ID A0A2H3E9M3_ARMGA Unreviewed; 1083 AA.
AC A0A2H3E9M3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN ORFNames=ARMGADRAFT_1003850 {ECO:0000313|EMBL:PBL03041.1};
OS Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=47427 {ECO:0000313|EMBL:PBL03041.1, ECO:0000313|Proteomes:UP000217790};
RN [1] {ECO:0000313|Proteomes:UP000217790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ar21-2 {ECO:0000313|Proteomes:UP000217790};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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; KZ293644; PBL03041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3E9M3; -.
DR STRING; 47427.A0A2H3E9M3; -.
DR InParanoid; A0A2H3E9M3; -.
DR OMA; PYPVGYM; -.
DR OrthoDB; 24955at2759; -.
DR Proteomes; UP000217790; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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; 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; 6.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000313|EMBL:PBL03041.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036945};
KW Protein biosynthesis {ECO:0000313|EMBL:PBL03041.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217790};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 161..251
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 256..283
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 415..442
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 468..495
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 590..615
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 681..708
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 779..935
FT /note="Spt5 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01104"
FT DOMAIN 1026..1053
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..89
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 117887 MW; 8506AAE62C2060FC CRC64;
MQNDADDALH DEEEEDAQSE TEHSKPRRRH YDEDEDDEDE EDEEEEEEEA SGRKPKKRKR
KQGASRFIDL EAEVSDEDEG EEDDEDYGGD GFIEHVDGGV DEDVGRAHHA RLDSKTFDGE
DRTAEEIATD LKHRYGGRNA VRYSGDMNEI PQRLLMPSVH DASLWQVKVK PGRERDIVFT
LMRKFIDVEF TARPLQILSA FERDTLPGMI YVEARSSKSV KDAVSGLNGA AQNVKVNLVP
IEEMASLLQI RKKELTVTPG SWVRIRRGKY LGDLAQVVDV TENGEDVGLK FIPRIDLNPR
DDGSLDALGK KRKKGSTAAG TMRPPQKLFN FEEVVKVYGR QAVAKRNQVY VFQSDTYKDG
FIEKDFKLNA LSLDDVNPTL DEITQFSRRQ DGMGGENPVD LSIIAEASRK AAVSVLQPGD
HVEVFEGEQA GVHGTVEEVS GDVVTITAVG VDIEGQKVDI PARSVRKRFK PGDHVKVMTG
KNADETGLVV AVADNIVTFL SDMSMQEVSV FSKDLREAAE VGSGTNIVGD YELHDLVQLD
LQTVGVIFKT DRDSFRVLDQ NGQVRIVQPR QITMRRDSRR AIATDHDGHE LRVEDNVKEV
DGEGRKGQVL HIHQSFFAFL YNREISENGG VFVTRARSLV SLAPKSSVFP KPGADLSKMN
PALALHPGGM AGSSIGRGPR DRMIGTIVQI TRGPHKGYVG TIKDTNGPIA RVELNTSNRV
VTIEKTKLVE KITPGSAPTR SFDRLKAMGP PGEPGKSWGT RSVNPYASGG STPTWGGGGG
RTPAWGGGGR TPNPSSDSRT PAWNASSRTP NPYANNAQTP AWNVSSRTPN PYADGGKTPA
WNVSSRTPNP YASNSGGATP ARNTNTWGGA TPGRNAWDTS TGWGDSWNAA PTPAAATSPA
YAAPTPGPGT YDVATPFSYG TGAMSAQTPA SAPTPAAAGW REEDPEGLSE EWLLDTALGN
VLQRIKIRIE GSRNYNYLDG KYEGLTGRVM AATRTGANME QTAMIAFDNG EQRSILMKFV
VPMQPSGVDG ENGVMLDGPY KGREARVRSL SEDGMITCHG YFGFAEISQD KFAILTAAPA
APA
//
