ID E4UWC0_ARTGP Unreviewed; 1455 AA.
AC E4UWC0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=RNA-dependent RNA polymerase {ECO:0000256|RuleBase:RU363098};
DE EC=2.7.7.48 {ECO:0000256|RuleBase:RU363098};
GN ORFNames=MGYG_05510 {ECO:0000313|EMBL:EFR02515.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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=2.7.7.48; Evidence={ECO:0000256|ARBA:ARBA00024517,
CC ECO:0000256|RuleBase:RU363098};
CC -!- SIMILARITY: Belongs to the RdRP family. {ECO:0000256|ARBA:ARBA00005762,
CC ECO:0000256|RuleBase:RU363098}.
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DR EMBL; DS989825; EFR02515.1; -; Genomic_DNA.
DR RefSeq; XP_003172926.1; XM_003172878.1.
DR STRING; 535722.E4UWC0; -.
DR GeneID; 10028202; -.
DR VEuPathDB; FungiDB:MGYG_05510; -.
DR eggNOG; KOG0988; Eukaryota.
DR HOGENOM; CLU_001366_0_0_1; -.
DR InParanoid; E4UWC0; -.
DR OMA; DDYLVIW; -.
DR OrthoDB; 5477883at2759; -.
DR Proteomes; UP000002669; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProt.
DR CDD; cd00590; RRM_SF; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR007855; RNA-dep_RNA_pol_euk-typ.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23079; RNA-DEPENDENT RNA POLYMERASE; 1.
DR PANTHER; PTHR23079:SF55; RNA-DIRECTED RNA POLYMERASE; 1.
DR Pfam; PF05183; RdRP; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU363098};
KW Reference proteome {ECO:0000313|Proteomes:UP000002669};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484,
KW ECO:0000256|RuleBase:RU363098};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363098}.
FT DOMAIN 61..139
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1376..1444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 734..761
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1393..1407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1440
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1455 AA; 165128 MW; 19DA7CC39BBD7D37 CRC64;
MSCYSNRAKY SLAGRGGPNG RVHGAFPPGI YTQSSHKSNQ TMLERVKPSH LAPRWISWDF
LAVTVSNLPP NVNTYTLWKS FSACGTVDYI ELSEDVRGKS EGRARIRFRP PPKESFWLDG
QHLLELEDGQ RIVISARVDT FKRRKEIPSP VDPKIMYPLS LEAVGRSLDI GCLSGEQSMI
IMRTITASFQ DYIRFVADLQ RREINIFFQM VKTEARPPTS LPHTVHSYRI RVPFVHLSSI
KRISEGEELS FIFSLDSPPS YHRKLQDLST TFSDSDNTWR SDDTWYRQTD IVHNPLDLVH
SKTSLKKAHP VINIGRWTTF RITFHLPDAD NVQNLETLSK ILKDFNVDIQ DIDSFELKKQ
PPTADLAWRW IDPPSTHASK HTSSLEDLAE NEYTHISYVV RYQLEVCISH GLLSEYAIDK
EFAKKLESLG ERDAKDLLEY VAHEKVVYHD PMKIFDIQFF SGVTNRRIPK YCCYMRSATV
TPSTIYFHTP TVDTSNRVIR HYIEYADRFL RVRFTDEKYE GRINSTYNNC MDEVFTRVKR
TMTNGVIVGD RHYEFLAFGN SQFREHGAYF FASLPNLTAS NIRAWMGHFS DIKIVAKHAA
RLGQCFSSTK AVTGCPVTIR EIDEIERNGY TFSDGVGRIS KFLAQMIMTE FKLKTPSEEP
PSVFQFRLGG CKGILTVSPE AQRREVHIKK SQYKFAAVHN GLEIIRWSQF AAAYLNRQLI
VVLSALGVTD EIFIKKLRLM LEDMEQAMTS ETKAMSLLQK QVDPNQMTLL LAQMVHDGFQ
GTSDPFVTSL LELWRAWQIK YLKEKAKICI DGGACLFGCL DETATLKGYH EKTRPSIDAT
YEERLGYLPE IFVQVFDAEA ERNYKIIEGP CILARNPSLH PGDIRVVRAV NVPALHHLKD
VIVFSQTGDR DVPSTCSGGD LDGDDYIVIW DQDLVPLPKD WFRQPMDYTA SNAQSLTRDV
TVNDITSFFV TYMKNDRLPQ IAHAHLAFAD FLEDGVNDKR CVQLAQLHSA AVDYNKSGIP
ANMTRDLVPR KWPHFMEKKY KPKEAQYHSK KILGQIYDIV ERVEFRPKLE APFDERILNC
DISVSEEMVL AAKKLKALYD ADMRRIMAQH EIKTEFEVWS TFVLGHANMS KDYKFHEELG
QISSALRERF LLMCHDEAGG KDFQHLAPLA VAMYRVTAQE VAEALGKEES SPGHDVGDAI
KKAYKHLSND QLPLISFPWV LQPVLGKIAN RHFDDAGIVE GGGKLITWSS AAYEQSRVRR
INGIKGANNT PRDVETAGGI QHAGEVLELF QEDLGFDPFD GLGDAFDQMV SVDGDTRSKA
KGAIPLLDTE LQSDSLIEID DEIFTPFTPC TIDSSGHGSV PMEEQSSLLD ISNENIQIGT
PKTDNPQPKL SAAHPKLEED QENRPPPQKD DPTPSFLDGS PVPEEMIEDE EVEMMEEDGD
VDPSAVNQLE MLLNI
//
