ID A0A0G2SSG2_9CAUD Unreviewed; 875 AA. AC A0A0G2SSG2; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 02-OCT-2024, entry version 37. DE RecName: Full=DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00012418, ECO:0000256|RuleBase:RU003805}; DE EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418, ECO:0000256|RuleBase:RU003805}; GN ORFNames=Pm5460_08 {ECO:0000313|EMBL:AKA61817.1}; OS Proteus phage vB_PmiP_Pm5460. OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Autographiviridae; Molineuxvirinae; Acadevirus; Acadevirus Pm5460. OX NCBI_TaxID=1636249 {ECO:0000313|EMBL:AKA61817.1, ECO:0000313|Proteomes:UP000201288}; RN [1] {ECO:0000313|EMBL:AKA61817.1, ECO:0000313|Proteomes:UP000201288} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Melo L.D.R., Veiga P., Cerca N., Kropinski A.M., Azeredo J., Almeida C., RA Sillankorva S.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC {ECO:0000256|RuleBase:RU003805}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.6; Evidence={ECO:0000256|ARBA:ARBA00024550, CC ECO:0000256|RuleBase:RU003805}; CC -!- SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase CC family. {ECO:0000256|ARBA:ARBA00009493, ECO:0000256|RuleBase:RU003805}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KP890822; AKA61817.1; -; Genomic_DNA. DR RefSeq; YP_009209198.1; NC_028916.1. DR SMR; A0A0G2SSG2; -. DR GeneID; 26635541; -. DR KEGG; vg:26635541; -. DR OrthoDB; 309at10239; -. DR Proteomes; UP000201288; Genome. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.260; -; 1. DR Gene3D; 1.10.287.280; -; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR Gene3D; 1.10.1320.10; DNA-directed RNA polymerase, N-terminal domain; 1. DR InterPro; IPR024075; DNA-dir_RNA_pol_helix_hairp_sf. DR InterPro; IPR046950; DNA-dir_Rpol_C_phage-type. DR InterPro; IPR002092; DNA-dir_Rpol_phage-type. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR037159; RNA_POL_N_sf. DR InterPro; IPR029262; RPOL_N. DR PANTHER; PTHR10102; DNA-DIRECTED RNA POLYMERASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR10102:SF0; DNA-DIRECTED RNA POLYMERASE, MITOCHONDRIAL; 1. DR Pfam; PF00940; RNA_pol; 1. DR Pfam; PF14700; RPOL_N; 1. DR SMART; SM01311; RPOL_N; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR PROSITE; PS00900; RNA_POL_PHAGE_1; 1. DR PROSITE; PS00489; RNA_POL_PHAGE_2; 1. PE 3: Inferred from homology; KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478, KW ECO:0000256|RuleBase:RU003805}; KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU003805}; KW Reference proteome {ECO:0000313|Proteomes:UP000201288}; KW Transcription {ECO:0000256|RuleBase:RU003805}; KW Transferase {ECO:0000256|RuleBase:RU003805}; KW Viral transcription {ECO:0000256|ARBA:ARBA00023314}. FT DOMAIN 5..298 FT /note="DNA-directed RNA polymerase N-terminal" FT /evidence="ECO:0000259|SMART:SM01311" SQ SEQUENCE 875 AA; 99635 MW; 39193A7B3AB95531 CRC64; MDLQEIQLQL ENEMFNGGIR RFEADQQRHL QAGNASDTAW NRKLISEFIA PMAQGIQAYK EEYKGKIGRA PRALAFLNCV ENEVSAYITM KVVMDMIQTD VTLQSIAMSI ADRIEDQVRF SNLEGKAKKY FEKVKASLKA SRSKQYAHGH KVMVVAEKNL AEKSEDIDRW IPWGKEELLN IGLTLLEILE NSVFFNGEPV FFRTIRTMGY KKTLYFLQTS ENIGEWVRAF KDHVAQLSPA YAPCVVPPRP WKSPFNGGFH TEKVASRIRL VKGDREHVRK LTQKQMPKVY KAINALQNTQ WQVNKDILNV ADEVVRLDLG YGVPHFKPLI DKDNKPANPV PVEFQHLRGR ELKEVLSDEQ WQAFIHWKGE CAKLYTAETK RGSKSASVVR MLGQARKYSM FDAIYFVYAM DSRSRVYAQS STLSPQSDDL GKSLLRFTEG RSINSVEDLK WFCINGANLW GWDKKTFDVR LNNVLQEDFQ EMCRDIASDP LTFTQWVGAD APYQFLAWAF EYANYLDLVD EGRAHEFKTH LPVHQDGSCS GIQHYSAMLK DEVGARAVNL KPSDAPQDIY GEVAKVVIRK NNENMEASEE DFMTSGSMHL QGAVLRAMAS SWDSVGITRG LTKKPVMTLP YGSTRITCRE SVEDYLITLE EEEVKRAIAE NRKANKVHPF VSDKEEGQIL ERDALNYMTA LIWPSISEVV KAPIVAMRMI KQLARYASKR NEGLEYTLPT GFILKQKIMA TEMLRVRTML MGDIRMSLQV DTDVVDETAM SGASAPNFVH GHDASHLILT VCDLVDKGIK SIAVIHDSFG THADNTVALR DSLRHKMVEM YENTNVLQKL LEEHEERWLV DTGIKVPEQG TFDIREILNS DYVFA //