ID L5KHJ6_PTEAL Unreviewed; 204 AA.
AC L5KHJ6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA12 {ECO:0000256|ARBA:ARBA00018784};
DE AltName: Full=DNA-directed RNA polymerase I subunit H {ECO:0000256|ARBA:ARBA00031781};
GN ORFNames=PAL_GLEAN10001320 {ECO:0000313|EMBL:ELK11159.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK11159.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase I which synthesizes ribosomal RNA
CC precursors. {ECO:0000256|ARBA:ARBA00002472}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits. {ECO:0000256|ARBA:ARBA00011251}.
CC -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC RNA polymerase family. {ECO:0000256|ARBA:ARBA00008925}.
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DR EMBL; KB030712; ELK11159.1; -; Genomic_DNA.
DR AlphaFoldDB; L5KHJ6; -.
DR STRING; 9402.L5KHJ6; -.
DR eggNOG; KOG2907; Eukaryota.
DR InParanoid; L5KHJ6; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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 CDD; cd10507; Zn-ribbon_RPA12; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
DR InterPro; IPR012164; Rpa12/Rpb9/Rpc10/TFS.
DR InterPro; IPR034004; Zn_ribbon_RPA12_C.
DR InterPro; IPR001222; Znf_TFIIS.
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 SMART; SM00440; ZnF_C2C2; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000313|EMBL:ELK11159.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00472}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..204
FT /note="DNA-directed RNA polymerase I subunit RPA12"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003969229"
FT DOMAIN 108..173
FT /note="TFIIS-type"
FT /evidence="ECO:0000259|PROSITE:PS51133"
SQ SEQUENCE 204 AA; 22080 MW; 198099E87EC51FA2 CRC64;
MTPEWGGGYP LLLINFSFSF SALDHLSVMD LASTGSSFQS DLDFCPDCGS VLPLPGTQDT
VTCTRCGFSI NVRDFEGKVV KTSFVFHKLG TAMPMSMEGG PEFQGPVVDR RCSRCGHEGM
AYHTRQMRSA DEGQTVFYTC TNCNSLVLPP IQGMGGNGLS NKMYEPKCGT QSTTPNPPLL
FGTAPSCLKC LCLRLLTSLR PPPQ
//