ID A0A1Q7M7H7_9CREN Unreviewed; 159 AA.
AC A0A1Q7M7H7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Transcription elongation factor Spt5 {ECO:0000256|HAMAP-Rule:MF_00950};
GN Name=spt5 {ECO:0000256|HAMAP-Rule:MF_00950};
GN ORFNames=AUI95_02655 {ECO:0000313|EMBL:OLD08620.1};
OS Crenarchaeota archaeon 13_1_40CM_3_52_4.
OC Archaea; Thermoproteota.
OX NCBI_TaxID=1805097 {ECO:0000313|EMBL:OLD08620.1, ECO:0000313|Proteomes:UP000186346};
RN [1] {ECO:0000313|EMBL:OLD08620.1, ECO:0000313|Proteomes:UP000186346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- FUNCTION: Stimulates transcription elongation. {ECO:0000256|HAMAP-
CC Rule:MF_00950}.
CC -!- SUBUNIT: Heterodimer composed of Spt4 and Spt5. Interacts with RNA
CC polymerase (RNAP). {ECO:0000256|HAMAP-Rule:MF_00950}.
CC -!- SIMILARITY: Belongs to the SPT5 family.
CC {ECO:0000256|ARBA:ARBA00006956}.
CC -!- SIMILARITY: Belongs to the archaeal Spt5 family. {ECO:0000256|HAMAP-
CC Rule:MF_00950}.
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:OLD08620.1}.
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DR EMBL; MNGM01000039; OLD08620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7M7H7; -.
DR Proteomes; UP000186346; Unassembled WGS sequence.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0140673; P:transcription elongation-coupled chromatin remodeling; IEA:InterPro.
DR CDD; cd06091; KOW_NusG; 1.
DR CDD; cd09887; NGN_Arch; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 3.30.70.940; NusG, N-terminal domain; 1.
DR HAMAP; MF_00950; Spt5_arch; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR005100; NGN-domain.
DR InterPro; IPR006645; NGN-like_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR011590; Spt5_arc.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR NCBIfam; TIGR00405; KOW_elon_Spt5; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR SMART; SM00739; KOW; 1.
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:OLD08620.1};
KW Protein biosynthesis {ECO:0000313|EMBL:OLD08620.1};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00950}; Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00950}.
FT DOMAIN 3..87
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 92..119
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
SQ SEQUENCE 159 AA; 17418 MW; 3D84999C7526264D CRC64;
MQKTSIYAVR TTSGQERTVV DLMASRAQPK KLPITAILAP EVIKGYIFVE ATGPHFVDEA
IAGTRHARTR TKGVVSIQAI ERFIVTKPVI EELSVGNLVE VVGGPFRGLR AKITHVDKVK
QEVVIELLEE GFATLPITVH ADYVKLVSRG EDSGRQENS
//
