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Database: UniProt
Entry: A0A183T0S2_SCHSO
LinkDB: A0A183T0S2_SCHSO
Original site: A0A183T0S2_SCHSO 
ID   A0A183T0S2_SCHSO        Unreviewed;       314 AA.
AC   A0A183T0S2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Transcription elongation factor {ECO:0000256|RuleBase:RU368078};
GN   ORFNames=SSLN_LOCUS10070 {ECO:0000313|EMBL:VDL96455.1};
OS   Schistocephalus solidus (Tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX   NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0001044601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SSLN_0001044601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL96455.1, ECO:0000313|Proteomes:UP000275846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NST_G2 {ECO:0000313|EMBL:VDL96455.1,
RC   ECO:0000313|Proteomes:UP000275846};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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|ARBA:ARBA00009647, ECO:0000256|RuleBase:RU368078}.
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DR   EMBL; UYSU01035629; VDL96455.1; -; Genomic_DNA.
DR   STRING; 70667.A0A183T0S2; -.
DR   WBParaSite; SSLN_0001044601-mRNA-1; SSLN_0001044601-mRNA-1; SSLN_0001044601.
DR   Proteomes; UP000050788; Unplaced.
DR   Proteomes; UP000275846; 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: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   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368078};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00649}; Reference proteome {ECO:0000313|Proteomes:UP000275846};
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          2..81
FT                   /note="TFIIS N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51319"
FT   DOMAIN          148..263
FT                   /note="TFIIS central"
FT                   /evidence="ECO:0000259|PROSITE:PS51321"
FT   DOMAIN          266..306
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51133"
FT   REGION          81..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   314 AA;  35713 MW;  95B77D6833C6D907 CRC64;
     MEVTEKIVRK LDKMMKRNSI DNELTLKYLH RLQETDMTLD ILTKTGIGII INKIRKETDC
     SEVTSLGKQL IKEWKKLVPE KVDGTAPSAG SKRSPDHTNG TSGDDGGPTE RKLARRLDDS
     EMHQSQDVPE AGGRAFFMSK SLDTDDGIRL KAREMIQSAL ESSPIPSGAF EAEYLAIRIE
     TEIFNLFKST DPKYKQRVRT RVMNLRDSNN PSLRINVLMG HVKPERLASM TSEEMASKDM
     KDLREKYTKE TIDDHQMAVT GGTESDILKC GKCKQNKCTY NQVQTRSADE PMTTFVYCNS
     CGHRWKVRIR DLRD
//
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