ID   TCEA2_BOVIN             Reviewed;         300 AA.
AC   Q148K0;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Transcription elongation factor A protein 2;
DE   AltName: Full=Transcription elongation factor S-II protein 2;
GN   Name=TCEA2;
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=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-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   -!- SUBUNIT: Interacts with the basal transcription factor GTF2B. Interacts
CC       with REXO1 (By similarity). {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}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; BC118232; AAI18233.1; -; mRNA.
DR   RefSeq; NP_001068797.1; NM_001075329.1.
DR   AlphaFoldDB; Q148K0; -.
DR   SMR; Q148K0; -.
DR   STRING; 9913.ENSBTAP00000029107; -.
DR   PRIDE; Q148K0; -.
DR   GeneID; 507729; -.
DR   KEGG; bta:507729; -.
DR   CTD; 6919; -.
DR   eggNOG; KOG1105; Eukaryota.
DR   InParanoid; Q148K0; -.
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; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..300
FT                   /note="Transcription elongation factor A protein 2"
FT                   /id="PRO_0000285503"
FT   DOMAIN          6..83
FT                   /note="TFIIS N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT   DOMAIN          139..255
FT                   /note="TFIIS central"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00651"
FT   ZN_FING         258..298
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   REGION          84..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         262
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         290
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         293
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   MOD_RES         60
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23193"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23193"
FT   CROSSLNK        58
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15560"
SQ   SEQUENCE   300 AA;  33642 MW;  4202E89DA81B7DED CRC64;
     MMGKEEEIAR IARRLDKMVT KKSAEGAMDL LRELKAMPVT LHLLQSTRVG MSVNALRKQS
     SDEEVVTLAK SLIKSWKKLL DASDAKARER RRGGSLPTSS SKEASEAQDP SRKRPELPRM
     PSTPRITTFP PVPVTCDAVR TKCREMLTAA LQTDHDHVAI GADCECLAGQ IEECIFRDVG
     NTDMKYKNRV RSRLSNLKDA KNPGLRRKVL CGAITPQQIA VMTSEEMASD ELKEIRKAMT
     KEAIREHQMA RTGGTQTDLF TCGKCRKKNC TYTQVQTRSS DEPMTTFVVC NECGNRWKFC