
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DR   EMBL; CP017624; AOW27194.1; -; Genomic_DNA.
DR   RefSeq; XP_722503.1; XM_717410.1.
DR   AlphaFoldDB; Q5ALX3; -.
DR   SMR; Q5ALX3; -.
DR   BioGRID; 1218941; 1.
DR   STRING; 237561.Q5ALX3; -.
DR   PRIDE; Q5ALX3; -.
DR   GeneID; 3635847; -.
DR   KEGG; cal:CAALFM_C201480WA; -.
DR   CGD; CAL0000192268; SPT5.
DR   VEuPathDB; FungiDB:C2_01480W_A; -.
DR   eggNOG; KOG1999; Eukaryota.
DR   HOGENOM; CLU_003537_1_0_1; -.
DR   InParanoid; Q5ALX3; -.
DR   OMA; FLAWDVE; -.
DR   OrthoDB; 828863at2759; -.
DR   PRO; PR:Q5ALX3; -.
DR   Proteomes; UP000000559; Chromosome 2.
DR   GO; GO:0032044; C:DSIF complex; IBA:GO_Central.
DR   GO; GO:0033553; C:rDNA heterochromatin; IEA:EnsemblFungi.
DR   GO; GO:0003677; F:DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
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: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:0009267; P:cellular response to starvation; IMP:CGD.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR   GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR   GO; GO:0008298; P:intracellular mRNA localization; IEA:EnsemblFungi.
DR   GO; GO:0060195; P:negative regulation of antisense RNA transcription; 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 from RNA polymerase I promoter; IEA:EnsemblFungi.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:2000232; P:regulation of rRNA processing; IEA:EnsemblFungi.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
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; -; 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_dom.
DR   InterPro; IPR036735; NGN_dom_sf.
DR   InterPro; IPR039385; NGN_Euk.
DR   InterPro; IPR014722; Rib_L2_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; PTHR11125; 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; SSF50104; 1.
PE   3: Inferred from homology;
KW   mRNA processing; Nucleus; Reference proteome; Transcription.
FT   CHAIN           1..956
FT                   /note="Transcription elongation factor SPT5"
FT                   /id="PRO_0000238557"
FT   REGION          1..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          805..835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..956
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..93
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..133
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..834
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        892..956
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   956 AA;  105824 MW;  5A4F65FD44643723 CRC64;
     MSDSDLPVQV KKEPSFANDD DLTFDEEFRR AGDQENKEVE NPDDGRSLKR TREESEQEEN
     NEKEQDQEAG QDEEEQDEDE EEEEDDEEED EEDEVSSRRK RRRGANQFFD IEAEVDDEEE
     DEEDEDEEAE LMREEFITDD HAPVETVEKM PQDDRLHRQY DNRRQQAEDQ DAEQLAETLK
     QRYRKTHSVY RGETAASGTV SQKLLMPSIN DPSIYAIRCT PGREKELVRK LYEKKRTLER
     QGNPLDILTV FQRDAFTGYI YIEAKRPDAI DKALVGMVNV FVRDKLLVPV KEYPDLLKQV
     KSSDVEIRPG IYVRIKRGIY RGDLAIVDNL SENGLDVRCQ VVPRLDYGQN DEIGPDGKVI
     KSKIKPLPAL FSEQKARMYD PYKLQMGRVP NSFIYRGNEY YDGYLYKDFK LQFIQTKDVN
     PTLEELDRFQ NQNDEDGLNL QAIAATLKGN NAGEGKSSTA FQPGDKVEIR RGEQAKTIGI
     VVETALNEIT IKVTDSGDPR FVDQRLTVPA NDLRKIFYEG DHVRIVEGKH FDETGLVIKI
     DGDSVVIVSD QTKEDVRVFA NYLVKATDAS SNFDLLNSKY DIKDLVELSG LTVGVIIKAE
     KNIFDVLTTD GRLISVRQSG IASKLKQSRR EQVATDRNGT TIRVGDTVKE LLGEKSREGA
     ILHIYKNALF IKSNEIVENL GIFVANRMNV TTVATKDSTV SKSLGPDLTS MNPNLRLPNP
     VAVAGLKTRV GGRDKLLYKD VAVTSGSYKG LKGKVTEADD LYARIELHTK SKKIKVLKNN
     LNVIVHGQPV PYLRFIGAAP EFSQPTPPTY GSSSGGRSAW NGGMTPSVSA GNGGVSAWGG
     SRGGFGGDGG KTPAYGAGGA STWGGASAWG GGAGGSSAWG GIKGAGSVWD RSKGGSSASS
     GNQGGNTAWD RNKGGNSTWD RSKGGSSSWE SGSTWEGGNN TTWGSKKGNT SAWGRN
 
 
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