ID H2C9Q7_9CREN Unreviewed; 100 AA.
AC H2C9Q7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Transcription factor S, archaeal {ECO:0000313|EMBL:EHP68883.1};
GN ORFNames=MetMK1DRAFT_00033310 {ECO:0000313|EMBL:EHP68883.1};
OS Metallosphaera yellowstonensis MK1.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=671065 {ECO:0000313|EMBL:EHP68883.1, ECO:0000313|Proteomes:UP000003980};
RN [1] {ECO:0000313|EMBL:EHP68883.1, ECO:0000313|Proteomes:UP000003980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MK1 {ECO:0000313|EMBL:EHP68883.1,
RC ECO:0000313|Proteomes:UP000003980};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Kozubal M., Macur R.E., Jay Z., Inskeep W., Woyke T.;
RT "Improved High-Quality Draft sequence of Metallosphaera yellowstonensis
RT MK1.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the archaeal rpoM/eukaryotic RPA12/RPB9/RPC11
CC RNA polymerase family. {ECO:0000256|PIRNR:PIRNR005586,
CC ECO:0000256|RuleBase:RU003474}.
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DR EMBL; JH597770; EHP68883.1; -; Genomic_DNA.
DR AlphaFoldDB; H2C9Q7; -.
DR STRING; 671065.MetMK1DRAFT_00033310; -.
DR eggNOG; arCOG00579; Archaea.
DR HOGENOM; CLU_093932_3_2_2; -.
DR Proteomes; UP000003980; Unassembled WGS sequence.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd10511; Zn-ribbon_TFS; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR InterPro; IPR012164; Rpa12/Rpb9/Rpc10/TFS.
DR InterPro; IPR006288; TFS.
DR InterPro; IPR001222; Znf_TFIIS.
DR NCBIfam; TIGR01384; TFS_arch; 1.
DR PANTHER; PTHR11239; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR11239:SF14; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA12; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR PIRSF; PIRSF005586; RNApol_RpoM; 1.
DR SMART; SM00661; RPOL9; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR005586-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003980};
KW Transcription {ECO:0000256|PIRNR:PIRNR005586,
KW ECO:0000256|RuleBase:RU003474};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR005586-1};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00472}.
FT DOMAIN 57..97
FT /note="TFIIS-type"
FT /evidence="ECO:0000259|PROSITE:PS51133"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
SQ SEQUENCE 100 AA; 11704 MW; A738C3DF69992FA9 CRC64;
MMTPRKVNGT SVYRCPKCGY EEEAVKPTVI KSKVKHTERE KTIVLEEEMP VGSQTMRGVV
CPSCKNDEVY FWMVQTRAAD EPPTRFYRCT RCGKTWREYE
//
