ID A0A218XQT9_PUNGR Unreviewed; 348 AA.
AC A0A218XQT9;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Transcription elongation factor {ECO:0000256|RuleBase:RU368078};
GN Name=LOC116187951 {ECO:0000313|RefSeq:XP_031372865.1};
GN ORFNames=CDL15_Pgr022444 {ECO:0000313|EMBL:OWM87333.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM87333.1, ECO:0000313|Proteomes:UP000197138};
RN [1] {ECO:0000313|Proteomes:UP000197138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX PubMed=28654223; DOI=10.1111/tpj.13625;
RA Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT "The pomegranate (Punica granatum L.) genome and the genomics of
RT punicalagin biosynthesis.";
RL Plant J. 91:1108-1128(2017).
RN [2] {ECO:0000313|EMBL:OWM87333.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Fresh leaf {ECO:0000313|EMBL:OWM87333.1};
RA Xu C.;
RT "The pomegranate genome and the genomics of punicalagin biosynthesis.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_031372865.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_031372865.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR EMBL; MTKT01000813; OWM87333.1; -; Genomic_DNA.
DR RefSeq; XP_031372865.1; XM_031517005.1.
DR OrthoDB; 1383197at2759; -.
DR Proteomes; UP000197138; Unassembled WGS sequence.
DR Proteomes; UP000515151; Chromosome 8.
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|RefSeq:XP_031372865.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU368078};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00649};
KW Protein biosynthesis {ECO:0000313|RefSeq:XP_031372865.1};
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 10..88
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51319"
FT DOMAIN 180..303
FT /note="TFIIS central"
FT /evidence="ECO:0000259|PROSITE:PS51321"
FT DOMAIN 306..346
FT /note="TFIIS-type"
FT /evidence="ECO:0000259|PROSITE:PS51133"
FT REGION 95..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 39402 MW; E1DEEB7E1E54D07A CRC64;
MAEELVQLFQ EASKAADAAA VRVTGGEADE SRCLDALKRL KTYPVTSQVL VSTQVGKGIR
RLTKHPRKKI QAFASEVIRI WKQIVTEESN GCKRKEAEHG RGTVNVGNDN EVEKDSPFRA
NEGSENGTVK ARKIERNGTP GSNKVEKANF EEKSDDALNR AIPNHSPQKS TPLVNCNDPM
RDKVREQLHE ALSKVSGEAE EDMIEEVNAC DPARVAVSVE SVMFAKWGKM NGVHKIKYRS
IMFNIKDQNN PDFRRKILLG QIKPERLLTM TTQEMASDHR QKENQQIKEK AMYECELGAA
PKATTDQFKC SRCRQRKCTY YQMQTRSADE PMTTYVTCVN CNNHWKFC
//
