ID   TCEA3_BOVIN             Reviewed;         349 AA.
AC   Q2KI09;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Transcription elongation factor A protein 3;
DE   AltName: Full=Transcription elongation factor S-II protein 3;
GN   Name=TCEA3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) 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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649,
CC       ECO:0000255|PROSITE-ProRule:PRU00651}.
CC   -!- SIMILARITY: Belongs to the TFS-II family. {ECO:0000305}.
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DR   EMBL; BC112812; AAI12813.1; -; mRNA.
DR   RefSeq; NP_001039825.1; NM_001046360.1.
DR   AlphaFoldDB; Q2KI09; -.
DR   SMR; Q2KI09; -.
DR   STRING; 9913.ENSBTAP00000004501; -.
DR   PaxDb; Q2KI09; -.
DR   PRIDE; Q2KI09; -.
DR   GeneID; 533803; -.
DR   KEGG; bta:533803; -.
DR   CTD; 6920; -.
DR   eggNOG; KOG1105; Eukaryota.
DR   InParanoid; Q2KI09; -.
DR   OrthoDB; 1579101at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IBA:GO_Central.
DR   Gene3D; 1.10.472.30; -; 1.
DR   Gene3D; 1.20.930.10; -; 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   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; SSF46942; SSF46942; 1.
DR   SUPFAM; SSF47676; SSF47676; 1.
DR   TIGRFAMs; TIGR01385; TFSII; 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   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..349
FT                   /note="Transcription elongation factor A protein 3"
FT                   /id="PRO_0000285504"
FT   DOMAIN          5..82
FT                   /note="TFIIS N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT   DOMAIN          188..304
FT                   /note="TFIIS central"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00651"
FT   ZN_FING         307..347
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   REGION          80..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..134
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         314
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         339
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         342
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   MOD_RES         115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75764"
FT   MOD_RES         141
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75764"
SQ   SEQUENCE   349 AA;  39159 MW;  C98F510EC94DA3B4 CRC64;
     MGQEEELLRI AKKLEKMVAR KKTEGALDLL KKLGSWQMSI QLLQTTRIGV AVNGVRKHCS
     NKEVVALAKV LIRNWKQLLD SPATPKGEKG EERVKAKKKE KGLDCSDWKP ETSLSPPRKK
     RVEEPKDRRD SVDSKSSATS SPKRPSMERS NSSKSKAETP RTPSSPSSPT FAPSVCLLAP
     CYLTGDSVRD KCVEMLSAAL KADDDYKDYG VNCDKMASEI EDHIYQELKS TDMKYRNRVR
     SRISNLKDPR NPGLRRNVLS GAISAGLIAK MTAEEMASDE LRELRNAMTQ EAIREHQMAK
     TGGTTTDLFQ CSKCKKKNCT YNQVQTRSAD EPMTTFVLCN ECGNRWKFC