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Database: UniProt
Entry: K9H3H5_PEND2
LinkDB: K9H3H5_PEND2
Original site: K9H3H5_PEND2 
ID   K9H3H5_PEND2            Unreviewed;      1081 AA.
AC   K9H3H5;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=ATP dependent RNA helicase (Dob1), putative {ECO:0000313|EMBL:EKV19706.1};
GN   ORFNames=PDIG_01530 {ECO:0000313|EMBL:EKV19706.1};
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:EKV19706.1, 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   -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010140}.
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:EKV19706.1}.
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DR   EMBL; AKCT01000010; EKV19706.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9H3H5; -.
DR   STRING; 1170229.K9H3H5; -.
DR   eggNOG; KOG0948; Eukaryota.
DR   HOGENOM; CLU_002902_0_1_1; -.
DR   InParanoid; K9H3H5; -.
DR   OMA; IMLKNYN; -.
DR   OrthoDB; 1352at2759; -.
DR   Proteomes; UP000009882; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR   CDD; cd18024; DEXHc_Mtr4-like; 1.
DR   CDD; cd13154; KOW_Mtr4; 1.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.30; -; 1.
DR   Gene3D; 2.40.30.300; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR048392; MTR4-like_stalk.
DR   InterPro; IPR025696; MTR4_beta-barrel.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016438; SKI2-like.
DR   InterPro; IPR012961; Ski2/MTR4_C.
DR   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08148; DSHCT; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF21408; MTR4-like_stalk; 1.
DR   Pfam; PF13234; MTR4_beta-barrel; 1.
DR   PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01142; DSHCT; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EKV19706.1};
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}.
FT   DOMAIN          168..324
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          407..608
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1081 AA;  122031 MW;  05FA00C34AC7AEB7 CRC64;
     MDELFDVFED QPQAVKPSEV APKRLKKNKN KKRQMNGDVK KTADAQPEQK EDVAMTDASA
     GEVESADAEA PTTPSEPEQP ETKRPRLDQE PEPVVADSFE TEQEREIAAS GGLSGATDTS
     AVVVSHQVRH QVAIPPNYPY VPISQHKPPA NPAKTWPFTL DPFQQVAVSS IQREESVLVS
     AHTSAGKTVV AEYAIAQSLK QNQRVIYTSP IKALSNQKYR EFAAEFGDVG LMTGDVTINP
     TATCLVMTTE ILRSMLYRGS EIMREVQWVV FDEIHYMRDL NRGVVWEETI ILLPDKVRYV
     FLSATIPNAM QFAEWIVKMH NQPCHVVYTN YRPTPLQNYF FPAGGEGIHL VVDEKGVFRE
     ENFQKAMSAI ADKKGDDPAD ALAKRKGKGK DKQINKGGNK GPSDIFKIVR MIMLKNYNPV
     IVFSFSKREC EAGALQMSKL TFNDDSEKNM VSKVFESAIE MLSPEDRQLP QIQNILPLLQ
     QGIGVHHSGL LPILKETIEI LFQEGLIKVL FATETFSIGL NMPAKTVVFT SVRKFDGTSQ
     RWVTPSEFIQ MSGRAGRRGL DDRGIVIMMV GEEMDPAVAK EIVRGEQDRL NSAFHLGYNM
     ILNLMRVEGI SPEYMLERCF KQFQNTGSVS GLEKELESLE EKRTNMIISD EGTIREYYDL
     RKQLDAFADD VQHVITHPNY SLTFIHPGRL IHVKYKDADF GWGVVINQKK RKQASNDTEK
     LTPHQSYIVD VLMRTTEGSS IGTKSFQDLP PGVHPAKEGE PARSEVVPIV LSCITEISHI
     RIMLPKDITS PSSRNDVMKS VGEVKRRFPD GVPLLDPIEN MQIKDESFKK LLRKIEVLES
     RLLSNPLHNS PRLTELYEQY AEKVDLTVKI KAIKKQIAEA MSILQLDELK CRKRVLRRFG
     FINEAEVVQL KARVACEIST GDELMLSELL FNGFFNNLTA EQIASVMSCF VFEEKVKEAP
     ALAKDELAKP LKDIQSQARI IAKVSQESKM AVNEDEYVQS FHWELMEVIY EWTQGKSFAD
     ICKMTDVYEG SLIRVFRRLE ECLRQMAQAA KVMGSEDLES KFEEALGKVR RDIVAAQSLY
     L
//
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