ID M3BRA0_SPHMS Unreviewed; 1084 AA.
AC M3BRA0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=ATP-dependent RNA helicase DOB1 {ECO:0000313|EMBL:EMF08648.1};
GN ORFNames=SEPMUDRAFT_152259 {ECO:0000313|EMBL:EMF08648.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF08648.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF08648.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF08648.1,
RC ECO:0000313|Proteomes:UP000016931};
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; KB456271; EMF08648.1; -; Genomic_DNA.
DR RefSeq; XP_016756769.1; XM_016907335.1.
DR AlphaFoldDB; M3BRA0; -.
DR STRING; 692275.M3BRA0; -.
DR GeneID; 27904472; -.
DR eggNOG; KOG0948; Eukaryota.
DR HOGENOM; CLU_002902_0_1_1; -.
DR OMA; IMLKNYN; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000016931; 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:EMF08648.1};
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:UP000016931}.
FT DOMAIN 167..323
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 436..608
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1084 AA; 122272 MW; 9A0FC5850460226F CRC64;
MDDDLFNVFD DKPQPANSNK TNLKRSLNGN VKQNGGDSVM ADAPVETKDF ANTVAAKGGD
KKGNGDDEAN GEQEEGQRGQ KRQRMEDAPD AVVTDEFETE QQREVAASAG LQAQQDGSAA
VTLKHQVRHQ VSLPPDCDYV PISQHKRPEH PAKVFPFTLD PFQEVSVASI ERNESVLVSA
HTSAGKTVVA EYAIAQCLKN NQRVIYTSPI KALSNQKYRE FNAEFGDCGL MTGDVTINPT
ATCLVMTTEI LRSMLYRGSE IMREVAWVVF DEVHYMRDRA RGVVWEETII LLPDKVRYVF
LSATIPNAMQ FAEWITKIHN QPCHVVYTDF RPTPLQHYFF PASADGIHLI VDEKGVFREE
NFNKAMAAIA DKAGDDGSDP LAKRKGRGKD KKTNKGGKKD GPTDIYKIVK MIMLKNYNPV
IVFSFSKRDC ENYALQMSQL AFNDESEKAM VSKVFDSAIE MLSDEDKQLP QIQHILPLLR
RGIGIHHSGL LPILKETIEI LFQEGLIKVL FATETFSIGL NMPAKTVVFT AVRKFDGREL
RWVTPSEFIQ MSGRAGRRGL DERGIVIMMI DEKMDPPVAK EIVKGEQDKL NSAFYLGYNM
ILNLMRVEGI SPEFMLERCF FQFQNAASVS SIEKQLMELE QKRADAVIED EAQIKEYYDL
RQSLETYSSD MKKVISHPQY LCKFMQSGRL VKVKHNGQDF GWGVVVNFMK VKPARGQSED
DMNIGHSVVI DVLLNIAADS SAPGTSSQLR DDMPKEVRPC EPGEKGKMEV VPVMNGTIDA
VGHIRVFLPN DLRTSEQRNT VRKSLEEVAR RFPDGVAVLD PIENMGIDDD SFKKLLRKIE
VLEHKLLNNP LHTSDKLPDL YDRYAAKIEI TNEIKATRKK MTDALSVLQL DELKNRKRVL
RRLGFVNEAD VVQLKARVAC EISTGDELVL SELLFNRFFN ELTPEQCAAT LSVFIFEEKS
DEAPALKEDL AKAFREIQAQ ARQIAKVSME CKVLVNEEEY IQGFKHQLMD VVFSWCNGAS
FAEICKMTDV YEGSLIRLFR RLEELLRQMA QASKVMGSED LEKKFEGALG KVRRDIVAAQ
SLYL
//
