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Database: UniProt
Entry: A0A1E5RAH4_9ASCO
LinkDB: A0A1E5RAH4_9ASCO
Original site: A0A1E5RAH4_9ASCO 
ID   A0A1E5RAH4_9ASCO        Unreviewed;       293 AA.
AC   A0A1E5RAH4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Transcription elongation factor {ECO:0000256|RuleBase:RU368078};
GN   ORFNames=AWRI3579_g2565 {ECO:0000313|EMBL:OEJ83871.1};
OS   Hanseniaspora osmophila.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX   NCBI_TaxID=56408 {ECO:0000313|EMBL:OEJ83871.1, ECO:0000313|Proteomes:UP000095728};
RN   [1] {ECO:0000313|Proteomes:UP000095728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI3579 {ECO:0000313|Proteomes:UP000095728};
RX   PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA   Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT   "Genome sequences of three species of Hanseniaspora isolated from
RT   spontaneous wine fermentations.";
RL   Genome Announc. 4:E01287-E01287(2016).
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}.
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:OEJ83871.1}.
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DR   EMBL; LPNM01000008; OEJ83871.1; -; Genomic_DNA.
DR   STRING; 56408.A0A1E5RAH4; -.
DR   InParanoid; A0A1E5RAH4; -.
DR   OrthoDB; 1383197at2759; -.
DR   Proteomes; UP000095728; 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:OEJ83871.1};
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:OEJ83871.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095728};
KW   Transcription {ECO:0000256|RuleBase:RU368078};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   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..80
FT                   /note="TFIIS N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51319"
FT   DOMAIN          134..248
FT                   /note="TFIIS central"
FT                   /evidence="ECO:0000259|PROSITE:PS51321"
FT   DOMAIN          251..291
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51133"
FT   REGION          83..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   293 AA;  33278 MW;  EDA99BA37036CF98 CRC64;
     MDSKTVLQYA KDLEAMKNQE DKVLPLLTTL EKDFGQPTEK ILRETKIGVV VNGFKKSTNP
     EIANKAKRII IAWKEAITKQ KKSKVKASSG APXSGSSTST KKTQQQSNDE DSMPEKPRSS
     KIDGVNTTVH NVKLRDMVIK AVYDALCKES RKSSDDILKI SVGIEDALNK YSDKDEKKYK
     DKYRVVFSNI ISKTNRDLKK KILNQDISAE YLVNCDPMDL APEHLQKKLE EIKKKNLHDA
     QGATIERSVT DRFQCGKCKE RKVSYYQLQT RSADEPLTTF CTCENCGNRW KFS
//
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