ID A0A177D4E3_ALTAL Unreviewed; 1311 AA.
AC A0A177D4E3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=DsRNA-specific nuclease dicer {ECO:0000313|EMBL:OAG14368.1};
GN ORFNames=CC77DRAFT_1025767 {ECO:0000313|EMBL:OAG14368.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG14368.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG14368.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG14368.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC {ECO:0000256|PROSITE-ProRule:PRU00657}.
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DR EMBL; KV441500; OAG14368.1; -; Genomic_DNA.
DR RefSeq; XP_018379789.1; XM_018526136.1.
DR STRING; 5599.A0A177D4E3; -.
DR GeneID; 29111730; -.
DR KEGG; aalt:CC77DRAFT_1025767; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1025767; -.
DR OMA; ARECICT; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd00593; RIBOc; 2.
DR CDD; cd18802; SF2_C_dicer; 1.
DR Gene3D; 3.30.160.380; Dicer dimerisation domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.1520.10; Ribonuclease III domain; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR PANTHER; PTHR14950; DICER-RELATED; 1.
DR PANTHER; PTHR14950:SF37; ENDORIBONUCLEASE DICER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF03368; Dicer_dimer; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00636; Ribonuclease_3; 2.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00535; RIBOc; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF69065; RNase III domain-like; 2.
DR PROSITE; PS51327; DICER_DSRBF; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00517; RNASE_3_1; 1.
DR PROSITE; PS50142; RNASE_3_2; 2.
PE 3: Inferred from homology;
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW Antiviral protein {ECO:0000256|ARBA:ARBA00022721};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00657}.
FT DOMAIN 1..136
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 302..481
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 498..592
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000259|PROSITE:PS51327"
FT DOMAIN 850..988
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1030..1206
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT REGION 188..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1311 AA; 147112 MW; 5C73CF3330873CFD CRC64;
MAPTVALCTQ QHAYLRSYLP AVRTKLLTGA DNVDRWSEQS TWDSVLEGVR IVVSTHAVLE
DALSHGFIAM RRLALLVFDE AHSCVGGHAG NRIMRNLYYP TKARSGVVPH ILGLSASPIL
RSNLKGLSNI EANLDATCVT PRLHRQDLLK FVHHPKVQRL EFPPCKTSEE SITGHVFSKL
RRLSERLSLE QRTSSAPSVP HRSSTRAGRS TSQGSFTDFS DQIRKFYNKA THVYKELGPS
AAAYYILRTT ERIRNKAELL EASAFYIKEE DKMVYQLQHV FNREELTQAP DVLSLRSQLS
PKVERLIAFL ERQEPEQCSG LIFVQQRAIV GVLYTILANH PRTMTRFKCA TFVGLSNSSH
GKLALCELLD KEAQKDTMLE FRTGKKNIVI ATDALEEGID VAACNLVVCF DAPSNLKSYI
QRRGRARMYA SQYVIMVPTD SIQTKLDSWP ELENALAKMY QDDDRARTRI ALLENEQESV
DDSLCVGATG AYLTAEKAMS HLHHFCDVMP RQRYAETRPV FSFREKDSGL ITCTVTLPNC
VKSSLRSTRG RRGWRTERAA MRDAAFQCYV ALFEAGLLNG HLLPLTHEWK DHDANTEQLL
KKALRSKQIK PFTQMARAWA TPDLHQTTIT VSCNRTHEKL SMRLTTPTRL SYIPDVLLYW
DSETIFQASF GNQSRKSVAS IDMLEQLRAV TQLLDKSTRS DQSVSHKTDF VLLLGPDIEE
NQLMDWFKAY EGRVDMLDAL TSSSEDIQGL VRSTKLNGKP LVFFCMTSEP QQKLDLEVVC
VPLIKRRNFE APNALTNHFA AAPAVDLRRP SAAVQIRARE CTVDLLDHRF AIFNLFVPSL
WRHIEASTVA HQLQETILLN VSFCSLSHIV TAISAPSAGR ATNYQRFEFF GDALLKFQTS
VQLFTDHGNW PEGYLSQRKD SLVSNARLAR AAIAKGLGSF ILTDPLRRKW SVPRISDADQ
EAEERTLGIK ALADVVEALI GAAYIDSGFK AARACTNVFL PEISAVVPQF PERISVKSNS
PRDPEAETLI GYRFQDELLL LEALTHPSCG IDAKTESYQR LEFLGDAVLD VLISTFLSRC
LPELSQGQMT RIKAALGNKN ILGYLCLHFS MDRDLVRIET GPDHRPHEVR YCEKVPLWQF
MRHHSPEVVQ AHKNAGHTFE QCGAEIQKIL SEGATYPWKL LARLGLDKFY SDLVESVFGA
VFNDSQGDLS ECEKLFERIG LKYYAARMAE GSLDVVHPRD ELQGLIGSSK LEIDVQPVFS
GEDRAIFVCS VRVEGTVIAE AQGCITEDEA CVGGIQAAVA FLRSQQEGRG R
//
