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Database: UniProt
Entry: A0A139IU57_9PEZI
LinkDB: A0A139IU57_9PEZI
Original site: A0A139IU57_9PEZI 
ID   A0A139IU57_9PEZI        Unreviewed;      1080 AA.
AC   A0A139IU57;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=ATP-dependent RNA helicase DOB1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AC579_2915 {ECO:0000313|EMBL:KXT18301.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT18301.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT18301.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT18301.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXT18301.1}.
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DR   EMBL; LFZO01000009; KXT18301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139IU57; -.
DR   STRING; 113226.A0A139IU57; -.
DR   Proteomes; UP000073492; 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:UP000073492}.
FT   DOMAIN          164..320
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          401..605
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1080 AA;  122490 MW;  77774A6BE80CA8AE CRC64;
     MEDDLFDVFD EKPQANKGGA KHKKSKKRSL NGDIKKGSAD VAMSDAAALG HDQTETKDFA
     NASGADTATP SSDGQRGQKR QRRQNEPEPI VTDTFETEQL RSVAAAAGLQ AQKEDQAVVL
     QHQVRHQVSL PPDYEYVPIS QHKRPEEPAR VWPFKLDPFQ EVSIASIERD ESVLVSAHTS
     AGKTVVAEYA IAQCLKNNQR IIYTSPIKAL SNQKYREFHA EFGDVGLMTG DVTINPTATC
     LVMTTEILRS MLYRGSEIMR EVAWVVFDEV HYMRDKSRGV VWEETIILLP DKVRYVFLSA
     TIPNAMQFAE WITKTHNQPC HVVYTDFRPT PLQHYFFPAG AEGIHLVVDE KGVFREENFN
     KAMAAIADKA GDDGSDPMAK RKGRGKDKKT NKGGKKEGPT DIYKIVKMIM IKNYNPVIVF
     SFSKRECETY ALQMSQLAFN DDSEKQMVQK VFDSAIEMLS EEDKQLPQIL HLLPLLRRGI
     GIHHSGLLPI LKETIEILFQ EGLIKVLFAT ETFSIGLNMP AKTVVFTSVR KFDGVSLRWV
     TPSEFIQMSG RAGRRGLDER GIVIMMIDEK MDPTVAKEIV RGEQDKLNSA FHLGYNMVLN
     LIRVEGISPE FMLERCFFQF QNAASVSGLE KQLMELEQKR AEMIIEDEAE IKEYYDLRQS
     LRNYANDMKK VINHPQYLTR FLQSGRLVKI KYKDYDFGWG AVVNFTNVRP GRNQTAEDIP
     SSQRVVVDVI MNVAADVNPP DRSQLKDDLP PGVRPPAPGE KSKMEVVPVM NGTIDSVGHL
     RVFMPNDLRA QEQRNTVRKA LEEISRRFPD GVAILDPIEN MGINDDGFKK LLRKIEVLEH
     KLLSHPLHKS ERLPELYDKY AAKVELGTEI KNLRKKMTDA LSVLQLDELK NRKRVLRRLG
     FISEADVVQI KARVACEIST GDELVISELL FNGFFNDLSP EQCAAVLSCF IFEEKSDDAP
     QLKEQLGKAY REVQAAARQV AKVSMECKVL VNEEEYLQSF KPQLMEVVYA WCHGETFAKI
     CKMTDVYEGS LIRLFRRLEE LLRQTAEAAK VMGSEELKEK FEQSLTKVRR DIVAAQSLYL
//
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