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Database: UniProt
Entry: Q5YF58_ISKNV
LinkDB: Q5YF58_ISKNV
Original site: Q5YF58_ISKNV 
ID   Q5YF58_ISKNV            Unreviewed;      1168 AA.
AC   Q5YF58;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
OS   Rock bream iridovirus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Alphairidovirinae; Megalocytivirus;
OC   Infectious spleen and kidney necrosis virus.
OX   NCBI_TaxID=263891 {ECO:0000313|EMBL:AAT71844.1, ECO:0000313|Proteomes:UP000125745};
RN   [1] {ECO:0000313|EMBL:AAT71844.1, ECO:0000313|Proteomes:UP000125745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RBIV-KOR-TY1 {ECO:0000313|EMBL:AAT71844.1};
RX   PubMed=15246274; DOI=10.1016/j.virol.2004.05.008;
RA   Do J.W., Moon C.H., Kim H.J., Ko M.S., Kim S.B., Son J.H., Kim J.S.,
RA   An E.J., Kim M.K., Lee S.K., Han M.S., Cha S.J., Park M.S., Park M.A.,
RA   Lee J.S., Kim Y.C., Choi D.L., Kim J.W., Park J.W.;
RT   "Complete genomic DNA sequence of rock bream iridovirus.";
RL   Virology 325:351-363(2004).
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|RuleBase:RU004279}.
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DR   EMBL; AY532606; AAT71844.1; -; Genomic_DNA.
DR   Proteomes; UP000125745; 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   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   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; 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; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000125745};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          183..464
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
SQ   SEQUENCE   1168 AA;  129346 MW;  405EF2A39618EB73 CRC64;
     MDIGRFVFGM YTADDVLNTS VVEITKAALK QEPGALYDPK LGPFMLPSDD EPVYDQRCVT
     CDSVTCPGHF GHIELAQDVI LHYKECVAFL RVICHSCGAH VPGTRFESAL RRLPPQHIQC
     QVCGLYQPVV RCGSSVTDPA YIVTEDYCGA SHVHSDVEYA RSVFQRVTPQ TLAIVGPKLT
     HPLNLIMKRF MVLPSCCRPP NKVGGSMVHD DLTLLISYIV KRNLKLAAAT SPEQRILYYQ
     ALKGDILCYM DNSKGRAVHV TSNKSLMGIK ECITKKGGLL RHNLMGKRRN YTARSVVGPE
     STLALDQVGV PPQVADTLTI EEPVTKYNIE HVRQMRATGH LKALYDVDGQ VRHVVRCGLT
     LHRSLRDGDV VVLNRQPTLH RNSMLGMRVK VLPGNTIRVN LAVTHGFNMD FDGDEGNLYL
     PRSLSARAEV ATLMSPYTNI LSDCSKGVEV LLVQDTVLAL YMMSMWPHTR LEQQFVSMCC
     MAVGVYHHRI CTAGDLFRLM VPEGFTWRRY GIVFVNGHLA DNSGPVTKRA LSGGYNSIIR
     TMALHRGQKA AGRFIDCAQF VAREWLSWFP FSMGLDDMVV PGARNTAEAX YRHHMMLMES
     ARDEIEVVSI LESIKNTLMA IPLAPTCMSV MTSAGSKGDA FNIMQISMLL GQQYVDGMRV
     QREIDYGYRS LPHYKPVEVH SVEAKYESRG FVRSSFMDGL NPREAFFHAK CGREGMISTS
     QMTGVTGYAE RRMVKFSEDL RIANDLSVRD ANGNIVQLLY GGHGMDPMMC WQDGCPVNFE
     RMAMQIDQSL DICMMIPMDM AQAAQSVCER LAPIFPPLVR DSVMERHARI IKQGAAQFPC
     SDADRWAQEV YDAYVRALCV PGSPVGIVCA QAFGARQTQS TLNIFHKAGG LHDTGSIRFG
     ELLNLSKKSS RRLLYVHALG EQTLSSVKDV LGNAFFKGPL QDFVVDSTDD GVYTFNRAAL
     FDRRIDMCHV LNEISSKHGS CCTIEQLSQY VIKIQRCSDA DGYLAGVFVG GAPTICNVHF
     VFNNNKWVAV VSGSTLLYAL GVQGVDVDNT ACNNVWDVYE AKGLIAAKRF LTHSMVECLG
     DDVHMAHIRV LVDRMTFSGL PTAVDRYTMR SCETGPISKA TFEESLDILV SSAVRGERDN
     NTGVGACLVA GKMLPLGTGS CRVATDYL
//
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