ID K9FUM5_PEND2 Unreviewed; 1211 AA.
AC K9FUM5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=PDIG_45670 {ECO:0000313|EMBL:EKV12242.1};
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:EKV12242.1, 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 -!- 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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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:EKV12242.1}.
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DR EMBL; AKCT01000182; EKV12242.1; -; Genomic_DNA.
DR AlphaFoldDB; K9FUM5; -.
DR STRING; 1170229.K9FUM5; -.
DR eggNOG; KOG0926; Eukaryota.
DR HOGENOM; CLU_001832_0_4_1; -.
DR InParanoid; K9FUM5; -.
DR OMA; EAIHNNS; -.
DR OrthoDB; 5490433at2759; -.
DR Proteomes; UP000009882; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd17982; DEXHc_DHX37; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:EKV12242.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009882}.
FT DOMAIN 367..544
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 567..812
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..267
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1211 AA; 134543 MW; FAB9C02A4256091F CRC64;
MPPKFTPRLR KQRHRQNPDG ESTDTNVAQL QPVSKDEKEA RRQKLRGELQ EQHPQMSSKK
QKRLDKYIEN KLKKEENVEL LKKLAQSSVD TSSLKSSRDL SKRKRQGDDI SAPTISTPKH
NAPADISGYD TDDSDIHLKV SNPATDPDEQ KLREEAAAGS GLKRPLELGA DGFPVLKKRK
RAPKKKPAPA PVKAEVAWEG FDSDEEEGDV EEEEEEDDDD EDGMDEESES EIEEDSEEED
TSSSEDNSPD EDEEDSEESE DDDEMDEDKP TLKTRQSAFK SWAVQQINEA AGFKPTEGAV
TQEEQVFDPS KLPATHNTTQ EEPLPRELQV THGDPNRKAY SVAVDRTEEI QAARLGLPVV
GEEQKIMEAI HNNSVVVIWG ATGSGKTTQL PQFLFESGFG SPGSPNPGLI GVTQPRRVAA
VSMANRVSQE LGQHAEKVSY QIRFESTASK KTAIKFMTDG ILLREIADDF ALRKYSIILI
DEAHERSVNT DILIGMVSRI VGLRKSLSEE DPSVKPLKVV IMSATLRISD FTENPSLFRD
GAPPLVQAEG RQYPVAVHFS RRTQRDYVED AFRKVSRGHR KLPAGGMLVF LTGQNEIRQL
SKRLKQAFKP TQREDTTQAK VQLSATEAPL EAEDLELGGT EMDNPGHDDY DSDMEITGLD
DAEEDEGFEL AEGEEAMDSS TRVHVLPLYS QLPTKEQMKV FEPAPENSRL IILATNVAET
SLTIPGIKYV FDCGRAKEKQ FDLFTGVQSF QVGWISKASA NQRAGRAGRT GPGHCYRMYS
SAVYESEFAE YTDPEILRTP IEGVVLQMKS MGLHNVINFP FPTPPSRQGL AKAEKLLKNL
GALTADGQVT PIGRRLSTYP LSPRFSKMLH IGHQHGCMPY VIALVAALAV GDLFVPENQL
DPNQPLPTTA KKQVDDDSDS DSDRRKVYTN ADRLKDDERA QRNKAYARAQ RLFSKHDDTS
DALKSLSAIC AYGYASDGDS FSEKMFLRAK AFKEATQLRR QLTDIVRSNN PGLVPAYEAR
LPEPSSKQIK ALKQIVTAGF IDHVAIRADQ APVPPENPRT PRRAIDVPYL TLFRSRDGKG
EDLQERAVYV HPSSLLAKLS PKEMPKYITY SHLQQSSASL VSDQVPRIRM FPLVVPSGLQ
LSAIAHDTPL IEYGKPIGKA DAIEGVPPRR SCWVIPSLVG DEGGVGWPMP AKKVVQKKDA
KQGWVIEKFV A
//
