ID A0A2K3QND2_9HYPO Unreviewed; 1151 AA.
AC A0A2K3QND2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=TCAP_01052 {ECO:0000313|EMBL:PNY29034.1};
OS Tolypocladium capitatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY29034.1, ECO:0000313|Proteomes:UP000236621};
RN [1] {ECO:0000313|EMBL:PNY29034.1, ECO:0000313|Proteomes:UP000236621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY29034.1,
RC ECO:0000313|Proteomes:UP000236621};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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:PNY29034.1}.
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DR EMBL; NRSZ01000166; PNY29034.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3QND2; -.
DR STRING; 45235.A0A2K3QND2; -.
DR OrthoDB; 161833at2759; -.
DR Proteomes; UP000236621; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17913; DEXQc_Suv3; 1.
DR CDD; cd14498; DSP; 1.
DR CDD; cd18805; SF2_C_suv3; 1.
DR Gene3D; 1.20.272.40; -; 1.
DR Gene3D; 1.20.58.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR022192; SUV3_C.
DR InterPro; IPR041082; Suv3_C_1.
DR InterPro; IPR044774; Suv3_DEXQc.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF1; ATP-DEPENDENT RNA HELICASE SUPV3L1, MITOCHONDRIAL; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF12513; SUV3_C; 1.
DR Pfam; PF18147; Suv3_C_1; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:PNY29034.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000236621};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 377..539
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 20..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1151 AA; 128096 MW; BC67969FD15284AE CRC64;
MRHLARAVAW RVSPQPARIS RRVLSTTTTL QANRGPPRKQ GQHSNKPVPH KGPASPRDES
KTAAKIAARS RADSVSQGHD PKSRLRLDFT KKYTGRHGVF RSTVLHRLQV VLTQLASSQF
SAAGIGEDEL NRQAALFMNA LDHAFSLAEQ NVTRRDKNPL FWNLRDAFIM KDIKGLTKEI
QYSFQSFVVR QRFSRELEDS QKRLLDFRFP HEWFPATRTM QRTIHVHVGP TNSGKTYNAL
KALENSTCGV YAGPLRLLAT EVYQRLKAKG RPCALITGEE VRMPEDADLY FSSCTVEMVP
LNTRFDVAVI DEIQMIADPE RGNAWTTALL GVQAKEVHLC GEDRAVALIQ ALCASIGDKC
VVHHYDRLSP LRTMDTAIEG DYNNLQKGDA IVAFSRLSLH VLKRNVETQT GRRCAIIYGS
LPPEVRVQQA ALFNDPDNDY DFIVASDAIG MGLNLEIRRV ILESVTKFDG NQSRLLTYPE
IKQIGGRAGR YRTAQSAVRE GSASAEEAEL EKVGYVTTMD HADLRNVHRA FQKKVDDIEA
ACIQPPAGIV ERFASYFPPD TPLSFILMRI KAAATVGPRY RLNIGNDILE IADIIQDLPL
TIHDRLTFCY LPVALRAEGA VDVLRALARV VAENSAGDLL SIKEIPLEFL DLNLEDYAGG
AQEYLYKLES LHVAINQYVW LSYRYAGMFR SQALAFHVRS LVEEKLIQTL ERLDFTEEQL
ENKRKNKRLQ AQSRKMSKMS MEQIGEGEGA VEDLEQEHDD ALIADGLRLS VPRERAERAE
GLRADGAEDR TPQHVDWLII ITTDDDEALG SSLSAAMHPS AAASHKPERS TPVSGDTVRA
APYTYRAPSP PFIHVPIPQR RAGSDMDLMP SFEHVDPTQL TSTDLAVITR HTTQVARDSA
ISWTYEQRRE AQPILDFLYL GPTSVIRDHG FLTAHGITMI LVARDTRMAG SKIISLETAS
TTLGLAAHVL DIDGTQGMVR TFPVAVRLIN DHLLAVYRAQ ALEGSQLGHP LSGSAAGFRR
AKVLVVCESG NDRSAGIVAA YIMAMFGKKM VPTIQFISVQ RFCCSFDEEM KRILQTWEDI
LKARHAVAQH TLAAGQPQNG ATAQSGATAG AGVREKRRVD EMMDIDQDGA TDLDRFTDRD
AFVPFKDKTP H
//
