ID F4RBH1_MELLP Unreviewed; 264 AA.
AC F4RBH1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Transcription elongation factor S-II {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=MELLADRAFT_33850 {ECO:0000313|EMBL:EGG10362.1};
OS Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN [1] {ECO:0000313|Proteomes:UP000001072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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|PROSITE-ProRule:PRU00649}.
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DR EMBL; GL883095; EGG10362.1; -; Genomic_DNA.
DR RefSeq; XP_007406663.1; XM_007406601.1.
DR AlphaFoldDB; F4RBH1; -.
DR STRING; 747676.F4RBH1; -.
DR EnsemblFungi; EGG10362; EGG10362; MELLADRAFT_33850.
DR GeneID; 18927344; -.
DR KEGG; mlr:MELLADRAFT_33850; -.
DR VEuPathDB; FungiDB:MELLADRAFT_33850; -.
DR eggNOG; KOG1105; Eukaryota.
DR HOGENOM; CLU_037637_2_0_1; -.
DR InParanoid; F4RBH1; -.
DR OrthoDB; 1383197at2759; -.
DR Proteomes; UP000001072; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001139; F:RNA polymerase II complex recruiting activity; IEA:EnsemblFungi.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:EnsemblFungi.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001193; P:maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IEA:EnsemblFungi.
DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0031440; P:regulation of mRNA 3'-end processing; IEA:EnsemblFungi.
DR GO; GO:0031564; P:transcription antitermination; IEA:EnsemblFungi.
DR GO; GO:0006362; P:transcription elongation by RNA polymerase I; IEA:EnsemblFungi.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IEA:EnsemblFungi.
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; 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; IPR001222; Znf_TFIIS.
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; 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; PS51133; ZF_TFIIS_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00649};
KW Reference proteome {ECO:0000313|Proteomes:UP000001072};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00472}.
FT DOMAIN 1..57
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51319"
FT DOMAIN 104..216
FT /note="TFIIS central"
FT /evidence="ECO:0000259|PROSITE:PS51321"
FT DOMAIN 219..264
FT /note="TFIIS-type"
FT /evidence="ECO:0000259|PROSITE:PS51133"
FT REGION 54..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGG10362.1"
SQ SEQUENCE 264 AA; 29921 MW; 58332BB788A6B56B CRC64;
VKNILNRLRK EVVPTEELIR TTKIGISVGK QRQNPDHEIS KLAKLIVNEW KNGVKKEPNH
PTHSSTPTHL ASGSQPQKSF TKRTGPRSSK TETHLKFESL QDKVRDGSMK SVFDALIFDS
DAPADLVYER AKSIESEVNR TNDSNGYKNK MRSLIFNLKD KNNPGLREAV VSGEISSMKL
CSMGPADMAS EERKAQDRKL AEENLFKARG AGPQQAETDA FRCGRCGQRK CTYYQMQTRS
ADEPMTVSFE FFFYMTSFFG YYID
//
