ID A0A423WB65_9PEZI Unreviewed; 1089 AA.
AC A0A423WB65;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=ATP-dependent RNA helicase mtr4 {ECO:0008006|Google:ProtNLM};
GN ORFNames=VSDG_03301 {ECO:0000313|EMBL:ROW00498.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROW00498.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROW00498.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROW00498.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-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:ROW00498.1}.
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DR EMBL; LJZO01000008; ROW00498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423WB65; -.
DR STRING; 252740.A0A423WB65; -.
DR Proteomes; UP000284375; 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:UP000284375}.
FT DOMAIN 168..324
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..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1089 AA; 122806 MW; CD6227779ABE1BEA CRC64;
MDELFDVFDA PAGAAAPREA EPTQVTPKKE TKEKTDKSKK RKADGHMKNG TDADVDMADG
DEPSGDDEGS EQNAETPQDS KRRKKQNEAD PVMADTFTTA ESRQVAAAAG FAATKGDEAL
TLAHNIQHQV ALPPDLDTEY VPLSQHKPPK EPARTYSFKL DPFQSLSVAS IERDESVLVS
AHTSAGKTVV AEYAIAQCLK NKQRVIYTSP IKALSNQKYR DFQAEFGDVG LMTGDVTINP
TASCLVMTTE ILRSMLYRGS EIMREVAWVV FDEIHYLRDK SRGVVWEETI ILLPDKVRYV
FLSATIPNAF QFAEWIAKIH RQACHVVYTD FRPTPLQNYF FPAGGEGIFL IVDEKGNFKE
HNFNTAMTLI ENKKGADPSD PTAARKGTGK NKKTNKGGKA ADSQSDISKI VKMIMKKMFH
PVIIFNFSKR DCEAMALAIS HMTFNNASEK QLVREVFTSA INQLSEEDRT LPQITHILPL
LEKGIGVHHS GLLPILKESI EILFQEGLIK ALFATETFSI GLNMPARTVV FTSVMKFDGT
RQRPLTTGEY IQMSGRAGRR GLDDRGIVIM MVDDKLEPDT AKNIVSGPQD KLNSAFYLGY
NMVLNLQRIE TISPEFMLER CFYQFQNAAS VPGLEKDLIA LQQERDNMVI PDENTVKEYY
NLRNQIEDYT KDMVSVIQHP NYCTEFLQPG RLVQIKTPSG EDFDWGVIIN FIPRRSPKVG
EPPHAPQESI FIDVLLRLDG DSDNVKRIQP TSGVMPPGIR PFVESKSKFC RYEVVPVLLN
CVKAFGQLRL FVKGDLRSEQ EMGHCGKNLE EAKRRFPDGI PILDPIENMG ITDESFKKLM
RKIEVLESRL LSNPLHGSPL LPELWDQYSK KVALADQIKE KKKAIAKAHT IAQLDELKSR
KRVLRRLGFI NDAEVVQMKA RVACEISSTE GHELVLSELL FNRFFNELSP ELCAAVLSVF
IFDEKVETQE LKEELAKPYR EIQRQARVIA KVSQESKLDV NEEEYVQSLK WQLMETVYAW
AQGRPFAEIC KMTNAYEGSL IRLFRRLEEL LRQMAEAGKV MGSEELSKKF TESLGKVKRD
IVAAQSLYL
//
