ID F0ULI4_AJEC8 Unreviewed; 1387 AA.
AC F0ULI4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=RNA-dependent RNA polymerase {ECO:0000256|RuleBase:RU363098};
DE EC=2.7.7.48 {ECO:0000256|RuleBase:RU363098};
GN ORFNames=HCEG_06353 {ECO:0000313|EMBL:EGC47138.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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; DS990640; EGC47138.1; -; Genomic_DNA.
DR STRING; 544711.F0ULI4; -.
DR VEuPathDB; FungiDB:I7I53_00529; -.
DR HOGENOM; CLU_002322_0_0_1; -.
DR OMA; VHFGFSN; -.
DR Proteomes; UP000008142; 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; 1.
PE 3: Inferred from homology;
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU363098};
KW Reference proteome {ECO:0000313|Proteomes:UP000008142};
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 143..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1367
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1387 AA; 157026 MW; 2C719051073EACA9 CRC64;
MATPRTPRSG VDFNLLIFNL NATYNLDLPN PPVSTPRQRP IEGRTLPERC VGLAKFLYYD
DPVNFQRVID SFSEWAMAFF SGWVQKPKQE PEVLPSSRSF IRSNTISMAR NITPEQRARV
LDELWKVLSD EEYIVTRGAS RIPRGASVSS PAGARSGPGC DSGAAATTTG DPMAGSGTKS
NGAPKVPPTT PAKMPPSPTK RKEVVDHSEV FSTAPSTPSN PLHMMSSSSS DDEFENSDLD
DLDINLDIPS LGLADSSDNN QGPKAPKQRR IDEYMTTSKN VRKSVSSPSG KPLSNENTSF
QTVTTEQSNS FGASFGASTP ATSFSRSFET GQFDLNEAST CSSTARPPPD AKFSGLWGNA
NTTSPSKNTK MQPEADLDWR EQNIRNIIQD LEENGPFSNK NVVETTVPLR YRYEAQRAAN
FFKVPAENIL QKLDRRKLPE YEDFWKSLHN GKQERLEKTA PEPWDMAVDQ YKDRKLTGDV
VTLSCELTWC SQKEPGYFKL TLKPLKLMRG YRFCRRFGSD RFLELTYPIL TEPPAHLVRK
GNAVEKEILI DAISRWMATS EHHLVGRVWK VLYLEDIQNK QKKAKKYDSG EIRAGGSAIE
TPHKQKAYFF ATDGIDFRKA RDPLEIPPQG ETSGQRTSMS IDALIDWHMP RAKNSHQSDM
KLFQRLHLGL SRTLATVILR REEIIYVKDP PGTVMNDGCA LMSKSLGMAV ASALGLDGHP
AIFQARISGA KGVWMVDLDD SRFKTGDRGF WLQITQSQLK IYPAPPHDTK PMDDTQLTFE
VVQWSRPLSP ASLNMQLLNI LQHGGIRNDH IRNLIRQEMS SFYDEFLRTL LCSSGVECRS
WLQKMKWITN ESSKRQSKRT DNFFPPQYAE QAIMLLDAGF LPLKLPYLTK IFRRLLQDYL
DNLKKLKITV SQSTFAYCVA DPFGVLRPDE VHLGFSREWE HGSASTELHD IDVLLARLPA
HLATDIQKRR SVYKNELRHM KDVIVFPTTG DTPLASLLSG GDYDGDQCWV CWDPIIVREF
KSTEFDPGTV PSAESLGLRS CSTLMSKIGS TEEFLTNAFR FNVKPSKLGQ CTIERETYCY
HENNITSPMA VKLAWLLSYL VDSKKAGLEL TDDAWEYLKP KYSKVITEKQ PLVPAYKSLS
RGFKPLVWNS CNIIDYLLFD VIVAESDQML VRFDKFCSEH CELPLDHDLL SEWGKVEKRG
IKEKDEMNPV LYNALNDIKK RFRDKKINWE RQHGLNSETP YSRKILEAAQ SLQELTPPNF
DHPLSHTWAN STYEWKRLRA LCAYKDCRSD FVWYAVGPVL CEIKAKAMGQ CRIVLPNIHK
VLHVNRNVAK RVAEDVMRRN AGELSGDEGG GEDDYDDDDE FFDIDPFSFP EDLERDIDDT
ESHNSFP
//