ID D4ANY5_ARTBC Unreviewed; 1079 AA.
AC D4ANY5;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN ORFNames=ARB_05952 {ECO:0000313|EMBL:EFE34996.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE34996.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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}.
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:EFE34996.1}.
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DR EMBL; ABSU01000004; EFE34996.1; -; Genomic_DNA.
DR RefSeq; XP_003015641.1; XM_003015595.1.
DR AlphaFoldDB; D4ANY5; -.
DR STRING; 663331.D4ANY5; -.
DR GeneID; 9525922; -.
DR KEGG; abe:ARB_05952; -.
DR eggNOG; KOG1999; Eukaryota.
DR HOGENOM; CLU_003537_1_1_1; -.
DR OMA; PYPVGYM; -.
DR OrthoDB; 24955at2759; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 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:UP000008866};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 232..324
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 328..355
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 490..517
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 543..571
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 666..691
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 757..784
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 868..1021
FT /note="Spt5 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01104"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..32
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..121
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 116421 MW; 7797F6F1550F7E7F CRC64;
MSHPGNEQQF ASEDEEDFNP APAGDSEPEA EDDQQDNRSG GKHIDNDDGQ EVGKNKKEDD
EENGDEVKKM NDGENGDLNT NESQQARGED EAGAEDDDEG EPEGDNEDDD EEEEEEEEDE
EAVTGRPRKR RRHGLGAFFE EEAEVDDEDE AEDEEDEIEA GFVHHDDEVV LPAGAETDDR
RHRELDRKRD MDATMDAEQQ AQALKERYGR NRASGADLVV VPKRLLLPSV DDPSIWGVKC
RPGKEREIVF SIIKRMEERP LGSRNPIKII SAFERGGTMA GYIYVEARKQ ADIIDALDGM
SNIYVRSKMT LISVKEMPDL LRVKKSEELT PGGWVRIKRG RYQGDLAQLE EVETNGLNVT
VRLVPRLEYG LNEDSNAPAL DPKRKRIGGG SSAIARPPQR LFSEAEAKKR HSKYLSATSS
LGGKSWSYLG DTYVDGFLIK NMKVQHLITK NVNPQLDEVT KFARGADDGT SNLDLASLAA
TIKNTTEEDA YLVGDTVEVF AGEQRGVVGQ TVATRGDIVT IKVTQGELQG QHIDVPTKGL
RKRFSEGDHV KVIGGSKYRD ELGMVVRIKD DRVTILTDMT MQEITVFSKD LREADDIGVD
GKLGQYDVHD LVQIDQTTVG CVVKLDRESM RVIDQNGSTQ IVLPSRVLGK IEHRRHAVTT
DRNGSEIKCG DTVKEVTGEQ RTGTILHIHR AFLFCTSKVV GDNAGIMVTR AINVTTVATS
GSKLGRSAPD LSKMNPALQK NGMNGSGMPP PRTFGRDRLV GKTVHIRRGP FKGLLGIVKD
TTDIIARVEL HSVSKVVPVE KENLSVKDPI TGQPVDINRF GGRGGGAPRV PQSMATGRAG
PQDAAWQGGR TPIAMGDSSR TPAWRASSSR TPAWNAAVGS RTPAWKAEGS RTANPYDGNR
TSYGGFGGRT PAWTSGTKTP HDAGSGFSGG SSNSGFDAFM AGSRTPGHPG AMAANSGSRT
PAWGHSGSSS SHLSANAGRA FDAPTPGGDY AAPSPAPFAS APTPGATAAT PRAWPDNAPT
PGASTFAGKR MDGDAYDAPT PAGDHRPYDA PTPAIGMGFP ATPGAMDDAP RYAEGTPSP
//
