ID K9G6M7_PEND2 Unreviewed; 912 AA.
AC K9G6M7;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=PDIG_13840 {ECO:0000313|EMBL:EKV17605.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV17605.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
CC -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits and is required for the normal formation of 25S and
CC 5.8S rRNAs. {ECO:0000256|ARBA:ARBA00003706}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC subfamily. {ECO:0000256|ARBA:ARBA00010379}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKV17605.1}.
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DR EMBL; AKCT01000056; EKV17605.1; -; Genomic_DNA.
DR AlphaFoldDB; K9G6M7; -.
DR STRING; 1170229.K9G6M7; -.
DR eggNOG; KOG0337; Eukaryota.
DR HOGENOM; CLU_003041_5_0_1; -.
DR InParanoid; K9G6M7; -.
DR OMA; EDQFGMM; -.
DR OrthoDB; 5475716at2759; -.
DR Proteomes; UP000009882; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17959; DEADc_DDX54; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR012541; DBP10_C.
DR InterPro; IPR033517; DDX54/DBP10_DEAD-box_helicase.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF8; RNA HELICASE; 1.
DR Pfam; PF08147; DBP10CT; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01123; DBP10CT; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EKV17605.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000009882};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 84..112
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 115..287
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 353..503
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 22..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 84..112
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 29..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..676
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 101454 MW; 39D4FB445076C9E7 CRC64;
MPRRAASPAE SEVEFDITKS LFENDSDSDG GIKPPKKKFQ KPDTNQDLDF LNEDDGDAAF
IANSQASANR KGANLKGRTV KKGGGFQAMG LSMTLLKAIT RKGFSVPTPI QRKTIPVIMD
DKDVVGMART GSGKTASFVI PMIEKLKSHS TSFGARALIM SPSRELALQT LKVVKEMGKG
TNLTSVLLIG GDSLEDQFGM MANNPDIIIA TPGRFLHLKV EMDMDLSSIK YVVFDEADRL
FEMGFAAQLT EILHGLPTNR QTLLFSATLP KSLVEFARAG LQEPSLIRLD TENKVSPDLQ
NAFFAVKSSD KEGALLHILH NIIKMPTGET QIGGKLRQEA ENPTRKRKRS DVRLPSGFKE
SPTEHSTIVF AATKHHVDYL YSLLVEAGFA TSYAYGSLDQ TARNHHVQNF RSGISNILVV
TDVAARGIDI PVLANVINYD FPSQPKIFIH RVGRTARAGQ KGWSYSLVRD KDAPYLLDLQ
LFLGRRLVLG RQYGTELNFA EDVVVGTLPR EPVSRSCEWV QKVLDDDVDI YGQKQVSQKG
EKLYLRTRNS ASAESAKRSK EVVSSDHWAE IHPLFNDATS EREVERESML ARIGGYRPHE
TIFEANNRRG GKVADNEAVD TIRRLRTSVE NKRKRADAKA EAELAALGMS APGEDGQVED
EDVPEQAGEN MSEASDDELE VTFSAYSSKS KQGEKKDAAA AFQNPDYFMG YTPQHNDMAE
DKAYGVHSGT NSNFASDSRN ATMDLNGDEG KRGFGEARSI MRWDKRHKKY VARQNDEDGS
KGSRLVRGES GAKIAASFRS GRFQAWKKGK RVERMPRVGE AETPAMNNIN SRMSSGRFRH
NQDRAPKRAD PLRGDYDKMK KKNDAARERQ HEKLGGAAYR GKSELRSTED IRKARKLVQQ
RRDKNARPSK RR
//