ID M3B3S4_PSEFD Unreviewed; 1085 AA.
AC M3B3S4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=ATP-dependent RNA helicase DOB1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=MYCFIDRAFT_202861 {ECO:0000313|EMBL:EME84027.1};
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855 {ECO:0000313|EMBL:EME84027.1, ECO:0000313|Proteomes:UP000016932};
RN [1] {ECO:0000313|EMBL:EME84027.1, ECO:0000313|Proteomes:UP000016932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86 {ECO:0000313|EMBL:EME84027.1,
RC ECO:0000313|Proteomes:UP000016932};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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DR EMBL; KB446557; EME84027.1; -; Genomic_DNA.
DR RefSeq; XP_007924651.1; XM_007926460.1.
DR AlphaFoldDB; M3B3S4; -.
DR STRING; 383855.M3B3S4; -.
DR GeneID; 19336080; -.
DR KEGG; pfj:MYCFIDRAFT_202861; -.
DR eggNOG; KOG0948; Eukaryota.
DR HOGENOM; CLU_002902_0_1_1; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000016932; 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};
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:UP000016932}.
FT DOMAIN 169..325
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 406..610
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1085 AA; 122677 MW; A037F775291F3690 CRC64;
MEDDLFDVFD EKPQANGGAK HKKSRKRSLN GDIKNGSADV AMSDAAAIGH DHTETKDPAS
GNGAGAGAGA DTATPSSDDQ RGQKRQRREN EPEPIVADTF ETEQSREVAA AAGLQAQKED
QAVVLQHQVR HQVSLPPDYE YVPISQHKRP EEPARVWPFQ LDPFQEVSIA SIERNESVLV
SAHTSAGKTV VAEYAIAQCL KNNQRIIYTS PIKALSNQKY REFQAEFGDV GLMTGDVTIN
PTATCLVMTT EILRSMLYRG SEIMREVAWV VFDEVHYMRD KSRGVVWEET IILLPDKVRY
VFLSATIPNA MQFAEWITKT HNQPCHVVYT DFRPTPLQHY FFPAGAEGIH LVVDEKGVFR
EENFNKAMAA IAEKAGDDGS DPMAKRKGRG KDKKTNKGGK KEGPTDIYKI VKMIMMKNYN
PVIVFSFSKR ECETYALQMS QLAFNDDSEK QMVQKVFDSA IEMLSEEDKQ LPQILHLLPL
LRRGIGIHHS GLLPILKETI EILFQEGLIK VLFATETFSI GLNMPAKTVV FTSVRKFDGV
TQRWVTPSEF IQMSGRAGRR GLDERGIVIM MIDEKMDPTV AKEIVRGEQD KLNSAFHLGY
NMVLNLIRVE GISPEFMLER CFFQFQNAAS VSGLEKQLME LEQKRADMII EDEAEIKEYY
DLRQSLTNYA NDMKKVINHP QYLTRFLQSG RLVKIKYKDH DFGWGAVVNF TNVRPGRNQT
AEDIPSSQRV VVDVIMNVAA DVTPPDRSQL KDDLPPGVRP PAPGEKSKME VVPVMNGTID
SVGHLRVFMP NDLRAQEQRN TVRKALEEIS RRFPDGVAIL DPIENMGIND DGFKKLLRKI
EVLEHKLLSH PLHKSERLPE LYDKYAAKVE LGTEIKNLRK KMTDALSVLQ LDELKNRKRV
LRRLGFVNEA DVVQIKARVA CEISTGDELV ISELLFNGFF NDLTPEQCAA VLSCFIFEEK
SDDAPQLKEE LGKAFREVQA AARQVAKVSM ECKVLVNEEE YLQSFKPQLM EVVYAWCHGE
TFAKICTMTD VYEGSLIRLF RRLEELLRQT AEAAKVMGSE ELKEKFEQSL TKVRRDIVAA
QSLYL
//