ID M3BY99_SPHMS Unreviewed; 1082 AA.
AC M3BY99;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-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=SEPMUDRAFT_117582 {ECO:0000313|EMBL:EMF13046.1};
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:EMF13046.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF13046.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF13046.1,
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB456264; EMF13046.1; -; Genomic_DNA.
DR RefSeq; XP_016761167.1; XM_016901349.1.
DR AlphaFoldDB; M3BY99; -.
DR STRING; 692275.M3BY99; -.
DR GeneID; 27898486; -.
DR eggNOG; KOG0923; Eukaryota.
DR HOGENOM; CLU_001832_7_0_1; -.
DR OMA; HITLMNV; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000016931; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; IPR011709; DEAD-box_helicase_OB_fold.
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:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 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 Pfam; PF07717; OB_NTP_bind; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EMF13046.1};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931}.
FT DOMAIN 453..617
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 642..816
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 61..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1082 AA; 123568 MW; 9183E2EB2ED23D34 CRC64;
MDLRTYVSDH LLKLVGASED MIVDFVVSEA KRAKSPSQLL DKLSSMLDST DDDLRRFSEG
LYAQVAKPSS NGAASDGKGQ KSAKPGMAKK KYALVDMEVE EEAPRPSATK TERKREDNGE
RKSRHRSDRD RRRSHSGERR KKLRRRDGDF DDRWGDEEEE DEEDFPSPPA KRTRFDNGST
SPKEDEPEKE DEEDEEDEEE RDRRERKAFE ERLKQKEKDS TKKLTEDRSS KRDAADAERR
AQAGKLTAQE MKDLRLRSRQ DYLKKRSAQE LALLRRQVAE EEEEERNNPT LTQQEKDEFA
RNREALRLAE EREGIDDHID GYALPDDYIT EKGKLDTKRK EKALYSRYVE RDDQGREKYV
TEHEEWEREQ LAKTKAQIIV PDHQDEGDYE YVFDEEQQLR WVTDAVLKGG MSDMKSPQEK
LLAQQMLAAE RKAKTMEEKR KTLPVYQYRQ QFLDAVKEYQ ILIIVGETGS GKTTQLPQFL
YEDGYCKDGM KVGCTQPRRV AAMSVAARVA EEVGVKLGNE VGYAIRFEDN TTDKTALKYM
TDGMLLREFL TEPDLGGYSA LMIDEAHERT LHTDILFGLV KDIARGRPDL KLLISSATLD
AQKFSEFFDD APILNIPGRT YDVEMNYSLQ PEANYLSAAI TTVFQIHLSQ PMPGDILVFL
TGQDEIEQAE QSLQETARKL GSAAPELLIC PIYANLPTDL QQKIFDPTPP KVRKVVLATN
IAETSLTIDG IVYVIDPGYV KENRYTPATN MESLVSVPIS RASANQRAGR AGRNQPGKCF
RLYTKWAYYN DLPESTTPEI QRTNLNSIVL LLKSLGINDL INFDFMDPPA PDMLIRSLEQ
LYALGALNDK GELTKVGRQM AEFPTDPMLA KAVLQADKEG CVEEVLSIIA MLGEASALFY
RPKDKKLQAD AARARFTSKE GGDHISYLNI WNQWVDADFS YVWAKENFLQ QRSLTRARDV
RDQLAKLCDR VEVTLSSCGT SNLPPIQRAI TAGFFPNAAR LQRSGDSYRT VKNNLTVHIH
PSSVLMDVRP KWVIFYELVL TSKEFMRSVM PLQPEWLMEV APHYYKPKDV ESLGVDRKMP
KI
//
