ID Q6YHB9_9VIRU Unreviewed; 1294 AA.
AC Q6YHB9;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
OS Ambystoma tigrinum stebbensi virus.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Alphairidovirinae; Ranavirus;
OC Ambystoma tigrinum virus.
OX NCBI_TaxID=217733 {ECO:0000313|EMBL:AAP33183.1, ECO:0000313|Proteomes:UP000157741};
RN [1] {ECO:0000313|EMBL:AAP33183.1, ECO:0000313|Proteomes:UP000157741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14599794; DOI=10.1016/j.virol.2003.08.001;
RA Jancovich J.K., Mao J., Chinchar V.G., Wyatt C., Case S.T., Kumar S.,
RA Valente G., Subramanian S., Davidson E.W., Collins J.P., Jacobs B.L.;
RT "Genomic sequence of a ranavirus (family Iridoviridae) associated with
RT salamander mortalities in North America.";
RL Virology 316:90-103(2003).
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:RU004279}.
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:RU004279};
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR EMBL; AY150217; AAP33183.1; -; Genomic_DNA.
DR RefSeq; YP_003777.1; NC_005832.1.
DR GeneID; 3678174; -.
DR KEGG; vg:3678174; -.
DR Proteomes; UP000157741; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 6.10.250.2940; -; 1.
DR Gene3D; 6.20.50.80; -; 1.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 2.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 189..528
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 352..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1294 AA; 141058 MW; A9B399BC3318C9C2 CRC64;
MEMFASKSLQ VEGLLFGVCS PEEILATSVV EVTKSCLKAE TGSVYDPRMG SAGADDENAL
CPTCENTGRE CPGHFGHIEL AKPVVLFYKE TVAWLKRCCH VCGAVGNEPM PFFFAPYSAC
DACGAQRPLV RLVDAHDPCA IRVTVRRKDG EPETMPPELI LATLDRVRDS DVDRVLGRGK
GSHVRFHPRR LVMTRMPVLP PCCRPNARQW PDGAMQDDNL SVFVSQIVKV NQRIKALEHD
DPAVEGLVAQ LRLKTLCFVD NTKGKVMHAT NRKPMVGIKE RIGKKGGLLR QNIMGKRRNQ
TGRSVVGPDG TLEVDEVGVP EAIADNLTVP VMVTPFNVSY LEAMMREGRV SSVETRDGTV
HRPSEWRPSH GDHMETADGS PLGRVTRPSY DARDPSVVLR SWKTGETVTR PPPFSWPKLE
PGMTVTRCLV DGDPVALNRQ PTLHRNSMLG MRVKRLPGKT IRLNLSVTSG FNMDFDGDEG
NLYLPQGPQA RSETMLLMNP KSVIMSARGP HAEVSLVQDG VLGCHLMSLN SAIPCPPEEL
AACLMEVRGC EGWDVRDVEK GATPRDILSS VLPSTLTVDC GGGCRIESGK IVSGHLTKSA
VKKIVRVVCL ENGGDAAGKL VDKLQFLTNA WLSHRPFSVG YSDCLTERPE ETVRMVADAV
CSKILEAEAA DDEDGVSVAL CGARDRGQAV TCAALTPDNR MAVMSRAQSK GDMFNLTQIA
GLLGQQYVGG SRPGKEIDGG RRSLPHYPRV WDSEHTTLKY ESRGFVRSSF LKGLNPREVF
FHAKSGREGM ISTSQMTGVT GYAERKMVKL NEDLVSAYDG TVRDAMGNVV QFVYGGHGMD
PQRCWSDGCP VNFKTLAEEY SSQECFSQIS GLRSPAVTSV EEASLLVPVG LCPGAPDPVR
ESLVLKHASV ILKGAEEHPC EDHFAWRERV ARSYAAAVLC PGEAVGVLCA QSIGAKQTQQ
TLDTFHKAGG WLDDAGSVPF GELLGLSQKP MRRQCVVPLK VDPSTPGDEV RDLVGCSFVR
RDLLDLLAVR PSTATVGKTA SLELDPVKCF KLRISPADVA YAVAEKFPHP HFDVSVSSFG
VTLSWSANYP VNNLFTGLFS VQVGGTPGVE SYRLLRGRDG GWVAVTKGTN LGAFLCHPLA
DWERVRTDDV WDVYETLGLA AAKKRLYELM FSCVGDNLYP AHIKLLTDRM MRRGRPTPID
RYTMRTCEVG PLSRAAFEES LDILTGAGCT AETEHCAGAG ARVAAGLPVR AGTGYMGLLC
GKGFFDEPMV KVPEADGREY VDYSYSDDES FEWC
//
