ID A0A091DSV2_FUKDA Unreviewed; 345 AA.
AC A0A091DSV2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Transcription elongation factor {ECO:0000256|RuleBase:RU368078};
GN ORFNames=H920_05253 {ECO:0000313|EMBL:KFO33355.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO33355.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO33355.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO33355.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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; KN122100; KFO33355.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DSV2; -.
DR STRING; 885580.ENSFDAP00000014506; -.
DR Ensembl; ENSFDAT00000003490; ENSFDAP00000014506; ENSFDAG00000001774.
DR OMA; ERKEPDT; -.
DR OrthoDB; 1383197at2759; -.
DR Proteomes; UP000028990; 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:SF4; TRANSCRIPTION ELONGATION FACTOR A PROTEIN 3; 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; PS51133; ZF_TFIIS_2; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|RuleBase:RU368078};
KW Elongation factor {ECO:0000313|EMBL:KFO33355.1};
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:KFO33355.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
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 5..82
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51319"
FT DOMAIN 184..300
FT /note="TFIIS central"
FT /evidence="ECO:0000259|PROSITE:PS51321"
FT DOMAIN 303..343
FT /note="TFIIS-type"
FT /evidence="ECO:0000259|PROSITE:PS51133"
FT REGION 112..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 38951 MW; C6DAD6C1B884C4FA CRC64;
MDQEKELLKI TKKLEKMVAR RSMEGALDLL KKLDSYQLSI RLLQTTRIGI AVNGVRKHCL
DKEVVALAKV LIKNWKQLLG SPGSPEGKKG KKREKAKKEK VLACSYWKPE AALSSPRGKG
REEPKSRRDS VHSKASGSSL KRPSMKRSNS SKSKVKTPKT PSDSSTFAPS LCLLSPCYLT
GDSIRDKCVE MLSVALKAED DYKNYGINCD KMASEIEYHI YQELKSTDMK YRNRVRSRIS
NLKDPKNPDL RRNVLSGAIS TGLIAKMMAE EMASDELREL RNAMTQEAIR EHQMAKTSGT
NTDLLQCGKC KKKNCTYNQV QTLSADEPMT TFVLCNECGH RWKFY
//
