ID A0A397TQY7_9GLOM Unreviewed; 1110 AA.
AC A0A397TQY7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 08-NOV-2023, entry version 16.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181};
DE AltName: Full=Chromatin Elongation factor SPT5 {ECO:0000256|ARBA:ARBA00029865, ECO:0000256|ARBA:ARBA00031006};
DE AltName: Full=Transcription elongation factor spt5 {ECO:0000256|ARBA:ARBA00021370};
GN ORFNames=C1645_752485 {ECO:0000313|EMBL:RIA97284.1};
OS Glomus cerebriforme.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Glomus.
OX NCBI_TaxID=658196 {ECO:0000313|EMBL:RIA97284.1, ECO:0000313|Proteomes:UP000265703};
RN [1] {ECO:0000313|EMBL:RIA97284.1, ECO:0000313|Proteomes:UP000265703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 227022 {ECO:0000313|EMBL:RIA97284.1,
RC ECO:0000313|Proteomes:UP000265703};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SIMILARITY: Belongs to the SPT5 family.
CC {ECO:0000256|ARBA:ARBA00006956}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RIA97284.1}.
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DR EMBL; QKYT01000031; RIA97284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397TQY7; -.
DR STRING; 658196.A0A397TQY7; -.
DR Proteomes; UP000265703; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 Gene3D; 2.30.30.30; -; 2.
DR Gene3D; 3.30.70.940; NusG, N-terminal domain; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR005100; NGN-domain.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR039659; SPT5.
DR InterPro; IPR024945; Spt5_C_dom.
DR InterPro; IPR022581; Spt5_N.
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 SMART; SM01104; CTD; 1.
DR SMART; SM00739; KOW; 4.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000265703}.
FT DOMAIN 387..414
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 438..465
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 663..690
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 786..949
FT /note="Spt5 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01104"
FT DOMAIN 1048..1075
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..62
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1110 AA; 124151 MW; 775B9CE9C405C539 CRC64;
MSKRRQNVSD DDESRLNETD GGWSAGEEVG EESVQDQQND YDEYDDFEQE SEGLEEDEDD
DYEDRRRDKK RHKGNKNDPS KFILNEADVD DEEEEEDEDE DAIFGKEDFI DNREVETELS
AYHRDTTRRA DIDIERSVFV EENFDAERVA QVLNERYRRT AGRLSDEDDD LTKPELASVD
KLFAVKCRKG HVFHAIEKLE NLKKLRSDPL KIKKVIPIDG IEDFVYIEAD KEQDVQNAAM
RCNKYLYSSK KFIKRLSPKE KQDLMAPKRP RLNIQNGSFV RINKRDEYYG DLARVISYNT
DEVVEVEIIP RILVDQDGAS LKRKRKDTDT YIKTYNRGYL KVKYKIKDLI YSNMDLLLHD
VEDFLKAKFD NESIMMELSN VASKITVYEI QDEIKVLQGS LKSSVGSVIS VNDGVLTATD
KDNSNKIFKV NSEECVKNIN VHDYVQITNG PYQGQSGFVF NCDRHVMTMY LDHTNKQISV
FAKDLKKGVQ NSINNEFGGY RYFDLVQLKD SSVGIIIDIR KAQKNYEYDV LNTENSLIKS
VTAARITRTL IDTKLPAFKK GDQVSMTKSE SFNNKQPSIY EVFRINETNV FVRTYDDDTN
LGFSCFKTKD LKLKYESARS SNNKINDQQI TFPGQRSRGS NNNNRGGRGR GRGRGRDRSV
YQHPLVNKRV QASQGALKGY QGTVKGVYGN MADVEFDAKL TTVKVELGQL FHVNEKGEAL
DPVIPRNHES NRNSMDMSPG LGSYSEPSWT TGLSKQQKSW GYSLGSAMTP NPHLLDNTNS
GLNMDGSKTP ALHSSGSLSG SKTPALRNSS ANNSSNNASL GSKTPAWDLG SKTPAYGLMS
DGSKTPAWDS GSHTPHSSGI VGGTGGTSSN SVNNISNIFG GGSSSNSTTN TTNTTINIAT
AETPGGYSAV ATPAADGPNY PPVFTPANTG NLMPPTPRPF TPGNIPMTPA NMIPQTPFAT
QHSANHAVHP GRDPKKPPDV KDFGEWLTPG IEVRIVPIDG IQSFENGRYD NRVGVVVRLE
RSNSGSIKLD DSDGMTISVE QKYLKPTEVQ RRDDIKVIFG EHKGELGFLA AIDNLEGVVR
SQGGDHSFIN IYYLAKYRGN EIEDLMQISQ
//
