ID   A6QTB6_AJECN            Unreviewed;      1055 AA.
AC   A6QTB6;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=RNA-dependent RNA polymerase {ECO:0000256|RuleBase:RU363098};
DE            EC=2.7.7.48 {ECO:0000256|RuleBase:RU363098};
GN   ORFNames=HCAG_00622 {ECO:0000313|EMBL:EDN02758.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN02758.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476655; EDN02758.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6QTB6; -.
DR   STRING; 339724.A6QTB6; -.
DR   VEuPathDB; FungiDB:HCAG_00622; -.
DR   HOGENOM; CLU_002322_0_0_1; -.
DR   OMA; DRNTHQE; -.
DR   OrthoDB; 2735303at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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   InterPro; IPR007855; RNA-dep_RNA_pol_euk-typ.
DR   PANTHER; PTHR23079; RNA-DEPENDENT RNA POLYMERASE; 1.
DR   PANTHER; PTHR23079:SF14; RNA-DEPENDENT RNA POLYMERASE; 1.
DR   Pfam; PF05183; RdRP; 2.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU363098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009297};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU363098};
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   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1005..1055
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1013..1035
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1055 AA;  119952 MW;  621A54E7D68C9ADD CRC64;
     MSSSSDDEFE NSDLDDLDIN LDIPSLGLAD SSDNNQGPKA PKQRRIDEYM TTSKNVRKSV
     SSPSGKPLNN ENTSFQTVTT EQSNSFGASF GASTPATSFS RSFETGQFDL NEASTYSSTA
     RPPPDAKFSG LWGNANTTSP SKNTKMQPEA DLDWREQKIR NIIQDLEEKG PFSNKNVVKT
     TVPLRYRYEA QRAANFFKVP AENILQKLDR RKLPEYEDFW KSLHNGEQER LEKTAPEPWD
     MAVDQYKDRK LTGDVVTLSC ELTWCSQKEP GYFKLNLKPL KLMRGYRFCR RFGSDRFLEL
     TYPILTEPPA HLVRKGNAVE KDILIDAISR WMATSEHHLV GRVWKVLYLE DIQNKQKKAK
     KYDSGEIRAG VSAIEIPHKQ KAYFFATDGI DFRKAGDPLD IPPHVETSGQ RTSMSIDALI
     DWHMPRAKNS HQSDMKLFQR LHLGLSRTLA TVILRREEII YVKDPPGTVM NDGCALMSKS
     LGMAVASALG LDGHPAIFQA RISGAKGVWM VDLDDSRFKT GDRGFWLQIT ESQLKIHPAP
     PHDTKPMDEP QLTFEVVQWR LLQDYLDNLK KLKITVSQST FAYCVADPFG VLRPDEVHLG
     FSREWEHGSA GTELHDIDVL LARLPAHLAT DIQKRKSVYK NELRHMKDVI VFPTTGDTPL
     ASLLSGGDYD GDQCWVCWDP IIVREFKSTE FDPGTVPSAE SLGLRSCSTL MSKIGSTEEF
     LTNAFRFNIK PSKLGQCTIE RETYCYHENN ITSPMAVKLA WLLSYLVDSK KAGLELTDDT
     WECLRPKYSK VITEKQPLVP AYKSLSRGVK PLVWNSCNII DYLLFDVIVA ESDQMLVRFD
     KFCSEHCELP LDHDLLSEWG KVEKRGIQEK NEMNPVLYNA LNDIKKRFRD KKINWERQHG
     LNSEIPYARK ILEAAQSLQE LTPPTFDHPL SHTWANSTYE WERLRALCAY KDCRSDFVWY
     AVGPVLCEIK AKAMGQCRIV LPNIHKVLHV NRNVAKRVAE DVMRRNAGEL SGDEGGGEDD
     YDDDDDDEFF DIDPFSFPED LERDIDDTTS HNSSP
//