ID C0NKQ4_AJECG Unreviewed; 306 AA.
AC C0NKQ4;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Transcription elongation factor {ECO:0000256|RuleBase:RU368078};
GN ORFNames=HCBG_03734 {ECO:0000313|EMBL:EEH08445.1};
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH08445.1, ECO:0000313|Proteomes:UP000001631};
RN [1] {ECO:0000313|Proteomes:UP000001631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC {ECO:0000313|Proteomes:UP000001631};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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 EMBL; GG663366; EEH08445.1; -; Genomic_DNA.
DR AlphaFoldDB; C0NKQ4; -.
DR STRING; 447093.C0NKQ4; -.
DR VEuPathDB; FungiDB:I7I50_07442; -.
DR HOGENOM; CLU_037637_1_1_1; -.
DR InParanoid; C0NKQ4; -.
DR OrthoDB; 1383197at2759; -.
DR Proteomes; UP000001631; Unassembled WGS sequence.
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|EMBL:EEH08445.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU368078};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00649}; Protein biosynthesis {ECO:0000313|EMBL:EEH08445.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001631};
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..82
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51319"
FT DOMAIN 147..262
FT /note="TFIIS central"
FT /evidence="ECO:0000259|PROSITE:PS51321"
FT DOMAIN 265..305
FT /note="TFIIS-type"
FT /evidence="ECO:0000259|PROSITE:PS51133"
FT REGION 82..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 306 AA; 34032 MW; B7A7F1A36287DB7C CRC64;
MDVKEIEFKS KALTKAATSG ETPATLISLL RELQKGVRPT EDLLRSTKIG IIVNKLKQHK
SPDVARLSSE IVSKWRSEVN KQKVTVGGSP AASQRSSDSP KQTPNGTASP ASTGAAASDR
LAKSTVPPDK RSWKTDQLTI THTQNKSRDS CIGLIYDGLC LHSTEPPRVV LQKAIQVELA
AYNAFGPETK EQYRTKMRSL FQNLKNKSNP DLRVRVLSNE ITPDKFVRMT HDELKSDAQR
EEERRIHKEN MDKAMVAKAE RSISTSLQCG KCGQKKVTYT EAQTRSADEP MTLFCTCVVC
GKSWRQ
//
