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Database: UniProt
Entry: A0A1S3U7I6_VIGRR
LinkDB: A0A1S3U7I6_VIGRR
Original site: A0A1S3U7I6_VIGRR 
ID   A0A1S3U7I6_VIGRR        Unreviewed;       366 AA.
AC   A0A1S3U7I6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Transcription elongation factor {ECO:0000256|RuleBase:RU368078};
GN   Name=LOC106762536 {ECO:0000313|RefSeq:XP_014501992.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014501992.1};
RN   [1] {ECO:0000313|RefSeq:XP_014501992.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014501992.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Necessary for efficient RNA polymerase II transcription
CC       elongation past template-encoded arresting sites. The arresting sites
CC       in DNA have the property of trapping a certain fraction of elongating
CC       RNA polymerases that pass through, resulting in locked ternary
CC       complexes. Cleavage of the nascent transcript by S-II allows the
CC       resumption of elongation from the new 3'-terminus.
CC       {ECO:0000256|ARBA:ARBA00025408}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00649, ECO:0000256|RuleBase:RU368078}.
CC   -!- SIMILARITY: Belongs to the TFS-II family.
CC       {ECO:0000256|RuleBase:RU368078}.
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DR   RefSeq; XP_014501992.1; XM_014646506.2.
DR   AlphaFoldDB; A0A1S3U7I6; -.
DR   STRING; 3916.A0A1S3U7I6; -.
DR   EnsemblPlants; Vradi05g05190.1; Vradi05g05190.1; Vradi05g05190.
DR   GeneID; 106762536; -.
DR   Gramene; Vradi05g05190.1; Vradi05g05190.1; Vradi05g05190.
DR   KEGG; vra:106762536; -.
DR   OrthoDB; 1383197at2759; -.
DR   Proteomes; UP000087766; Chromosome 5.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:InterPro.
DR   CDD; cd00183; TFIIS_I; 1.
DR   CDD; cd13749; Zn-ribbon_TFIIS; 1.
DR   Gene3D; 2.20.25.10; -; 1.
DR   Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR   Gene3D; 1.10.472.30; Transcription elongation factor S-II, central domain; 1.
DR   InterPro; IPR035100; TF_IIS-typ.
DR   InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR   InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR   InterPro; IPR003618; TFIIS_cen_dom.
DR   InterPro; IPR036575; TFIIS_cen_dom_sf.
DR   InterPro; IPR017923; TFIIS_N.
DR   InterPro; IPR006289; TFSII.
DR   InterPro; IPR001222; Znf_TFIIS.
DR   NCBIfam; TIGR01385; TFSII; 1.
DR   PANTHER; PTHR11477:SF0; IP08861P-RELATED; 1.
DR   PANTHER; PTHR11477; TRANSCRIPTION FACTOR S-II ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF08711; Med26; 1.
DR   Pfam; PF01096; TFIIS_C; 1.
DR   Pfam; PF07500; TFIIS_M; 1.
DR   PIRSF; PIRSF006704; TF_IIS; 1.
DR   SMART; SM00510; TFS2M; 1.
DR   SMART; SM00509; TFS2N; 1.
DR   SMART; SM00440; ZnF_C2C2; 1.
DR   SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR   SUPFAM; SSF46942; Elongation factor TFIIS domain 2; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR   PROSITE; PS51319; TFIIS_N; 1.
DR   PROSITE; PS00466; ZF_TFIIS_1; 1.
DR   PROSITE; PS51133; ZF_TFIIS_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|RuleBase:RU368078};
KW   Elongation factor {ECO:0000313|RefSeq:XP_014501992.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368078};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00649};
KW   Protein biosynthesis {ECO:0000313|RefSeq:XP_014501992.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW   Transcription {ECO:0000256|RuleBase:RU368078};
KW   Transcription regulation {ECO:0000256|RuleBase:RU368078};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368078};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00472}.
FT   DOMAIN          1..86
FT                   /note="TFIIS N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51319"
FT   DOMAIN          198..321
FT                   /note="TFIIS central"
FT                   /evidence="ECO:0000259|PROSITE:PS51321"
FT   DOMAIN          324..364
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51133"
FT   REGION          89..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   366 AA;  40992 MW;  BC2BCC3534893BDF CRC64;
     MEKELVELYD AAKKAADAAL SGDAEHEESR CIDALEQLKK FPVNYKILVN TQVGKHLKVL
     TKHPRQTIRA FAVDLIEIWK GIIIKETSKN KNGGADGKVE SANGDRSKPG KMQKSPSVKV
     EKGETVKAER NDRNGTSKSE SMKKAQNDVK NEKTDRAASV KVEKSAKEVK PFSGTKKFSS
     SSATPPKLTT MIKSNDATRD KIRELLHEAL SKVSGEADED LVEIVNASDP IRVAVTVESV
     LFEKWGPSNG AQKVKYRSLM FNLKDSNNPD FRRKVLLGVV EPEQLINMTS AEMASEQRKQ
     ENQKITEKAL FECERGMQPK ATTDQFKCGR CGQRKCTYYQ MQTRSADEPM TTYVTCVVCN
     NRWKFC
//
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