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Database: UniProt
Entry: T5AC76_OPHSC
LinkDB: T5AC76_OPHSC
Original site: T5AC76_OPHSC 
ID   T5AC76_OPHSC            Unreviewed;      1066 AA.
AC   T5AC76;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN   ORFNames=OCS_04850 {ECO:0000313|EMBL:EQK99437.1};
OS   Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS   caterpillar fungus) (Hirsutella sinensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=911162 {ECO:0000313|EMBL:EQK99437.1, ECO:0000313|Proteomes:UP000019374};
RN   [1] {ECO:0000313|EMBL:EQK99437.1, ECO:0000313|Proteomes:UP000019374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC   TISSUE=Fruit-body {ECO:0000313|EMBL:EQK99437.1};
RX   DOI=10.1007/s11434-013-5929-5;
RA   Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA   Liu X., Wang C.;
RT   "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT   fungus.";
RL   Chin. Sci. Bull. 58:2846-2854(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   -!- 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}.
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DR   EMBL; KE653343; EQK99437.1; -; Genomic_DNA.
DR   AlphaFoldDB; T5AC76; -.
DR   eggNOG; KOG1999; Eukaryota.
DR   HOGENOM; CLU_003537_1_1_1; -.
DR   Proteomes; UP000019374; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006354; P:DNA-templated transcription elongation; IEA:InterPro.
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   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; 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; 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   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:UP000019374};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR036945}.
FT   DOMAIN          324..352
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          485..512
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          538..566
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          661..686
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          748..775
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          858..1021
FT                   /note="Spt5 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01104"
FT   REGION          1..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          724..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          790..1066
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..31
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..109
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..155
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        854..905
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        927..966
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1066 AA;  114648 MW;  CA1B9B40615FFBFD CRC64;
     MAPDEPPRFD DSEDEEDFHP APADLSDEEP ADDEGDRRAK KPVLYNSSAN RDDAAADDDS
     SPPRKPRASG SGGGGDENEP SQHRGGNDDD DDQGDEEEEE DEDEDDEDED VQHGHRRKRR
     RDRRNAFFDI EAEVDDEDEG EDEEKDGEEI EDFIDNAHPD DMAESARLDD DRRHRELDRR
     REMEASMDAE KQAEILRQRY GNRRPAKGFG DSAVVPKRLL LPSVDDPSIW AVRCKEGKER
     EVVLSITKRI EERLGTKDEL AITAAFERGG AQSVMKGFIY VEAQRQTDIL VALDSMLNVY
     PRSKMTLVDI KDMPELLRIT KTPTLEPGAW VRLRRPPKHS GDLAQVVDVT ENGLEAKVRF
     IPRLDYGVRD DALASLTASD GKRKRPGGLA GPRPPQRLFS EVEARKRHPR HIQGNPTTNT
     WSYMGDEFEN GFQVKDVKIQ QLVVTDVNPS LEEVTRFASG AEDGTENLDL KALAASLKDS
     NTLVTYLPGD IIEVYSGEQK GVVGKATNVQ GDIVTMAVTE GDLKGQTIEV PIKGLRKRFK
     VGDHVKVIGG SKFRDEVGTV VKISEDRVTL LTDQTNTEVT VFSKDLREAS DIGGQGSLGQ
     FSLHDLVQLD PTTVGCVVKV DRESLMVLDQ YGDTRQLMPS QIPNKLPKRK QAVAADREGS
     EIRLDDKVKE FTGQQRQGKI IHIHRSYIFL HTNDSTENAG VFVTKASMVN TVAAKGGRVN
     AASSGPDLNA MNPALKESPP PVKTFGRDRA INQTAIIKKG PYKGLLGIVK DTTDTHARVE
     LHTKGKTVTV PRESLSFRDK TSGATIDING RGRGSSGGPS RGPSDRAPSW QGGSRTPMGA
     GNSDRVPAWG SRTPTAANGR TPAWKAQDYS GSRTPAWADG SRTVNPYDGS RTAYGSGSRT
     PAWQSGARTP AAGDAFGAGS RTPAYGGGTD SWMSGSKTPA WGSSAPTPGA SGNDSWGYTP
     GATSSAAYDA PTPGAGMGAP TPGALNAPTP GAYSAPTPAA NAPTPGGNWQ GGWGADSAPT
     PGAGAPTPGA SGYVSSAGYY GAPTPAAYGG TPETPAASGP IYTDDD
//
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